ID AP3A_SARS2 Reviewed; 275 AA.
AC P0DTC3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 02-DEC-2020, entry version 5.
DE RecName: Full=ORF3a protein;
DE Short=ORF3a;
DE AltName: Full=Accessory protein 3a;
DE AltName: Full=Protein 3a;
DE AltName: Full=Protein U274;
DE AltName: Full=Protein X1;
GN ORFNames=3a;
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: Forms homotetrameric potassium sensitive ion channels
CC (viroporin) and may modulate virus release. Up-regulates expression of
CC fibrinogen subunits FGA, FGB and FGG in host lung epithelial cells.
CC Induces apoptosis in cell culture. Downregulates the type 1 interferon
CC receptor by inducing serine phosphorylation within the IFN alpha-
CC receptor subunit 1 (IFNAR1) degradation motif and increasing IFNAR1
CC ubiquitination. {ECO:0000250|UniProtKB:P59632}.
CC -!- SUBUNIT: Homotetramer composed of two homodimers linked non covalently.
CC Interacts with M, S and E proteins. Also interacts with the accessory
CC protein 7a. {ECO:0000250|UniProtKB:P59632}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P59632}. Host Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:P59632}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P59632}. Host cell membrane
CC {ECO:0000250|UniProtKB:P59632}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P59632}. Secreted
CC {ECO:0000250|UniProtKB:P59632}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P59632}. Note=The cell surface expressed protein
CC can undergo endocytosis. The protein is secreted in association with
CC membranous structures. {ECO:0000250|UniProtKB:P59632}.
CC -!- DOMAIN: The second or the third transmembrane region are responsible
CC for Golgi localization. {ECO:0000250|UniProtKB:P59632}.
CC -!- PTM: Exists in both O-glycosylated and non-glycosylated forms. The
CC glycosylated form is associated with the virion.
CC {ECO:0000250|UniProtKB:P59632}.
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DR EMBL; MN908947; QHD43417.1; -; Genomic_RNA.
DR RefSeq; YP_009724391.1; NC_045512.2.
DR PDB; 6XDC; EM; 2.90 A; A/B=1-275.
DR PDBsum; 6XDC; -.
DR SMR; P0DTC3; -.
DR BioGRID; 4383868; 367.
DR IntAct; P0DTC3; 367.
DR GlyGen; P0DTC3; 2 sites.
DR GeneID; 43740569; -.
DR Proteomes; UP000464024; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma 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:0005216; F:ion channel activity; IEA:InterPro.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:InterPro.
DR InterPro; IPR024407; Protein_3a_bCoV.
DR Pfam; PF11289; bCoV_viroporin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Host cell membrane; Host cytoplasm;
KW Host Golgi apparatus; Host membrane; Membrane; Reference proteome;
KW Secreted; Transmembrane; Transmembrane helix; Virion.
FT CHAIN 1..275
FT /note="ORF3a protein"
FT /id="PRO_0000449650"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 133
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250|UniProtKB:P59632"
FT CARBOHYD 32
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P59632"
FT CARBOHYD 34
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT HELIX 44..60
FT /evidence="ECO:0000244|PDB:6XDC"
FT HELIX 68..99
FT /evidence="ECO:0000244|PDB:6XDC"
FT HELIX 103..133
FT /evidence="ECO:0000244|PDB:6XDC"
FT HELIX 137..140
FT /evidence="ECO:0000244|PDB:6XDC"
FT STRAND 144..148
FT /evidence="ECO:0000244|PDB:6XDC"
FT STRAND 158..160
FT /evidence="ECO:0000244|PDB:6XDC"
FT STRAND 165..172
FT /evidence="ECO:0000244|PDB:6XDC"
FT STRAND 183..186
FT /evidence="ECO:0000244|PDB:6XDC"
FT STRAND 189..192
FT /evidence="ECO:0000244|PDB:6XDC"
FT STRAND 199..204
FT /evidence="ECO:0000244|PDB:6XDC"
FT STRAND 209..218
FT /evidence="ECO:0000244|PDB:6XDC"
FT HELIX 220..223
FT /evidence="ECO:0000244|PDB:6XDC"
FT STRAND 228..235
FT /evidence="ECO:0000244|PDB:6XDC"
SQ SEQUENCE 275 AA; 31123 MW; 4688E6D477E031C4 CRC64;
MDLFMRIFTI GTVTLKQGEI KDATPSDFVR ATATIPIQAS LPFGWLIVGV ALLAVFQSAS
KIITLKKRWQ LALSKGVHFV CNLLLLFVTV YSHLLLVAAG LEAPFLYLYA LVYFLQSINF
VRIIMRLWLC WKCRSKNPLL YDANYFLCWH TNCYDYCIPY NSVTSSIVIT SGDGTTSPIS
EHDYQIGGYT EKWESGVKDC VVLHSYFTSD YYQLYSTQLS TDTGVEHVTF FIYNKIVDEP
EEHVQIHTID GSSGVVNPVM EPIYDEPTTT TSVPL
//