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   10-FEB-2021, entry version 6.
DE   RecName: Full=ORF7a protein;
DE            Short=ORF7a;
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; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Sarbecovirus.
OX   NCBI_TaxID=2697049;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
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: Plays a role as antagonist of host tetherin (BST2),
CC       disrupting its antiviral effect. Acts by binding to BST2 thereby
CC       interfering with its glycosylation. May suppress small interfering RNA
CC       (siRNA). May bind to host ITGAL, thereby playing a role in attachment
CC       or modulation of leukocytes. {ECO:0000250|UniProtKB:P59635}.
CC   -!- SUBUNIT: Interacts with the spike glycoprotein. Interacts with M
CC       protein. Interacts with E protein. Interacts with the ORF3a protein.
CC       Interacts with human SGT. Interacts with host ITGAL. Interacts with
CC       host BST2. {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}.
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DR   EMBL; MN908947; QHD43421.1; -; Genomic_RNA.
DR   RefSeq; YP_009724395.1; NC_045512.2.
DR   PDB; 6W37; X-ray; 2.90 A; A=16-82.
DR   PDBsum; 6W37; -.
DR   SMR; P0DTC7; -.
DR   BioGRID; 4383872; 1115.
DR   IntAct; P0DTC7; 101.
DR   GeneID; 43740573; -.
DR   KEGG; vg:43740573; -.
DR   Reactome; R-HSA-9694322; Virion Assembly and Release.
DR   Reactome; R-HSA-9694614; Attachment and Entry.
DR   PRO; PR:P0DTC7; -.
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   GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1550; -; 1.
DR   InterPro; IPR014888; NS7A_CoV.
DR   InterPro; IPR036495; NS7A_sf_CoV.
DR   Pfam; PF08779; bCoV_NS7A; 1.
DR   SUPFAM; SSF117066; SSF117066; 1.
DR   PROSITE; PS51919; X4E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond;
KW   G0/G1 host cell cycle checkpoint dysregulation by virus;
KW   Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW   Host-virus interaction; Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host tetherin by virus; Membrane;
KW   Modulation of host cell cycle by virus; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Viral immunoevasion; Virion.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..121
FT                   /note="ORF7a protein"
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"
FT   STRAND          21..24
FT                   /evidence="ECO:0000244|PDB:6W37"
FT   STRAND          27..32
FT                   /evidence="ECO:0000244|PDB:6W37"
FT   STRAND          34..37
FT                   /evidence="ECO:0000244|PDB:6W37"
FT   STRAND          39..41
FT                   /evidence="ECO:0000244|PDB:6W37"
FT   STRAND          47..49
FT                   /evidence="ECO:0000244|PDB:6W37"
FT   TURN            50..52
FT                   /evidence="ECO:0000244|PDB:6W37"
FT   STRAND          53..57
FT                   /evidence="ECO:0000244|PDB:6W37"
FT   STRAND          60..66
FT                   /evidence="ECO:0000244|PDB:6W37"
FT   STRAND          72..80
FT                   /evidence="ECO:0000244|PDB:6W37"
SQ   SEQUENCE   121 AA;  13744 MW;  891E7EAB9E8A5BA9 CRC64;
     MKIILFLALI TLATCELYHY QECVRGTTVL LKEPCSSGTY EGNSPFHPLA DNKFALTCFS
     TQFAFACPDG VKHVYQLRAR SVSPKLFIRQ EEVQELYSPI FLIVAAIVFI TLCFTLKRKT
     E
//