AP3A_BCRP3
ID AP3A_BCRP3 Reviewed; 274 AA.
AC Q3I5J4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 23-FEB-2022, entry version 77.
DE RecName: Full=Protein 3;
DE AltName: Full=Accessory protein 3;
GN ORFNames=3;
OS Bat coronavirus Rp3/2004 (BtCoV/Rp3/2004) (SARS-like coronavirus Rp3).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=349344;
OH NCBI_TaxID=59479; Rhinolophus ferrumequinum (Greater horseshoe bat).
OH NCBI_TaxID=196889; Rhinolophus macrotis (Big-eared horseshoe bat).
OH NCBI_TaxID=188571; Rhinolophus pearsonii.
OH NCBI_TaxID=89399; Rhinolophus sinicus (Chinese rufous horseshoe bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16195424; DOI=10.1126/science.1118391;
RA Li W., Shi Z., Yu M., Ren W., Smith C., Epstein J.H., Wang H., Crameri G.,
RA Hu Z., Zhang H., Zhang J., McEachern J., Field H., Daszak P., Eaton B.T.,
RA Zhang S., Wang L.F.;
RT "Bats are natural reservoirs of SARS-like coronaviruses.";
RL Science 310:676-679(2005).
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. Down-regulates 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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host Golgi apparatus
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host
CC cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Secreted {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=The cell
CC surface expressed protein can undergo endocytosis. The protein is
CC secreted in association with membranous structures (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The second or the third transmembrane region are responsible
CC for Golgi localization. {ECO:0000250}.
CC -!- PTM: Exists in both O-glycosylated and non-glycosylated forms. The
CC glycosylated form is associated with the virion (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Bat coronavirus rp3 is highly similar to SARS-CoV (SARS-
CC like).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ071615; AAZ67053.1; -; Genomic_RNA.
DR SMR; Q3I5J4; -.
DR Proteomes; UP000006570; 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:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR CDD; cd21648; SARS-CoV-like_ORF3a; 1.
DR InterPro; IPR024407; Protein_3a_bCoV.
DR Pfam; PF11289; bCoV_viroporin; 1.
DR PROSITE; PS51967; COV_VIROPORIN_3A_CD; 1.
DR PROSITE; PS51966; COV_VIROPORIN_3A_TM; 1.
PE 3: Inferred from homology;
KW Apoptosis; Glycoprotein; Host cell membrane; Host cytoplasm;
KW Host Golgi apparatus; Host membrane; Ion channel; Ion transport; Membrane;
KW Secreted; Transmembrane; Transmembrane helix; Transport; Viral ion channel;
KW Virion.
FT CHAIN 1..274
FT /note="Protein 3"
FT /id="PRO_0000106130"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 33..141
FT /note="CoV 3a-like viroporin TM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01311"
FT DOMAIN 145..237
FT /note="CoV 3a-like viroporin CD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01312"
FT SITE 133
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 34
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 274 AA; 30794 MW; AE17D810FD454594 CRC64;
MDLFMSIFTL GAITRQPAKI ENASPASTVH ATATIPLQAS LPFGWLVVGV ALLAVFQSAS
KVIALHKRWQ LALHKGIQLV CNLLLLFVTI YSHLLLLAAG MEAQFLYIYA LIYILQIVSF
CRFIMRCWLC WKCRSKNPLL YDANYFVCWH TNCFDYCIPY NSITDTIVLT SGDGTTQPKL
KEDYQIGGYS EDWHSGVKDY VVIHGYFTEV YYQLESTQLS TDTGAENATF FIYSKLVKDV
DHVQIHTIDG SSGVVNPAMD PIYDEPTTTT SVPL
