ID   AMPN_HUMAN              Reviewed;         967 AA.
AC   P15144; Q16728; Q6GT90; Q8IUK3; Q8IVH3; Q9UCE0;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 4.
DT   12-AUG-2020, entry version 226.
DE   RecName: Full=Aminopeptidase N {ECO:0000305};
DE            Short=AP-N;
DE            Short=hAPN;
DE            EC=3.4.11.2 {ECO:0000269|PubMed:22932899, ECO:0000269|PubMed:6149934, ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8887485};
DE   AltName: Full=Alanyl aminopeptidase;
DE   AltName: Full=Aminopeptidase M;
DE            Short=AP-M;
DE   AltName: Full=Microsomal aminopeptidase;
DE   AltName: Full=Myeloid plasma membrane glycoprotein CD13;
DE   AltName: Full=gp150;
DE   AltName: CD_antigen=CD13;
GN   Name=ANPEP; Synonyms=APN, CD13, PEPN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLN-86 AND MET-603.
RC   TISSUE=Intestine;
RX   PubMed=2901990; DOI=10.1016/0014-5793(88)80502-7;
RA   Olsen J., Cowell G.M., Koenigshoefer E., Danielsen E.M., Moeller J.,
RA   Laustsen L., Hansen O.C., Welinder K.G., Engberg J., Hunziker W.,
RA   Spiess M., Sjoestroem H., Noren O.;
RT   "Complete amino acid sequence of human intestinal aminopeptidase N as
RT   deduced from cloned cDNA.";
RL   FEBS Lett. 238:307-314(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-21, VARIANT GLN-86, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=2564851; DOI=10.1172/jci114015;
RA   Look A.T., Ashmun R.A., Shapiro L.H., Peiper S.C.;
RT   "Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to
RT   aminopeptidase N.";
RL   J. Clin. Invest. 83:1299-1307(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RC   TISSUE=Intestinal epithelium;
RX   PubMed=1675638;
RA   Shapiro L.H., Ashmun R.A., Roberts W.M., Look A.T.;
RT   "Separate promoters control transcription of the human aminopeptidase N
RT   gene in myeloid and intestinal epithelial cells.";
RL   J. Biol. Chem. 266:11999-12007(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-479 AND 524-967, AND VARIANT GLN-86.
RC   TISSUE=Peripheral blood;
RA   Eiz-Vesper B., Fuchs N., Gottschalk D., Mueller K., Reuter S., Blasczyk R.;
RT   "Genomic organisation of aminopeptidase N.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PROTEIN SEQUENCE OF 2-20 AND 70-81, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=7576235; DOI=10.1515/bchm3.1995.376.7.397;
RA   Watanabe Y., Iwaki-Egawa S., Mizukoshi H., Fujimoto Y.;
RT   "Identification of an alanine aminopeptidase in human maternal serum as a
RT   membrane-bound aminopeptidase N.";
RL   Biol. Chem. Hoppe-Seyler 376:397-400(1995).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-18, AND FUNCTION.
RX   PubMed=8102610; DOI=10.1016/0014-5793(93)80199-5;
RA   Nunez L., Amigo L., Rigotti A., Puglielli L., Mingrone G., Greco A.V.,
RA   Nervi F.;
RT   "Cholesterol crystallization-promoting activity of aminopeptidase-N
RT   isolated from the vesicular carrier of biliary lipids.";
RL   FEBS Lett. 329:84-88(1993).
RN   [9]
RP   CATALYTIC ACTIVITY, CHARACTERIZATION, AND SUBUNIT.
RX   PubMed=6149934; DOI=10.1159/000469453;
RA   Tokioka-Terao M., Hiwada K., Kokubu T.;
RT   "Purification and characterization of aminopeptidase N from human plasma.";
RL   Enzyme 32:65-75(1984).
RN   [10]
RP   GLYCOSYLATION.
RX   PubMed=1705556;
RA   O'Connell P.J., Gerkis V., d'Apice A.J.F.;
RT   "Variable O-glycosylation of CD13 (aminopeptidase N).";
RL   J. Biol. Chem. 266:4593-4597(1991).
RN   [11]
RP   FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HCOV-229E SPIKE
RP   GLYCOPROTEIN (MICROBIAL INFECTION), AND TOPOLOGY.
RX   PubMed=1350662; DOI=10.1038/357420a0;
RA   Yeager C.L., Ashmun R.A., Williams R.K., Cardellichio C.B., Shapiro L.H.,
RA   Look A.T., Holmes K.V.;
RT   "Human aminopeptidase N is a receptor for human coronavirus 229E.";
RL   Nature 357:420-422(1992).
RN   [12]
RP   IDENTIFICATION OF SOLUBLE FORM, AND TISSUE SPECIFICITY.
RX   PubMed=7902291;
RA   Favaloro E.J., Browning T., Facey D.;
RT   "CD13 (GP150; aminopeptidase-N): predominant functional activity in blood
RT   is localized to plasma and is not cell-surface associated.";
RL   Exp. Hematol. 21:1695-1701(1993).
RN   [13]
RP   FUNCTION (MICROBIAL INFECTION).
RX   PubMed=8105105;
RA   Soderberg C., Giugni T.D., Zaia J.A., Larsson S., Wahlberg J.M., Moller E.;
RT   "CD13 (human aminopeptidase N) mediates human cytomegalovirus infection.";
RL   J. Virol. 67:6576-6585(1993).
RN   [14]
RP   CATALYTIC ACTIVITY, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH
RP   HCOV-229E SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), REGION, AND MUTAGENESIS
RP   OF HIS-392.
RX   PubMed=8887485; DOI=10.1099/0022-1317-77-10-2515;
RA   Kolb A.F., Maile J., Heister A., Siddell S.G.;
RT   "Characterization of functional domains in the human coronavirus HCV 229E
RT   receptor.";
RL   J. Gen. Virol. 77:2515-2521(1996).
RN   [15]
RP   FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=9056417; DOI=10.1006/excr.1996.3455;
RA   Noren K., Hansen G.H., Clausen H., Noren O., Sjostrom H., Vogel L.K.;
RT   "Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13)
RT   is normally expressed at the cell surface and has full enzymatic
RT   activity.";
RL   Exp. Cell Res. 231:112-118(1997).
RN   [16]
RP   FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HCOV-229E SPIKE
RP   GLYCOPROTEIN (MICROBIAL INFECTION), AND REGION.
RX   PubMed=9367365; DOI=10.1099/0022-1317-78-11-2795;
RA   Kolb A.F., Hegyi A., Siddell S.G.;
RT   "Identification of residues critical for the human coronavirus 229E
RT   receptor function of human aminopeptidase N.";
RL   J. Gen. Virol. 78:2795-2802(1997).
RN   [17]
RP   FUNCTION, AND ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC.
RX   PubMed=10605003; DOI=10.4049/jimmunol.164.1.129;
RA   Dong X., An B., Salvucci Kierstead L., Storkus W.J., Amoscato A.A.,
RA   Salter R.D.;
RT   "Modification of the amino terminus of a class II epitope confers
RT   resistance to degradation by CD13 on dendritic cells and enhances
RT   presentation to T cells.";
RL   J. Immunol. 164:129-135(2000).
RN   [18]
RP   ROLE IN ANGIOGENESIS, AND CHARACTERIZATION OF RECEPTOR FOR TUMOR-HOMING
RP   PEPTIDES FUNCTION.
RX   PubMed=10676659;
RA   Pasqualini R., Koivunen E., Kain R., Lahdenranta J., Sakamoto M.,
RA   Stryhn A., Ashmun R.A., Shapiro L.H., Arap W., Ruoslahti E.;
RT   "Aminopeptidase N is a receptor for tumor-homing peptides and a target for
RT   inhibiting angiogenesis.";
RL   Cancer Res. 60:722-727(2000).
RN   [19]
RP   FUNCTION, AND INDUCTION BY ESTRADIOL AND IL8.
RX   PubMed=11384645; DOI=10.1016/s0015-0282(01)01779-4;
RA   Seli E., Senturk L.M., Bahtiyar O.M., Kayisli U.A., Arici A.;
RT   "Expression of aminopeptidase N in human endometrium and regulation of its
RT   activity by estrogen.";
RL   Fertil. Steril. 75:1172-1176(2001).
RN   [20]
RP   MUTAGENESIS OF 288-ASP--SER-295 AND ASN-818.
RX   PubMed=11559807; DOI=10.1128/jvi.75.20.9741-9752.2001;
RA   Wentworth D.E., Holmes K.V.;
RT   "Molecular determinants of species specificity in the coronavirus receptor
RT   aminopeptidase N (CD13): influence of N-linked glycosylation.";
RL   J. Virol. 75:9741-9752(2001).
RN   [21]
RP   FUNCTION OF SOLUBLE FORM.
RX   PubMed=12473585;
RA   van Hensbergen Y., Broxterman H.J., Hanemaaijer R., Jorna A.S.,
RA   van Lent N.A., Verheul H.M., Pinedo H.M., Hoekman K.;
RT   "Soluble aminopeptidase N/CD13 in malignant and nonmalignant effusions and
RT   intratumoral fluid.";
RL   Clin. Cancer Res. 8:3747-3754(2002).
RN   [22]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HCOV-229E SPIKE
RP   GLYCOPROTEIN.
RX   PubMed=12551991; DOI=10.1128/jvi.77.4.2530-2538.2003;
RA   Bonavia A., Zelus B.D., Wentworth D.E., Talbot P.J., Holmes K.V.;
RT   "Identification of a receptor-binding domain of the spike glycoprotein of
RT   human coronavirus HCoV-229E.";
RL   J. Virol. 77:2530-2538(2003).
RN   [23]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265.
RC   TISSUE=Bile;
RX   PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA   Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA   Argani P., Goggins M.G., Maitra A., Pandey A.;
RT   "A proteomic analysis of human bile.";
RL   Mol. Cell. Proteomics 3:715-728(2004).
RN   [24]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-234; ASN-265; ASN-681
RP   AND ASN-818.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [25]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-234; ASN-265; ASN-573;
RP   ASN-681 AND ASN-818.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [26]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 66-967 IN COMPLEX WITH
RP   ANGIOTENSIN-4 AND INHIBITORS, CATALYTIC ACTIVITY, COFACTOR,
RP   SUBSTRATE-BINDING REGION, ZINC-BINDING SITES, ACTIVE SITE, GLYCOSYLATION AT
RP   ASN-128; ASN-234; ASN-265; ASN-319; ASN-527; ASN-625; ASN-681 AND ASN-818,
RP   SUBUNIT, AND DISULFIDE BONDS.
RX   PubMed=22932899; DOI=10.1074/jbc.m112.398842;
RA   Wong A.H., Zhou D., Rini J.M.;
RT   "The X-ray crystal structure of human aminopeptidase N reveals a novel
RT   dimer and the basis for peptide processing.";
RL   J. Biol. Chem. 287:36804-36813(2012).
RN   [30]
RP   VARIANTS TYR-242 AND PRO-243.
RX   PubMed=9452074; DOI=10.1002/humu.1380110153;
RA   Lendeckel U., Wex T., Arndt M., Frank K., Franke A., Ansorge S.;
RT   "Identification of point mutations in the aminopeptidase N gene by SSCP
RT   analysis and sequencing.";
RL   Hum. Mutat. Suppl. 1:S158-S160(1998).
CC   -!- FUNCTION: Broad specificity aminopeptidase which plays a role in the
CC       final digestion of peptides generated from hydrolysis of proteins by
CC       gastric and pancreatic proteases. Also involved in the processing of
CC       various peptides including peptide hormones, such as angiotensin III
CC       and IV, neuropeptides, and chemokines. May also be involved the
CC       cleavage of peptides bound to major histocompatibility complex class II
CC       molecules of antigen presenting cells. May have a role in angiogenesis
CC       and promote cholesterol crystallization. May have a role in amino acid
CC       transport by acting as binding partner of amino acid transporter
CC       SLC6A19 and regulating its activity (By similarity).
CC       {ECO:0000250|UniProtKB:P97449, ECO:0000269|PubMed:10605003,
CC       ECO:0000269|PubMed:10676659, ECO:0000269|PubMed:11384645,
CC       ECO:0000269|PubMed:12473585, ECO:0000269|PubMed:7576235,
CC       ECO:0000269|PubMed:8102610, ECO:0000269|PubMed:9056417}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for human
CC       coronavirus 229E/HCoV-229E. In case of human coronavirus 229E (HCoV-
CC       229E) infection, serves as receptor for HCoV-229E spike glycoprotein.
CC       {ECO:0000269|PubMed:12551991, ECO:0000269|PubMed:1350662,
CC       ECO:0000269|PubMed:8887485, ECO:0000269|PubMed:9367365}.
CC   -!- FUNCTION: (Microbial infection) Mediates as well Human cytomegalovirus
CC       (HCMV) infection. {ECO:0000269|PubMed:8105105}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC         peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC         amino acids including Pro (slow action). When a terminal hydrophobic
CC         residue is followed by a prolyl residue, the two may be released as
CC         an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC         Evidence={ECO:0000269|PubMed:22932899, ECO:0000269|PubMed:6149934,
CC         ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8887485};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:22932899};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22932899};
CC   -!- SUBUNIT: Homodimer. Interacts with SLC6A19 (By similarity).
CC       {ECO:0000250|UniProtKB:P97449, ECO:0000269|PubMed:22932899,
CC       ECO:0000269|PubMed:6149934}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with the S1 domain of human
CC       coronavirus 229E/HCoV-229E spike protein. {ECO:0000269|PubMed:12551991,
CC       ECO:0000269|PubMed:1350662, ECO:0000269|PubMed:8887485}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2564851,
CC       ECO:0000269|PubMed:9056417}; Single-pass type II membrane protein
CC       {ECO:0000305|PubMed:1350662}. Note=Also found as a soluble form.
CC       {ECO:0000269|PubMed:7902291}.
CC   -!- TISSUE SPECIFICITY: Expressed in epithelial cells of the kidney,
CC       intestine, and respiratory tract; granulocytes, monocytes, fibroblasts,
CC       endothelial cells, cerebral pericytes at the blood-brain barrier,
CC       synaptic membranes of cells in the CNS. Also expressed in endometrial
CC       stromal cells, but not in the endometrial glandular cells. Found in the
CC       vasculature of tissues that undergo angiogenesis and in malignant
CC       gliomas and lymph node metastases from multiple tumor types but not in
CC       blood vessels of normal tissues. A soluble form has been found in
CC       plasma. It is found to be elevated in plasma and effusions of cancer
CC       patients. {ECO:0000269|PubMed:7902291}.
CC   -!- INDUCTION: Estradiol and IL8/interleukin-8 decrease enzymatic activity
CC       in vitro in endometrial stromal cells by 40% and 30%, respectively.
CC       {ECO:0000269|PubMed:11384645}.
CC   -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.
CC   -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:15084671,
CC       ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:1705556,
CC       ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899,
CC       ECO:0000269|PubMed:9056417}.
CC   -!- PTM: May undergo proteolysis and give rise to a soluble form.
CC       {ECO:0000269|PubMed:7902291}.
CC   -!- MISCELLANEOUS: Found to serve as a receptor for tumor-homing peptides,
CC       more specifically NGR peptides. It could serve thus as a target for
CC       delivering drugs into tumors. Concentration in human hepatic bile,
CC       varies from 17.3 to 57.6 micrograms/ml. {ECO:0000269|PubMed:10676659}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
DR   EMBL; X13276; CAA31640.1; -; mRNA.
DR   EMBL; M22324; AAA51719.1; -; mRNA.
DR   EMBL; AC018988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC079075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC058928; AAH58928.1; -; mRNA.
DR   EMBL; M55522; AAA83399.1; -; Genomic_DNA.
DR   EMBL; AJ421875; CAD19098.2; -; Genomic_DNA.
DR   EMBL; AJ421876; CAD19098.2; JOINED; Genomic_DNA.
DR   EMBL; AJ426050; CAD19802.1; -; Genomic_DNA.
DR   EMBL; AJ427985; CAD20931.1; -; Genomic_DNA.
DR   EMBL; AJ427986; CAD20931.1; JOINED; Genomic_DNA.
DR   EMBL; AJ427987; CAD20931.1; JOINED; Genomic_DNA.
DR   EMBL; AJ427988; CAD20931.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS10356.1; -.
DR   PIR; A30325; A30325.
DR   RefSeq; NP_001141.2; NM_001150.2.
DR   RefSeq; XP_005254949.1; XM_005254892.4.
DR   RefSeq; XP_011519775.1; XM_011521473.1.
DR   PDB; 4FYQ; X-ray; 1.90 A; A=66-967.
DR   PDB; 4FYR; X-ray; 1.91 A; A=66-967.
DR   PDB; 4FYS; X-ray; 2.01 A; A=66-967.
DR   PDB; 4FYT; X-ray; 1.85 A; A=66-967.
DR   PDB; 5LHD; X-ray; 2.60 A; A/B/C/D=36-967.
DR   PDB; 6ATK; X-ray; 3.50 A; A/B/C=66-967.
DR   PDB; 6U7E; X-ray; 3.00 A; A/B=66-967.
DR   PDB; 6U7F; X-ray; 2.75 A; A/B=66-967.
DR   PDB; 6U7G; X-ray; 2.35 A; A/B=66-967.
DR   PDBsum; 4FYQ; -.
DR   PDBsum; 4FYR; -.
DR   PDBsum; 4FYS; -.
DR   PDBsum; 4FYT; -.
DR   PDBsum; 5LHD; -.
DR   PDBsum; 6ATK; -.
DR   PDBsum; 6U7E; -.
DR   PDBsum; 6U7F; -.
DR   PDBsum; 6U7G; -.
DR   SMR; P15144; -.
DR   BioGRID; 106787; 6.
DR   IntAct; P15144; 11.
DR   MINT; P15144; -.
DR   STRING; 9606.ENSP00000300060; -.
DR   BindingDB; P15144; -.
DR   ChEMBL; CHEMBL1907; -.
DR   DrugBank; DB00973; Ezetimibe.
DR   DrugBank; DB06773; Human calcitonin.
DR   DrugBank; DB06196; Icatibant.
DR   DrugCentral; P15144; -.
DR   GuidetoPHARMACOLOGY; 1560; -.
DR   MEROPS; M01.001; -.
DR   GlyConnect; 815; 35 N-Linked glycans (6 sites).
DR   GlyGen; P15144; 17 sites, 9 N-linked glycans (5 sites), 7 O-linked glycans (4 sites).
DR   iPTMnet; P15144; -.
DR   MetOSite; P15144; -.
DR   PhosphoSitePlus; P15144; -.
DR   SwissPalm; P15144; -.
DR   UniCarbKB; P15144; -.
DR   BioMuta; ANPEP; -.
DR   DMDM; 143811362; -.
DR   CPTAC; CPTAC-460; -.
DR   CPTAC; CPTAC-461; -.
DR   EPD; P15144; -.
DR   jPOST; P15144; -.
DR   MassIVE; P15144; -.
DR   MaxQB; P15144; -.
DR   PaxDb; P15144; -.
DR   PeptideAtlas; P15144; -.
DR   PRIDE; P15144; -.
DR   ProteomicsDB; 53109; -.
DR   Antibodypedia; 3713; 1871 antibodies.
DR   DNASU; 290; -.
DR   Ensembl; ENST00000300060; ENSP00000300060; ENSG00000166825.
DR   GeneID; 290; -.
DR   KEGG; hsa:290; -.
DR   UCSC; uc002bop.5; human.
DR   CTD; 290; -.
DR   DisGeNET; 290; -.
DR   EuPathDB; HostDB:ENSG00000166825.13; -.
DR   GeneCards; ANPEP; -.
DR   HGNC; HGNC:500; ANPEP.
DR   HPA; ENSG00000166825; Tissue enhanced (intestine, kidney, pancreas).
DR   MIM; 151530; gene.
DR   neXtProt; NX_P15144; -.
DR   OpenTargets; ENSG00000166825; -.
DR   PharmGKB; PA24815; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   GeneTree; ENSGT00940000154876; -.
DR   HOGENOM; CLU_003705_2_0_1; -.
DR   InParanoid; P15144; -.
DR   KO; K11140; -.
DR   OMA; TAKWFIF; -.
DR   OrthoDB; 110058at2759; -.
DR   PhylomeDB; P15144; -.
DR   TreeFam; TF300395; -.
DR   BRENDA; 3.4.11.2; 2681.
DR   PathwayCommons; P15144; -.
DR   Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SABIO-RK; P15144; -.
DR   SIGNOR; P15144; -.
DR   BioGRID-ORCS; 290; 0 hits in 872 CRISPR screens.
DR   ChiTaRS; ANPEP; human.
DR   GeneWiki; Alanine_aminopeptidase; -.
DR   GenomeRNAi; 290; -.
DR   Pharos; P15144; Tchem.
DR   PRO; PR:P15144; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P15144; protein.
DR   Bgee; ENSG00000166825; Expressed in intestine and 193 other tissues.
DR   ExpressionAtlas; P15144; baseline and differential.
DR   Genevisible; P15144; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR   GO; GO:0004177; F:aminopeptidase activity; TAS:ProtInc.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR   GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR   GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 2.60.40.1730; -; 1.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; SSF63737; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminopeptidase; Angiogenesis; Cell membrane;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW   Host-virus interaction; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Polymorphism; Protease; Receptor; Reference proteome;
KW   Signal-anchor; Sulfation; Transmembrane; Transmembrane helix; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2564851,
FT                   ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8102610"
FT   CHAIN           2..967
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000095081"
FT   TOPO_DOM        2..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:1350662"
FT   TRANSMEM        9..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..967
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:1350662"
FT   REGION          33..68
FT                   /note="Cytosolic Ser/Thr-rich junction"
FT   REGION          69..967
FT                   /note="Metalloprotease"
FT   REGION          288..295
FT                   /note="Necessary and sufficient to mediate interaction with
FT                   HCoV-229E"
FT                   /evidence="ECO:0000269|PubMed:1350662,
FT                   ECO:0000269|PubMed:8887485"
FT   REGION          352..356
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000269|PubMed:22932899"
FT   ACT_SITE        389
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT                   ECO:0000269|PubMed:22932899"
FT   METAL           388
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000244|PDB:4FYQ, ECO:0000244|PDB:4FYR,
FT                   ECO:0000244|PDB:4FYT, ECO:0000269|PubMed:22932899"
FT   METAL           392
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000244|PDB:4FYQ, ECO:0000244|PDB:4FYR,
FT                   ECO:0000244|PDB:4FYT, ECO:0000269|PubMed:22932899"
FT   METAL           411
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000244|PDB:4FYQ, ECO:0000244|PDB:4FYR,
FT                   ECO:0000244|PDB:4FYT, ECO:0000269|PubMed:22932899"
FT   SITE            477
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000269|PubMed:22932899"
FT   MOD_RES         176
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         419
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         424
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         913
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15084671,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:22932899"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22932899"
FT   CARBOHYD        527
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22932899"
FT   CARBOHYD        573
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        625
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22932899"
FT   CARBOHYD        681
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899"
FT   CARBOHYD        735
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        818
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899"
FT   DISULFID        761..768
FT                   /evidence="ECO:0000269|PubMed:22932899"
FT   DISULFID        798..834
FT                   /evidence="ECO:0000269|PubMed:22932899"
FT   VARIANT         20
FT                   /note="V -> M (in dbSNP:rs10152474)"
FT                   /id="VAR_031262"
FT   VARIANT         86
FT                   /note="R -> Q (in dbSNP:rs25653)"
FT                   /evidence="ECO:0000269|PubMed:2564851,
FT                   ECO:0000269|PubMed:2901990, ECO:0000269|Ref.6"
FT                   /id="VAR_014736"
FT   VARIANT         242
FT                   /note="D -> Y"
FT                   /evidence="ECO:0000269|PubMed:9452074"
FT                   /id="VAR_006727"
FT   VARIANT         243
FT                   /note="L -> P"
FT                   /evidence="ECO:0000269|PubMed:9452074"
FT                   /id="VAR_006728"
FT   VARIANT         311
FT                   /note="A -> V (in dbSNP:rs17240268)"
FT                   /id="VAR_031263"
FT   VARIANT         321
FT                   /note="T -> M (in dbSNP:rs8179199)"
FT                   /id="VAR_031264"
FT   VARIANT         603
FT                   /note="I -> K (in dbSNP:rs17240212)"
FT                   /id="VAR_031265"
FT   VARIANT         603
FT                   /note="I -> M (in dbSNP:rs8192297)"
FT                   /evidence="ECO:0000269|PubMed:2901990"
FT                   /id="VAR_031266"
FT   VARIANT         752
FT                   /note="S -> N (in dbSNP:rs25651)"
FT                   /id="VAR_014737"
FT   MUTAGEN         288..295
FT                   /note="DYVEKQAS->QSVEETAQ: No change in receptor activity
FT                   and HCoV-229E infection."
FT                   /evidence="ECO:0000269|PubMed:11559807"
FT   MUTAGEN         288..295
FT                   /note="DYVEKQAS->QSVNEQAQ: No change in receptor activity
FT                   and HCoV-229E infection."
FT                   /evidence="ECO:0000269|PubMed:11559807"
FT   MUTAGEN         288..295
FT                   /note="DYVEKQAS->QSVNETAQ: Complete loss of receptor
FT                   activity and blocks HCoV-229E infection. No loss of
FT                   enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:11559807"
FT   MUTAGEN         291..293
FT                   /note="EKQ->NKT: Complete loss of receptor activity and
FT                   blocks HCoV-229E infection. No loss of enzymatic activity."
FT   MUTAGEN         291
FT                   /note="E->N: No change of receptor activity and HCoV-229E
FT                   infection."
FT   MUTAGEN         293
FT                   /note="Q->T: No change of receptor activity and HCoV-229E
FT                   infection."
FT   MUTAGEN         392
FT                   /note="H->A: Loss of aminopeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:8887485"
FT   MUTAGEN         818
FT                   /note="N->E: Very low receptor activity and HCoV-229E
FT                   infection."
FT                   /evidence="ECO:0000269|PubMed:11559807"
FT   CONFLICT        536
FT                   /note="V -> E (in Ref. 1; CAA31640)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        887
FT                   /note="L -> P (in Ref. 1; CAA31640)"
FT                   /evidence="ECO:0000305"
FT   HELIX           70..72
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          73..75
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          78..91
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          102..115
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          118..123
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          126..129
FT                   /evidence="ECO:0000244|PDB:5LHD"
FT   STRAND          135..142
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          150..156
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            157..160
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          161..168
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          175..185
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          188..200
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          203..211
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            213..216
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           217..219
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          231..240
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          243..249
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          251..253
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          256..258
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          261..269
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           277..279
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          282..285
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          288..293
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          299..304
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           306..310
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            311..314
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           315..331
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          338..348
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          350..354
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          359..363
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           364..367
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            371..373
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           376..394
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            396..398
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          399..403
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           404..407
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           408..425
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           427..429
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           431..434
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           435..438
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           440..447
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           459..461
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           465..470
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           474..491
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           493..507
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          510..512
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           514..527
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           536..544
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          550..555
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            556..559
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          560..565
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            579..582
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          586..588
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          590..592
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          600..602
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          604..608
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           610..612
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          620..623
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           624..626
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   STRAND          631..634
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           636..649
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           650..652
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           655..670
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           676..681
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           682..688
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           692..709
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           715..736
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            737..741
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           747..762
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           766..781
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           790..792
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           793..803
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           806..817
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           822..832
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           838..848
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            851..853
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           856..858
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           859..868
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           872..882
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           884..890
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            891..894
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           898..906
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           912..924
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   TURN            925..928
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           931..933
FT                   /evidence="ECO:0000244|PDB:4FYT"
FT   HELIX           934..965
FT                   /evidence="ECO:0000244|PDB:4FYT"
SQ   SEQUENCE   967 AA;  109540 MW;  37B6BC1BF0D6B1F2 CRC64;
     MAKGFYISKS LGILGILLGV AAVCTIIALS VVYSQEKNKN ANSSPVASTT PSASATTNPA
     SATTLDQSKA WNRYRLPNTL KPDSYRVTLR PYLTPNDRGL YVFKGSSTVR FTCKEATDVI
     IIHSKKLNYT LSQGHRVVLR GVGGSQPPDI DKTELVEPTE YLVVHLKGSL VKDSQYEMDS
     EFEGELADDL AGFYRSEYME GNVRKVVATT QMQAADARKS FPCFDEPAMK AEFNITLIHP
     KDLTALSNML PKGPSTPLPE DPNWNVTEFH TTPKMSTYLL AFIVSEFDYV EKQASNGVLI
     RIWARPSAIA AGHGDYALNV TGPILNFFAG HYDTPYPLPK SDQIGLPDFN AGAMENWGLV
     TYRENSLLFD PLSSSSSNKE RVVTVIAHEL AHQWFGNLVT IEWWNDLWLN EGFASYVEYL
     GADYAEPTWN LKDLMVLNDV YRVMAVDALA SSHPLSTPAS EINTPAQISE LFDAISYSKG
     ASVLRMLSSF LSEDVFKQGL ASYLHTFAYQ NTIYLNLWDH LQEAVNNRSI QLPTTVRDIM
     NRWTLQMGFP VITVDTSTGT LSQEHFLLDP DSNVTRPSEF NYVWIVPITS IRDGRQQQDY
     WLIDVRAQND LFSTSGNEWV LLNLNVTGYY RVNYDEENWR KIQTQLQRDH SAIPVINRAQ
     IINDAFNLAS AHKVPVTLAL NNTLFLIEER QYMPWEAALS SLSYFKLMFD RSEVYGPMKN
     YLKKQVTPLF IHFRNNTNNW REIPENLMDQ YSEVNAISTA CSNGVPECEE MVSGLFKQWM
     ENPNNNPIHP NLRSTVYCNA IAQGGEEEWD FAWEQFRNAT LVNEADKLRA ALACSKELWI
     LNRYLSYTLN PDLIRKQDAT STIISITNNV IGQGLVWDFV QSNWKKLFND YGGGSFSFSN
     LIQAVTRRFS TEYELQQLEQ FKKDNEETGF GSGTRALEQA LEKTKANIKW VKENKEVVLQ
     WFTENSK
//