ID   NS7A_SARS2              Reviewed;         121 AA.
AC   P0DTC7;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   17-JUN-2020, entry version 2.
DE   RecName: Full=Protein 7a;
DE   AltName: Full=Accessory protein 7a;
DE   AltName: Full=Protein U122;
DE   AltName: Full=Protein X4;
DE   Flags: Precursor;
GN   ORFNames=7a;
OS   Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2).
OC   Viruses; Riboviria; Nidovirales; Cornidovirineae; Coronaviridae;
OC   Orthocoronavirinae; Betacoronavirus; Sarbecovirus.
OX   NCBI_TaxID=2697049;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RX   PubMed=32015508; DOI=10.1038/s41586-020-2008-3;
RA   Wu F., Zhao S., Yu B., Chen Y.-M., Wang W., Song Z.-G., Hu Y., Tao Z.-W.,
RA   Tian J.-H., Pei Y.-Y., Yuan M.-L., Zhang Y.-L., Dai F.-H., Liu Y.,
RA   Wang Q.-M., Zheng J.-J., Xu L., Holmes E.C., Zhang Y.-Z.;
RT   "A new coronavirus associated with human respiratory disease in China.";
RL   Nature 579:265-269(2020).
CC   -!- FUNCTION: Non-structural protein which is dispensable for virus
CC       replication in cell culture. {ECO:0000250|UniProtKB:P59635}.
CC   -!- SUBUNIT: Interacts with the spike glycoprotein, M protein, E protein
CC       and the accessory protein 3a. Interacts with human SGT. Interacts with
CC       host ITGAL. {ECO:0000250|UniProtKB:P59635}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P59635}. Host
CC       endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P59635}; Single-
CC       pass membrane protein {ECO:0000250|UniProtKB:P59635}. Host endoplasmic
CC       reticulum-Golgi intermediate compartment membrane
CC       {ECO:0000250|UniProtKB:P59635}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P59635}. Host Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P59635}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P59635}.
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC       for type I membrane proteins. {ECO:0000250|UniProtKB:P59635}.
DR   EMBL; MN908947; QHD43421.1; -; Genomic_RNA.
DR   IntAct; P0DTC7; 2.
DR   Proteomes; UP000464024; Genome.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0039646; P:modulation by virus of host G0/G1 transition checkpoint; IEA:UniProtKB-KW.
DR   Gene3D;; -; 1.
DR   InterPro; IPR014888; SARS_X4.
DR   InterPro; IPR036495; SARS_X4_sf.
DR   Pfam; PF08779; bCoV_NS7A; 1.
DR   SUPFAM; SSF117066; SSF117066; 1.
DR   PROSITE; PS51919; X4E; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; G0/G1 host cell cycle checkpoint dysregulation by virus;
KW   Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW   Host-virus interaction; Membrane; Modulation of host cell cycle by virus;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Virion.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..121
FT                   /note="Protein 7a"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000449654"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          16..81
FT                   /note="X4e"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01267"
FT   MOTIF           117..121
FT                   /note="Di-lysine motif"
FT                   /evidence="ECO:0000250|UniProtKB:P59635"
FT   DISULFID        23..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01267"
FT   DISULFID        35..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01267"
SQ   SEQUENCE   121 AA;  13744 MW;  891E7EAB9E8A5BA9 CRC64;