ID   SGTA_HUMAN              Reviewed;         313 AA.
AC   O43765; D6W610; Q6FIA9; Q9BTZ9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   17-JUN-2020, entry version 196.
DE   RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein alpha;
DE   AltName: Full=Alpha-SGT;
DE   AltName: Full=Vpu-binding protein;
DE            Short=UBP;
GN   Name=SGTA; Synonyms=SGT, SGT1;
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].
RX   PubMed=9740675; DOI=10.1006/geno.1998.5385;
RA   Kordes E., Savelyeva L., Schwab M., Rommelaere J., Jauniaux J.-C.,
RA   Cziepluch C.;
RT   "Isolation and characterization of human SGT and identification of
RT   homologues in Saccharomyces cerevisiae and Caenorhabditis elegans.";
RL   Genomics 52:90-94(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10567422; DOI=10.1074/jbc.274.48.34425;
RA   Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.;
RT   "Specific interaction of the 70-kDa heat shock cognate protein with the
RT   tetratricopeptide repeats.";
RL   J. Biol. Chem. 274:34425-34432(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH HIV-1V PU AND GAG
RP   (MICROBIAL INFECTION).
RX   PubMed=9573291;
RA   Callahan M.A., Handley M.A., Lee Y.H., Talbot K.J., Harper J.W.,
RA   Panganiban A.T.;
RT   "Functional interaction of human immunodeficiency virus type 1 Vpu and Gag
RT   with a novel member of the tetratricopeptide repeat protein family.";
RL   J. Virol. 72:5189-5197(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tobaben S., Stahl B.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, Muscle, and Uterus;
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   [10]
RP   PROTEIN SEQUENCE OF 138-160; 165-174 AND 185-196.
RC   TISSUE=Fetal brain cortex;
RA   Lubec G., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [11]
RP   SUBUNIT, AND INTERACTION WITH HSP90AA1 AND SLC2A1.
RX   PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
RA   Liou S.T., Wang C.;
RT   "Small glutamine-rich tetratricopeptide repeat-containing protein is
RT   composed of three structural units with distinct functions.";
RL   Arch. Biochem. Biophys. 435:253-263(2005).
RN   [12]
RP   INTERACTION WITH HSP90AB1, AND SUBCELLULAR LOCATION.
RX   PubMed=16580629; DOI=10.1016/j.bbrc.2006.03.090;
RA   Yin H., Wang H., Zong H., Chen X., Wang Y., Yun X., Wu Y., Wang J., Gu J.;
RT   "SGT, a Hsp90beta binding partner, is accumulated in the nucleus during
RT   cell apoptosis.";
RL   Biochem. Biophys. Res. Commun. 343:1153-1158(2006).
RN   [13]
RP   INTERACTION WITH SARS-COV ACCESSORY PROTEIN 7A (MICROBIAL INFECTION).
RX   PubMed=16580632; DOI=10.1016/j.bbrc.2006.03.091;
RA   Fielding B.C., Gunalan V., Tan T.H.P., Chou C.-F., Shen S., Khan S.,
RA   Lim S.G., Hong W., Tan Y.-J.;
RT   "Severe acute respiratory syndrome coronavirus protein 7a interacts with
RT   hSGT.";
RL   Biochem. Biophys. Res. Commun. 343:1201-1208(2006).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [15]
RP   INTERACTION WITH DNAJC5 AND DNAJC5B.
RX   PubMed=17034881; DOI=10.1016/j.bbamcr.2006.08.054;
RA   Boal F., Le Pevelen S., Cziepluch C., Scotti P., Lang J.;
RT   "Cysteine-string protein isoform beta (Cspbeta) is targeted to the trans-
RT   Golgi network as a non-palmitoylated CSP in clonal beta-cells.";
RL   Biochim. Biophys. Acta 1773:109-119(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81; SER-301; THR-303
RP   AND SER-305, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81 AND SER-305, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [20]
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   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-305, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [22]
RP   FUNCTION, AND INTERACTION WITH BAG6.
RX   PubMed=23129660; DOI=10.1073/pnas.1209997109;
RA   Leznicki P., High S.;
RT   "SGTA antagonizes BAG6-mediated protein triage.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:19214-19219(2012).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81 AND SER-301, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [24]
RP   FUNCTION, AND INTERACTION WITH BAG6.
RX   PubMed=25179605; DOI=10.1242/jcs.155648;
RA   Wunderley L., Leznicki P., Payapilly A., High S.;
RT   "SGTA regulates the cytosolic quality control of hydrophobic substrates.";
RL   J. Cell Sci. 127:4728-4739(2014).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81; THR-303 AND SER-305, AND
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   [26]
RP   FUNCTION (MICROBIAL INFECTION), IDENTIFICATION IN A COMPLEX WITH DNAJB12
RP   AND DNAJB14, AND INTERACTION WITH HSPA8.
RX   PubMed=24675744; DOI=10.1371/journal.ppat.1004007;
RA   Walczak C.P., Ravindran M.S., Inoue T., Tsai B.;
RT   "A cytosolic chaperone complexes with dynamic membrane J-proteins and
RT   mobilizes a nonenveloped virus out of the endoplasmic reticulum.";
RL   PLoS Pathog. 10:E1004007-E1004007(2014).
RN   [27]
RP   FUNCTION, AND MUTAGENESIS OF CYS-38.
RX   PubMed=25535373; DOI=10.1073/pnas.1402745112;
RA   Mock J.Y., Chartron J.W., Zaslaver M., Xu Y., Ye Y., Clemons W.M. Jr.;
RT   "Bag6 complex contains a minimal tail-anchor-targeting module and a mock
RT   BAG domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:106-111(2015).
RN   [28]
RP   FUNCTION, AND INTERACTION WITH BAG6.
RX   PubMed=27193484; DOI=10.1038/srep26433;
RA   Krysztofinska E.M., Martinez-Lumbreras S., Thapaliya A., Evans N.J.,
RA   High S., Isaacson R.L.;
RT   "Structural and functional insights into the E3 ligase, RNF126.";
RL   Sci. Rep. 6:26433-26433(2016).
RN   [29]
RP   FUNCTION.
RX   PubMed=28104892; DOI=10.1126/science.aah6130;
RA   Shao S., Rodrigo-Brenni M.C., Kivlen M.H., Hegde R.S.;
RT   "Mechanistic basis for a molecular triage reaction.";
RL   Science 355:298-302(2017).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 84-210, SUBUNIT (MICROBIAL
RP   INFECTION), AND FUNCTION.
RX   PubMed=18759457; DOI=10.1021/bi800758a;
RA   Dutta S., Tan Y.J.;
RT   "Structural and functional characterization of human SGT and its
RT   interaction with Vpu of the human immunodeficiency virus type 1.";
RL   Biochemistry 47:10123-10131(2008).
CC   -!- FUNCTION: Co-chaperone that binds misfolded and hydrophobic patches-
CC       containing client proteins in the cytosol. Mediates their targeting to
CC       the endoplasmic reticulum but also regulates their sorting to the
CC       proteasome when targeting fails (PubMed:28104892). Functions in tail-
CC       anchored/type II transmembrane proteins membrane insertion constituting
CC       with ASNA1 and the BAG6 complex a targeting module (PubMed:28104892).
CC       Functions upstream of the BAG6 complex and ASNA1, binding more rapidly
CC       the transmembrane domain of newly synthesized proteins
CC       (PubMed:28104892, PubMed:25535373). It is also involved in the
CC       regulation of the endoplasmic reticulum-associated misfolded protein
CC       catabolic process via its interaction with BAG6: collaborates with the
CC       BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated
CC       states (PubMed:23129660, PubMed:25179605). Competes with RNF126 for
CC       interaction with BAG6, preventing the ubiquitination of client proteins
CC       associated with the BAG6 complex (PubMed:27193484). Binds directly to
CC       HSC70 and HSP70 and regulates their ATPase activity (PubMed:18759457).
CC       {ECO:0000269|PubMed:18759457, ECO:0000269|PubMed:23129660,
CC       ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:25535373,
CC       ECO:0000269|PubMed:27193484, ECO:0000269|PubMed:28104892}.
CC   -!- FUNCTION: (Microbial infection) In case of infection by polyomavirus,
CC       involved in the virus endoplasmic reticulum membrane penetration and
CC       infection via interaction with DNAJB12, DNAJB14 and HSPA8/Hsc70
CC       (PubMed:24675744). {ECO:0000269|PubMed:24675744}.
CC   -!- SUBUNIT: Homodimer (PubMed:15708368). Homooligomer (By similarity).
CC       Interacts with DNAJC5 and DNAJC5B. Interacts (via TPR repeats) with
CC       HSP90AA1 (PubMed:15708368). Interacts (via Gln-rich region) with SLC2A1
CC       (PubMed:15708368). Interacts with HSP90AB1 (PubMed:16580629). Interacts
CC       (via TPR repeats) with HSPA8/Hsc70; the interaction is direct
CC       (PubMed:24675744). Interacts with BAG6 (via ubiquitin-like domain);
CC       interaction prevents interaction between BAG6 and RNF126
CC       (PubMed:23129660, PubMed:25179605, PubMed:27193484). Forms a
CC       multiprotein complex, at least composed of DNAJB12, DNAJB14,
CC       HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is
CC       direct (PubMed:24675744). {ECO:0000250|UniProtKB:O70593,
CC       ECO:0000269|PubMed:15708368, ECO:0000269|PubMed:16580629,
CC       ECO:0000269|PubMed:17034881, ECO:0000269|PubMed:18759457,
CC       ECO:0000269|PubMed:23129660, ECO:0000269|PubMed:24675744,
CC       ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:27193484}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Vpu and Gag from HIV-1.
CC       {ECO:0000269|PubMed:18759457, ECO:0000269|PubMed:9573291}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV accessory
CC       protein 7a. {ECO:0000269|PubMed:16580632}.
CC   -!- INTERACTION:
CC       O43765; Q9UKJ8: ADAM21; NbExp=3; IntAct=EBI-347996, EBI-12046857;
CC       O43765; A8K660: ADIPOQ; NbExp=3; IntAct=EBI-347996, EBI-10174479;
CC       O43765; Q15848: ADIPOQ; NbExp=7; IntAct=EBI-347996, EBI-10827839;
CC       O43765; O95994: AGR2; NbExp=3; IntAct=EBI-347996, EBI-712648;
CC       O43765; Q8TD06: AGR3; NbExp=6; IntAct=EBI-347996, EBI-3925742;
CC       O43765; Q16853: AOC3; NbExp=3; IntAct=EBI-347996, EBI-3921628;
CC       O43765; O95816: BAG2; NbExp=2; IntAct=EBI-347996, EBI-355275;
CC       O43765; P46379: BAG6; NbExp=6; IntAct=EBI-347996, EBI-347552;
CC       O43765; P46379-2: BAG6; NbExp=3; IntAct=EBI-347996, EBI-10988864;
CC       O43765; P35070: BTC; NbExp=6; IntAct=EBI-347996, EBI-6590057;
CC       O43765; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-347996, EBI-12062109;
CC       O43765; Q9BXJ1: C1QTNF1; NbExp=4; IntAct=EBI-347996, EBI-750200;
CC       O43765; Q9BXJ0: C1QTNF5; NbExp=3; IntAct=EBI-347996, EBI-19947914;
CC       O43765; Q9BXI9: C1QTNF6; NbExp=9; IntAct=EBI-347996, EBI-10301084;
CC       O43765; Q6UWT4: C5orf46; NbExp=3; IntAct=EBI-347996, EBI-11986083;
CC       O43765; Q8N6L0: CCDC155; NbExp=8; IntAct=EBI-347996, EBI-749265;
CC       O43765; P40259: CD79B; NbExp=6; IntAct=EBI-347996, EBI-2873732;
CC       O43765; Q8TCZ2: CD99L2; NbExp=8; IntAct=EBI-347996, EBI-2824782;
CC       O43765; P55291: CDH15; NbExp=8; IntAct=EBI-347996, EBI-10215061;
CC       O43765; P07510-2: CHRNG; NbExp=3; IntAct=EBI-347996, EBI-11979451;
CC       O43765; A0A0S2Z3K0: COL1A2; NbExp=3; IntAct=EBI-347996, EBI-16431143;
CC       O43765; P08123: COL1A2; NbExp=11; IntAct=EBI-347996, EBI-983038;
CC       O43765; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-347996, EBI-10241815;
CC       O43765; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-347996, EBI-852194;
CC       O43765; P09603: CSF1; NbExp=6; IntAct=EBI-347996, EBI-2872294;
CC       O43765; P01037: CST1; NbExp=3; IntAct=EBI-347996, EBI-1056240;
CC       O43765; P78358: CTAG1A; NbExp=3; IntAct=EBI-347996, EBI-1188472;
CC       O43765; P07711: CTSL; NbExp=3; IntAct=EBI-347996, EBI-1220160;
CC       O43765; Q9UHQ9: CYB5R1; NbExp=3; IntAct=EBI-347996, EBI-953870;
CC       O43765; P59861: DEFB131A; NbExp=5; IntAct=EBI-347996, EBI-12304807;
CC       O43765; Q9UBP4: DKK3; NbExp=3; IntAct=EBI-347996, EBI-954409;
CC       O43765; Q6E0U4: DMKN; NbExp=3; IntAct=EBI-347996, EBI-7943171;
CC       O43765; Q9HAV5: EDA2R; NbExp=3; IntAct=EBI-347996, EBI-526033;
CC       O43765; Q9UNE0-2: EDAR; NbExp=3; IntAct=EBI-347996, EBI-12964110;
CC       O43765; A0A0S2Z3V1: EFEMP1; NbExp=3; IntAct=EBI-347996, EBI-16434097;
CC       O43765; Q12805: EFEMP1; NbExp=14; IntAct=EBI-347996, EBI-536772;
CC       O43765; O95967: EFEMP2; NbExp=7; IntAct=EBI-347996, EBI-743414;
CC       O43765; Q96DN0: ERP27; NbExp=7; IntAct=EBI-347996, EBI-953772;
CC       O43765; P30040: ERP29; NbExp=3; IntAct=EBI-347996, EBI-946830;
CC       O43765; Q9HBU6: ETNK1; NbExp=3; IntAct=EBI-347996, EBI-2834493;
CC       O43765; Q9NVM1: EVA1B; NbExp=6; IntAct=EBI-347996, EBI-10314666;
CC       O43765; Q9Y624: F11R; NbExp=11; IntAct=EBI-347996, EBI-742600;
CC       O43765; Q96RJ6: FERD3L; NbExp=3; IntAct=EBI-347996, EBI-10183007;
CC       O43765; Q9NSA1: FGF21; NbExp=3; IntAct=EBI-347996, EBI-3909329;
CC       O43765; Q9Y680: FKBP7; NbExp=6; IntAct=EBI-347996, EBI-3918971;
CC       O43765; Q12841: FSTL1; NbExp=3; IntAct=EBI-347996, EBI-2349801;
CC       O43765; P54710-2: FXYD2; NbExp=5; IntAct=EBI-347996, EBI-13084584;
CC       O43765; P58549: FXYD7; NbExp=8; IntAct=EBI-347996, EBI-10216171;
CC       O43765; O75084: FZD7; NbExp=3; IntAct=EBI-347996, EBI-746917;
CC       O43765; P22466: GAL; NbExp=6; IntAct=EBI-347996, EBI-6624768;
CC       O43765; Q9UBC7: GALP; NbExp=3; IntAct=EBI-347996, EBI-12244186;
CC       O43765; P09681: GIP; NbExp=6; IntAct=EBI-347996, EBI-8588553;
CC       O43765; Q14440: GPErik; NbExp=3; IntAct=EBI-347996, EBI-10232920;
CC       O43765; Q96SL4: GPX7; NbExp=7; IntAct=EBI-347996, EBI-749411;
CC       O43765; P28799: GRN; NbExp=7; IntAct=EBI-347996, EBI-747754;
CC       O43765; Q02747: GUCA2A; NbExp=8; IntAct=EBI-347996, EBI-12244272;
CC       O43765; A0A0C4DFT7: GYPA; NbExp=3; IntAct=EBI-347996, EBI-12044847;
CC       O43765; B8Q183: GYPA; NbExp=4; IntAct=EBI-347996, EBI-10176190;
CC       O43765; P02724: GYPA; NbExp=3; IntAct=EBI-347996, EBI-702665;
CC       O43765; P48723: HSPA13; NbExp=8; IntAct=EBI-347996, EBI-750892;
CC       O43765; P46695: IER3; NbExp=6; IntAct=EBI-347996, EBI-1748945;
CC       O43765; P24592: IGFBP6; NbExp=3; IntAct=EBI-347996, EBI-947015;
CC       O43765; Q6PIQ7: IGL@; NbExp=3; IntAct=EBI-347996, EBI-6677651;
CC       O43765; Q8N355: IGL@; NbExp=4; IntAct=EBI-347996, EBI-748681;
CC       O43765; P40189: IL6ST; NbExp=3; IntAct=EBI-347996, EBI-1030834;
CC       O43765; Q14653: IRF3; NbExp=3; IntAct=EBI-347996, EBI-2650369;
CC       O43765; Q13568: IRF5; NbExp=3; IntAct=EBI-347996, EBI-3931258;
CC       O43765; Q6GPH6: ITPRIPL1; NbExp=3; IntAct=EBI-347996, EBI-953819;
CC       O43765; Q6GPH6-2: ITPRIPL1; NbExp=3; IntAct=EBI-347996, EBI-12337095;
CC       O43765; Q09470: KCNA1; NbExp=3; IntAct=EBI-347996, EBI-8286599;
CC       O43765; Q16322: KCNA10; NbExp=3; IntAct=EBI-347996, EBI-12265328;
CC       O43765; Q9UJ90: KCNE5; NbExp=3; IntAct=EBI-347996, EBI-11981259;
CC       O43765; P02538: KRT6A; NbExp=3; IntAct=EBI-347996, EBI-702198;
CC       O43765; Q86UP2: KTN1; NbExp=3; IntAct=EBI-347996, EBI-359761;
CC       O43765; Q86UP2-3: KTN1; NbExp=3; IntAct=EBI-347996, EBI-12007212;
CC       O43765; Q6ISS4: LAIR2; NbExp=6; IntAct=EBI-347996, EBI-10250491;
CC       O43765; O43561: LAT; NbExp=3; IntAct=EBI-347996, EBI-1222766;
CC       O43765; O43561-2: LAT; NbExp=3; IntAct=EBI-347996, EBI-8070286;
CC       O43765; P80188: LCN2; NbExp=5; IntAct=EBI-347996, EBI-11911016;
CC       O43765; O15165-2: LDLRAD4; NbExp=3; IntAct=EBI-347996, EBI-13302279;
CC       O43765; Q8N112: LSMEM2; NbExp=3; IntAct=EBI-347996, EBI-10264855;
CC       O43765; Q96G30: MRAP2; NbExp=6; IntAct=EBI-347996, EBI-9537218;
CC       O43765; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-347996, EBI-12806656;
CC       O43765; P08118: MSMB; NbExp=3; IntAct=EBI-347996, EBI-10195681;
CC       O43765; Q969H8: MYDGF; NbExp=8; IntAct=EBI-347996, EBI-718622;
CC       O43765; Q99972: MYOC; NbExp=3; IntAct=EBI-347996, EBI-11692272;
CC       O43765; Q8IW45: NAXD; NbExp=7; IntAct=EBI-347996, EBI-8650724;
CC       O43765; Q13232: NME3; NbExp=12; IntAct=EBI-347996, EBI-713684;
CC       O43765; Q9HCQ7: NPVF; NbExp=3; IntAct=EBI-347996, EBI-1753111;
CC       O43765; Q9GZP1: NRSN2; NbExp=3; IntAct=EBI-347996, EBI-724857;
CC       O43765; Q5JUK9: PAGE3; NbExp=6; IntAct=EBI-347996, EBI-10244544;
CC       O43765; C3PTT6: PAUF; NbExp=3; IntAct=EBI-347996, EBI-3505892;
CC       O43765; Q96AQ6: PBXIP1; NbExp=4; IntAct=EBI-347996, EBI-740845;
CC       O43765; Q9UN74: PCDHA4; NbExp=3; IntAct=EBI-347996, EBI-712273;
CC       O43765; Q9Y5G9: PCDHGA4; NbExp=3; IntAct=EBI-347996, EBI-12956949;
CC       O43765; Q96PD5-2: PGLYRP2; NbExp=3; IntAct=EBI-347996, EBI-12758027;
CC       O43765; Q9UL19: PLAAT4; NbExp=4; IntAct=EBI-347996, EBI-10323452;
CC       O43765; Q969W9-2: PMEPA1; NbExp=3; IntAct=EBI-347996, EBI-13318883;
CC       O43765; P23284: PPIB; NbExp=6; IntAct=EBI-347996, EBI-359252;
CC       O43765; P45877: PPIC; NbExp=6; IntAct=EBI-347996, EBI-953909;
CC       O43765; Q96NZ9: PRAP1; NbExp=9; IntAct=EBI-347996, EBI-2116102;
CC       O43765; Q8TAS3: PRRG2; NbExp=3; IntAct=EBI-347996, EBI-10272071;
CC       O43765; Q9UIG4: PSORS1C2; NbExp=5; IntAct=EBI-347996, EBI-11974061;
CC       O43765; Q15293: RCN1; NbExp=3; IntAct=EBI-347996, EBI-948278;
CC       O43765; Q5GAN6: RNASE10; NbExp=5; IntAct=EBI-347996, EBI-12423312;
CC       O43765; P50876: RNF144A; NbExp=3; IntAct=EBI-347996, EBI-2340657;
CC       O43765; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-347996, EBI-12055631;
CC       O43765; P04843: RPN1; NbExp=7; IntAct=EBI-347996, EBI-355963;
CC       O43765; P31431: SDC4; NbExp=6; IntAct=EBI-347996, EBI-3913237;
CC       O43765; Q9HCN8: SDF2L1; NbExp=3; IntAct=EBI-347996, EBI-2339921;
CC       O43765; P05121: SERPINE1; NbExp=6; IntAct=EBI-347996, EBI-953978;
CC       O43765; O75830: SERPINI2; NbExp=3; IntAct=EBI-347996, EBI-750144;
CC       O43765; Q16586: SGCA; NbExp=13; IntAct=EBI-347996, EBI-5663553;
CC       O43765; Q16586-2: SGCA; NbExp=4; IntAct=EBI-347996, EBI-16434133;
CC       O43765; O43765: SGTA; NbExp=4; IntAct=EBI-347996, EBI-347996;
CC       O43765; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-347996, EBI-744081;
CC       O43765; Q96DD7: SHISA4; NbExp=3; IntAct=EBI-347996, EBI-18035902;
CC       O43765; Q8N114-3: SHISA5; NbExp=3; IntAct=EBI-347996, EBI-13369834;
CC       O43765; P03973: SLPI; NbExp=6; IntAct=EBI-347996, EBI-355293;
CC       O43765; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-347996, EBI-10226799;
CC       O43765; Q96QK8: SMIM14; NbExp=3; IntAct=EBI-347996, EBI-373430;
CC       O43765; Q71RC9: SMIM5; NbExp=9; IntAct=EBI-347996, EBI-12334905;
CC       O43765; P08294: SOD3; NbExp=3; IntAct=EBI-347996, EBI-10195782;
CC       O43765; Q5DT21: SPINK9; NbExp=3; IntAct=EBI-347996, EBI-13119580;
CC       O43765; P16150: SPN; NbExp=5; IntAct=EBI-347996, EBI-10049055;
CC       O43765; P10451: SPP1; NbExp=8; IntAct=EBI-347996, EBI-723648;
CC       O43765; Q8TCT8: SPPL2A; NbExp=7; IntAct=EBI-347996, EBI-750784;
CC       O43765; P10124: SRGN; NbExp=10; IntAct=EBI-347996, EBI-744915;
CC       O43765; Q86TD4-2: SRL; NbExp=3; IntAct=EBI-347996, EBI-12304565;
CC       O43765; E0CX11: STMP1; NbExp=3; IntAct=EBI-347996, EBI-18397783;
CC       O43765; P51687: SUOX; NbExp=3; IntAct=EBI-347996, EBI-3921347;
CC       O43765; Q9BT88: SYT11; NbExp=7; IntAct=EBI-347996, EBI-751770;
CC       O43765; Q9H2B2: SYT4; NbExp=7; IntAct=EBI-347996, EBI-751132;
CC       O43765; Q07654: TFF3; NbExp=3; IntAct=EBI-347996, EBI-10224676;
CC       O43765; P02786: TFRC; NbExp=6; IntAct=EBI-347996, EBI-355727;
CC       O43765; P01135: TGFA; NbExp=3; IntAct=EBI-347996, EBI-1034374;
CC       O43765; P01135-2: TGFA; NbExp=6; IntAct=EBI-347996, EBI-12367411;
CC       O43765; Q6P9G4: TMEM154; NbExp=3; IntAct=EBI-347996, EBI-13329239;
CC       O43765; Q8WUU8: TMEM174; NbExp=6; IntAct=EBI-347996, EBI-10276729;
CC       O43765; Q96A57-2: TMEM230; NbExp=3; IntAct=EBI-347996, EBI-17546822;
CC       O43765; Q5JXX7: TMEM31; NbExp=3; IntAct=EBI-347996, EBI-10244617;
CC       O43765; Q9Y2Y6: TMEM98; NbExp=3; IntAct=EBI-347996, EBI-7333781;
CC       O43765; O60235: TMPRSS11D; NbExp=3; IntAct=EBI-347996, EBI-7639969;
CC       O43765; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-347996, EBI-2820477;
CC       O43765; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-347996, EBI-717441;
CC       O43765; O14836: TNFRSF13B; NbExp=3; IntAct=EBI-347996, EBI-519160;
CC       O43765; O14836-2: TNFRSF13B; NbExp=8; IntAct=EBI-347996, EBI-12023110;
CC       O43765; Q9NS68-2: TNFRSF19; NbExp=3; IntAct=EBI-347996, EBI-12089038;
CC       O43765; O75509: TNFRSF21; NbExp=3; IntAct=EBI-347996, EBI-2313231;
CC       O43765; O43508: TNFSF12; NbExp=3; IntAct=EBI-347996, EBI-6932080;
CC       O43765; Q9C035-3: TRIM5; NbExp=3; IntAct=EBI-347996, EBI-12840050;
CC       O43765; Q5BVD1: TTMP; NbExp=6; IntAct=EBI-347996, EBI-10243654;
CC       O43765; Q9GZX9: TWSG1; NbExp=3; IntAct=EBI-347996, EBI-10304067;
CC       O43765; O95881: TXNDC12; NbExp=3; IntAct=EBI-347996, EBI-2564581;
CC       O43765; P11441: UBL4A; NbExp=5; IntAct=EBI-347996, EBI-356983;
CC       O43765; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-347996, EBI-947187;
CC       O43765; O75631: UPK3A; NbExp=3; IntAct=EBI-347996, EBI-10188907;
CC       O43765; P01282: VIP; NbExp=3; IntAct=EBI-347996, EBI-751454;
CC       O43765; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-347996, EBI-10316321;
CC       O43765; Q8WWY7: WFDC12; NbExp=3; IntAct=EBI-347996, EBI-11958577;
CC       O43765; Q8IUB5: WFDC13; NbExp=5; IntAct=EBI-347996, EBI-12041955;
CC       O43765; Q8TCV5: WFDC5; NbExp=3; IntAct=EBI-347996, EBI-12175871;
CC       O43765; Q8NAP8: ZBTB8B; NbExp=3; IntAct=EBI-347996, EBI-17494306;
CC       O43765; O60844: ZG16; NbExp=12; IntAct=EBI-347996, EBI-746479;
CC       O43765; Q96DA0: ZG16B; NbExp=3; IntAct=EBI-347996, EBI-953824;
CC       O43765; A0A1U9X8X8; NbExp=3; IntAct=EBI-347996, EBI-17234977;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16580629}. Nucleus
CC       {ECO:0000269|PubMed:16580629}. Note=Co-localizes with HSP90AB1 in the
CC       cytoplasm. Increased nuclear accumulation seen during cell apoptosis.
CC       {ECO:0000269|PubMed:16580629}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The second tetratricopeptide repeat (TPR 2) mediates the
CC       interaction with SARS-CoV accessory protein 7a.
CC   -!- SIMILARITY: Belongs to the SGT family. {ECO:0000305}.
DR   EMBL; AJ223828; CAA11565.1; -; mRNA.
DR   EMBL; AJ133129; CAB39725.1; -; mRNA.
DR   EMBL; AF408399; AAL01051.1; -; mRNA.
DR   EMBL; AF368279; AAP29457.1; -; mRNA.
DR   EMBL; AL050156; CAB43297.2; -; mRNA.
DR   EMBL; CR533517; CAG38548.1; -; mRNA.
DR   EMBL; CR542282; CAG47077.1; -; mRNA.
DR   EMBL; AC006538; AAD13117.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69366.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69367.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69368.1; -; Genomic_DNA.
DR   EMBL; BC000390; AAH00390.1; -; mRNA.
DR   EMBL; BC002989; AAH02989.2; -; mRNA.
DR   EMBL; BC005165; AAH05165.1; -; mRNA.
DR   EMBL; BC008885; AAH08885.1; -; mRNA.
DR   CCDS; CCDS12094.1; -.
DR   RefSeq; NP_003012.1; NM_003021.3.
DR   RefSeq; XP_011526480.1; XM_011528178.2.
DR   PDB; 2VYI; X-ray; 2.40 A; A/B=84-210.
DR   PDB; 4CPG; NMR; -; A/B=1-69.
DR   PDB; 4GOD; X-ray; 1.40 A; A/B=4-54.
DR   PDB; 4GOE; X-ray; 1.45 A; A/B=4-54.
DR   PDB; 4GOF; X-ray; 1.35 A; A/B=4-54.
DR   PDBsum; 2VYI; -.
DR   PDBsum; 4CPG; -.
DR   PDBsum; 4GOD; -.
DR   PDBsum; 4GOE; -.
DR   PDBsum; 4GOF; -.
DR   SMR; O43765; -.
DR   BioGRID; 112347; 160.
DR   IntAct; O43765; 208.
DR   MINT; O43765; -.
DR   STRING; 9606.ENSP00000221566; -.
DR   iPTMnet; O43765; -.
DR   PhosphoSitePlus; O43765; -.
DR   SwissPalm; O43765; -.
DR   BioMuta; SGTA; -.
DR   EPD; O43765; -.
DR   jPOST; O43765; -.
DR   MassIVE; O43765; -.
DR   MaxQB; O43765; -.
DR   PaxDb; O43765; -.
DR   PeptideAtlas; O43765; -.
DR   PRIDE; O43765; -.
DR   ProteomicsDB; 49156; -.
DR   TopDownProteomics; O43765; -.
DR   Antibodypedia; 23040; 258 antibodies.
DR   DNASU; 6449; -.
DR   Ensembl; ENST00000221566; ENSP00000221566; ENSG00000104969.
DR   GeneID; 6449; -.
DR   KEGG; hsa:6449; -.
DR   UCSC; uc002lwi.2; human.
DR   CTD; 6449; -.
DR   DisGeNET; 6449; -.
DR   EuPathDB; HostDB:ENSG00000104969.9; -.
DR   GeneCards; SGTA; -.
DR   HGNC; HGNC:10819; SGTA.
DR   HPA; ENSG00000104969; Low tissue specificity.
DR   MIM; 603419; gene.
DR   neXtProt; NX_O43765; -.
DR   OpenTargets; ENSG00000104969; -.
DR   PharmGKB; PA35727; -.
DR   eggNOG; KOG0553; Eukaryota.
DR   eggNOG; COG0457; LUCA.
DR   GeneTree; ENSGT00940000159037; -.
DR   HOGENOM; CLU_044224_0_0_1; -.
DR   InParanoid; O43765; -.
DR   KO; K16365; -.
DR   OMA; TDCKSAL; -.
DR   OrthoDB; 687493at2759; -.
DR   PhylomeDB; O43765; -.
DR   TreeFam; TF313092; -.
DR   Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   BioGRID-ORCS; 6449; 5 hits in 788 CRISPR screens.
DR   ChiTaRS; SGTA; human.
DR   EvolutionaryTrace; O43765; -.
DR   GeneWiki; SGTA; -.
DR   GenomeRNAi; 6449; -.
DR   Pharos; O43765; Tbio.
DR   PRO; PR:O43765; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O43765; protein.
DR   Bgee; ENSG00000104969; Expressed in C1 segment of cervical spinal cord and 188 other tissues.
DR   ExpressionAtlas; O43765; baseline and differential.
DR   Genevisible; O43765; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0072380; C:TRC complex; IBA:GO_Central.
DR   GO; GO:1904288; F:BAT3 complex binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl.
DR   GO; GO:1903070; P:negative regulation of ER-associated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:1903646; P:positive regulation of chaperone-mediated protein folding; IBA:GO_Central.
DR   GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0006620; P:posttranslational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR032374; SGTA_dimer.
DR   InterPro; IPR013026; TPR-contain_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF16546; SGTA_dimer; 1.
DR   Pfam; PF00515; TPR_1; 2.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; TPR repeat.
FT   CHAIN           1..313
FT                   /note="Small glutamine-rich tetratricopeptide repeat-
FT                   containing protein alpha"
FT                   /id="PRO_0000106365"
FT   REPEAT          91..124
FT                   /note="TPR 1"
FT   REPEAT          125..158
FT                   /note="TPR 2"
FT   REPEAT          159..192
FT                   /note="TPR 3"
FT   COMPBIAS        275..287
FT                   /note="Gln-rich"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:23186163"
FT   MOD_RES         81
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:23186163,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70593"
FT   MOD_RES         137
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163"
FT   MOD_RES         303
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:24275569"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:24275569"
FT   MUTAGEN         38
FT                   /note="C->A: Reduces tail-anchored proteins transfer."
FT                   /evidence="ECO:0000269|PubMed:25535373"
FT   HELIX           5..21
FT                   /evidence="ECO:0000244|PDB:4GOF"
FT   HELIX           26..43
FT                   /evidence="ECO:0000244|PDB:4GOF"
FT   HELIX           48..51
FT                   /evidence="ECO:0000244|PDB:4CPG"
FT   HELIX           58..65
FT                   /evidence="ECO:0000244|PDB:4CPG"
FT   HELIX           87..103
FT                   /evidence="ECO:0000244|PDB:2VYI"
FT   HELIX           107..120
FT                   /evidence="ECO:0000244|PDB:2VYI"
FT   HELIX           125..137
FT                   /evidence="ECO:0000244|PDB:2VYI"
FT   HELIX           141..154
FT                   /evidence="ECO:0000244|PDB:2VYI"
FT   HELIX           159..171
FT                   /evidence="ECO:0000244|PDB:2VYI"
FT   HELIX           175..188
FT                   /evidence="ECO:0000244|PDB:2VYI"
FT   HELIX           193..206
FT                   /evidence="ECO:0000244|PDB:2VYI"
SQ   SEQUENCE   313 AA;  34063 MW;  80B3C71B41F3CB55 CRC64;
     MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE
     IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL
     NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPAYSK AYGRMGLALS SLNKHVEAVA
     YYKKALELDP DNETYKSNLK IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN
     PQIQQLMSGM ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR
     SRTPSASNDD QQE
//