AP3A_SARS
ID AP3A_SARS Reviewed; 274 AA.
AC P59632; Q7T6R6; Q7TA10; Q7TA18; Q7TFB0; Q7TLD0; Q80BV5;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=ORF3a protein;
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 (SARS-CoV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=694009;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9675; Paguma larvata (Masked palm civet).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Urbani;
RX PubMed=12730500; DOI=10.1126/science.1085952;
RA Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R.,
RA Icenogle J.P., Penaranda S., Bankamp B., Maher K., Chen M.-H., Tong S.,
RA Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D., Erdman D.D.,
RA Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E., Sanchez A., Liffick S.,
RA Holloway B., Limor J., McCaustland K., Olsen-Rasmussen M., Fouchier R.,
RA Guenther S., Osterhaus A.D.M.E., Drosten C., Pallansch M.A., Anderson L.J.,
RA Bellini W.J.;
RT "Characterization of a novel coronavirus associated with severe acute
RT respiratory syndrome.";
RL Science 300:1394-1399(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Tor2;
RX PubMed=12730501; DOI=10.1126/science.1085953;
RA Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A.,
RA Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y.,
RA Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L., Leach S.R.,
RA Mayo M., McDonald H., Montgomery S.B., Pandoh P.K., Petrescu A.S.,
RA Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E., Stott J.M.,
RA Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N., Bernard K.,
RA Booth T.F., Bowness D., Czub M., Drebot M., Fernando L., Flick R.,
RA Garbutt M., Gray M., Grolla A., Jones S., Feldmann H., Meyers A.,
RA Kabani A., Li Y., Normand S., Stroher U., Tipples G.A., Tyler S.,
RA Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M., Petric M.,
RA Skowronski D.M., Upton C., Roper R.L.;
RT "The genome sequence of the SARS-associated coronavirus.";
RL Science 300:1399-1404(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate CUHK-Su10, and Isolate CUHK-W1;
RX PubMed=12853594; DOI=10.1056/nejm200307103490216;
RA Tsui S.K.W., Chim S.S.C., Lo Y.M.D.;
RT "Coronavirus genomic-sequence variations and the epidemiology of the severe
RT acute respiratory syndrome.";
RL N. Engl. J. Med. 349:187-188(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU-39849;
RX PubMed=12876307; DOI=10.1177/15353702-0322807-13;
RA Zeng F.Y., Chan C.W., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C.C.,
RA Hui R.K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B.,
RA Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.;
RT "The complete genome sequence of severe acute respiratory syndrome
RT coronavirus strain HKU-39849 (HK-39).";
RL Exp. Biol. Med. 228:866-873(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, and
RC Isolate GD01;
RA Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W., Jiang T.,
RA Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y., Li X., Lu F.,
RA Tan G., Yang R., Cao W.S., Wang J., Chen W., Cong L., Deng Y., Dong W.,
RA Han Y., Hu W., Lei M., Li C., Li G., Li G., Li H., Li S., Li S., Li W.,
RA Li W., Lin W., Liu J., Liu Z., Lu H., Ni P., Qi Q., Sun Y., Tang L.,
RA Tong Z., Wang J., Wang X., Wu Q., Xi Y., Xu Z., Yang L., Ye C., Ye J.,
RA Zhang B., Zhang F., Zhang J., Zhang X., Zhou J., Yang H.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate TW1;
RA Yeh S.-H., Kao C.-L., Tsai C.-Y., Liu C.-J., Chen D.-S., Chen P.-J.;
RT "The complete genome of SARS coronavirus clone TW1.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate FRA;
RA Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K., Censini S.,
RA Guidotti S., Masignani V., Scarselli M., Mora M., Donati C., Han J.,
RA Song H.C., Abrignani S., Covacci A., Rappuoli R.;
RT "SARS virus is a close relative of type II coronaviruses.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Frankfurt 1;
RA Thiel V., Hertzig T., Putics A., Ivanov K.A., Schelle B., Bayer S.,
RA Scheiner B., Weinand H., Weissbrich B., Ziebuhr J.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Taiwan TC1, Isolate Taiwan TC2, and Isolate Taiwan TC3;
RA Chang J.-G.C., Lin T.-H., Chen C.-M., Lin C.-S., Chan W.-L., Shih M.-C.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate TWH, Isolate TWJ, Isolate TWK, Isolate TWS, and Isolate TWY;
RA Shu H.Y., Wu K.M., Tsai S.F.;
RT "The complete genome of SARS coronavirus TWH.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HSR 1;
RA Canducci F., Clementi M., Poli G., Vicenzi E.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate AS;
RA Balotta C., Corvasce S., Violin M., Galli M., Moroni M., Vigevani G.M.,
RA Ruan Y.J., Salemi M.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Shanghai QXC1;
RA Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
RT "Analysis of SARS coronavirus genome in Shanghai isolates.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-125.
RC STRAIN=Isolate Shanghai LY;
RA Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP IDENTIFICATION.
RX PubMed=15135062; DOI=10.1016/j.febslet.2004.03.086;
RA Yu C.-J., Chen Y.-C., Hsiao C.-H., Kuo T.-C., Chang S.C., Lu C.-Y.,
RA Wei W.-C., Lee C.-H., Huang L.-M., Chang M.-F., Ho H.-N., Lee F.-J.S.;
RT "Identification of a novel protein 3a from severe acute respiratory
RT syndrome coronavirus.";
RL FEBS Lett. 565:111-116(2004).
RN [16]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH M PROTEIN; E PROTEIN;
RP SPIKE GLYCOPROTEIN AND ACCESSORY PROTEIN 7A.
RX PubMed=15194747; DOI=10.1128/jvi.78.13.6723-6734.2004;
RA Tan Y.-J., Teng E., Shen S., Tan T.H.P., Goh P.-Y., Fielding B.C.,
RA Ooi E.-E., Tan H.-C., Lim S.G., Hong W.;
RT "A novel severe acute respiratory syndrome coronavirus protein, U274, is
RT transported to the cell surface and undergoes endocytosis.";
RL J. Virol. 78:6723-6734(2004).
RN [17]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH M AND E PROTEINS.
RX PubMed=15763150; DOI=10.1016/j.virusres.2005.01.001;
RA Yuan X., Li J., Shan Y., Yang Z., Zhao Z., Chen B., Yao Z., Dong B.,
RA Wang S., Chen J., Cong Y.;
RT "Subcellular localization and membrane association of SARS-CoV 3a
RT protein.";
RL Virus Res. 109:191-202(2005).
RN [18]
RP CHARACTERIZATION.
RX PubMed=15781262; DOI=10.1016/j.bbrc.2005.02.153;
RA Shen S., Lin P.S., Chao Y.C., Zhang A., Yang X., Lim S.G., Hong W.,
RA Tan Y.J.;
RT "The severe acute respiratory syndrome coronavirus 3a is a novel structural
RT protein.";
RL Biochem. Biophys. Res. Commun. 330:286-292(2005).
RN [19]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=15709039; DOI=10.1128/jvi.79.5.3182-3186.2005;
RA Ito N., Mossel E.C., Narayanan K., Popov V.L., Huang C., Inoue T.,
RA Peters C.J., Makino S.;
RT "Severe acute respiratory syndrome coronavirus 3a protein is a viral
RT structural protein.";
RL J. Virol. 79:3182-3186(2005).
RN [20]
RP FUNCTION.
RX PubMed=16014971; DOI=10.1128/jvi.79.15.10083-10087.2005;
RA Tan Y.J., Tham P.Y., Chan D.Z., Chou C.-F., Shen S., Fielding B.C.,
RA Tan T.H., Lim S.G., Hong W.;
RT "The severe acute respiratory syndrome coronavirus 3a protein up-regulates
RT expression of fibrinogen in lung epithelial cells.";
RL J. Virol. 79:10083-10087(2005).
RN [21]
RP FUNCTION.
RX PubMed=15958670; DOI=10.1099/vir.0.80813-0;
RA Law P.T., Wong C.H., Au T.C., Chuck C.P., Kong S.K., Chan P.K., To K.F.,
RA Lo A.W., Chan J.Y., Suen Y.K., Chan H.Y., Fung K.P., Waye M.M., Sung J.J.,
RA Lo Y.M.D., Tsui S.K.W.;
RT "The 3a protein of severe acute respiratory syndrome-associated coronavirus
RT induces apoptosis in Vero E6 cells.";
RL J. Gen. Virol. 86:1921-1930(2005).
RN [22]
RP GLYCOSYLATION, AND MUTAGENESIS OF SER-27; THR-28; THR-32 AND THR-34.
RX PubMed=16474139; DOI=10.1128/jvi.80.5.2326-2336.2006;
RA Oostra M., de Haan C.A., de Groot R.J., Rottier P.J.M.;
RT "Glycosylation of the severe acute respiratory syndrome coronavirus triple-
RT spanning membrane proteins 3a and M.";
RL J. Virol. 80:2326-2336(2006).
RN [23]
RP SUBCELLULAR LOCATION.
RX PubMed=16352545; DOI=10.1128/jvi.80.1.210-217.2006;
RA Huang C., Narayanan K., Ito N., Peters C.J., Makino S.;
RT "Severe acute respiratory syndrome coronavirus 3a protein is released in
RT membranous structures from 3a protein-expressing cells and infected
RT cells.";
RL J. Virol. 80:210-217(2006).
RN [24]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-81; CYS-117; CYS-121; CYS-127;
RP CYS-130; CYS-133; CYS-148 AND CYS-157.
RX PubMed=16894145; DOI=10.1073/pnas.0605402103;
RA Lu W., Zheng B.-J., Xu K., Schwarz W., Du L., Wong C.K.L., Chen J.,
RA Duan S., Deubel V., Sun B.;
RT "Severe acute respiratory syndrome-associated coronavirus 3a protein forms
RT an ion channel and modulates virus release.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12540-12545(2006).
RN [25]
RP FUNCTION.
RX PubMed=20020050; DOI=10.1371/journal.pone.0008342;
RA Minakshi R., Padhan K., Rani M., Khan N., Ahmad F., Jameel S.;
RT "The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and
RT induces ligand-independent downregulation of the type 1 interferon
RT receptor.";
RL PLoS ONE 4:E8342-E8342(2009).
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. {ECO:0000269|PubMed:15958670,
CC ECO:0000269|PubMed:16014971, ECO:0000269|PubMed:16894145,
CC ECO:0000269|PubMed:20020050}.
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:0000269|PubMed:15194747, ECO:0000269|PubMed:15763150,
CC ECO:0000269|PubMed:16894145}.
CC -!- INTERACTION:
CC P59632; P59632: 3a; NbExp=3; IntAct=EBI-15595051, EBI-15595051;
CC P59632; P59596: M; NbExp=2; IntAct=EBI-15595051, EBI-25487824;
CC P59632; PRO_0000037310 [P0C6X7]: rep; NbExp=2; IntAct=EBI-15595051, EBI-25474098;
CC P59632; P33724: CAV1; Xeno; NbExp=5; IntAct=EBI-15595051, EBI-79998;
CC -!- SUBCELLULAR LOCATION: Virion. Host Golgi apparatus membrane; Multi-pass
CC membrane protein. Host cell membrane; Multi-pass membrane protein.
CC Secreted. Host cytoplasm. Note=The cell surface expressed protein can
CC undergo endocytosis. The protein is secreted in association with
CC membranous structures.
CC -!- DOMAIN: The second or the third transmembrane region are responsible
CC for Golgi localization.
CC -!- PTM: Exists in both O-glycosylated and non-glycosylated forms. The
CC glycosylated form is associated with the virion.
CC {ECO:0000269|PubMed:16474139}.
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DR EMBL; AY278741; AAP13446.1; -; Genomic_RNA.
DR EMBL; AY274119; AAP41038.1; -; Genomic_RNA.
DR EMBL; AY282752; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278554; AAP13568.1; -; Genomic_RNA.
DR EMBL; AY278491; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278487; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278488; AAP30031.1; -; Genomic_RNA.
DR EMBL; AY278489; AAP51228.1; -; Genomic_RNA.
DR EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY291451; AAP37018.1; -; Genomic_RNA.
DR EMBL; AY310120; AAP50486.1; -; Genomic_RNA.
DR EMBL; AY291315; AAP33698.1; -; Genomic_RNA.
DR EMBL; AY338174; AAQ01598.1; -; Genomic_RNA.
DR EMBL; AY338175; AAQ01610.1; -; Genomic_RNA.
DR EMBL; AY348314; AAP97883.1; -; Genomic_RNA.
DR EMBL; AP006557; BAC81349.1; -; Genomic_RNA.
DR EMBL; AP006558; BAC81363.1; -; Genomic_RNA.
DR EMBL; AP006559; BAC81377.1; -; Genomic_RNA.
DR EMBL; AP006560; BAC81391.1; -; Genomic_RNA.
DR EMBL; AP006561; BAC81405.1; -; Genomic_RNA.
DR EMBL; AY323977; AAP72975.1; -; Genomic_RNA.
DR EMBL; AY427439; AAQ94061.1; -; Genomic_RNA.
DR EMBL; AY463059; AAP82984.2; -; Genomic_RNA.
DR EMBL; AY322207; AAP82969.1; -; Genomic_RNA.
DR RefSeq; NP_828852.2; NC_004718.3.
DR SMR; P59632; -.
DR BioGRID; 4383917; 67.
DR ComplexPortal; CPX-6095; SARS-CoV 3a complex.
DR DIP; DIP-61251N; -.
DR IntAct; P59632; 56.
DR MINT; P59632; -.
DR TCDB; 1.A.57.1.1; the human sars coronavirus viroporin (sars-vp).
DR GlyGen; P59632; 4 sites.
DR iPTMnet; P59632; -.
DR PRIDE; P59632; -.
DR GeneID; 1489669; -.
DR Reactome; R-HSA-9678110; Attachment and Entry.
DR Reactome; R-HSA-9679509; Virion Assembly and Release.
DR Reactome; R-HSA-9683673; Maturation of protein 3a.
DR Reactome; R-HSA-9683701; Translation of Structural Proteins.
DR Reactome; R-HSA-9686347; Microbial modulation of RIPK1-mediated regulated necrosis.
DR Reactome; R-HSA-9767675; SARS-CoV-1-host interactions.
DR SIGNOR; P59632; -.
DR Proteomes; UP000000354; Genome.
DR Proteomes; UP000103670; Genome.
DR Proteomes; UP000109640; Genome.
DR Proteomes; UP000116947; Genome.
DR Proteomes; UP000121636; Genome.
DR Proteomes; UP000131569; Genome.
DR Proteomes; UP000131955; Genome.
DR Proteomes; UP000137377; Genome.
DR Proteomes; UP000138690; Genome.
DR Proteomes; UP000143093; Genome.
DR Proteomes; UP000145651; Genome.
DR Proteomes; UP000146108; Genome.
DR Proteomes; UP000146181; Genome.
DR Proteomes; UP000146296; Genome.
DR Proteomes; UP000148194; Genome.
DR Proteomes; UP000153467; Genome.
DR Proteomes; UP000160648; Genome.
DR Proteomes; UP000164441; Genome.
DR Proteomes; UP000172416; Genome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0055036; C:virion membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IPI:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:ComplexPortal.
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 GO; GO:0039511; P:suppression by virus of host interferon receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; 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 1: Evidence at protein level;
KW Apoptosis; Glycoprotein; Host cell membrane; Host cytoplasm;
KW Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon receptors by virus;
KW Inhibition of host interferon signaling pathway by virus; Ion channel;
KW Ion transport; Membrane; Reference proteome; Secreted; Transmembrane;
KW Transmembrane helix; Transport; Viral immunoevasion; Viral ion channel;
KW Virion.
FT CHAIN 1..274
FT /note="ORF3a protein"
FT /id="PRO_0000106131"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:15194747"
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:0000305|PubMed:15194747"
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 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:0000305|PubMed:16474139"
FT CARBOHYD 32
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000305|PubMed:16474139"
FT CARBOHYD 34
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT VARIANT 11
FT /note="G -> R (in strain: Isolate Tor2, Isolate BJ02 and
FT Isolate BJ03)"
FT VARIANT 20
FT /note="I -> T (in strain: Isolate Shanghai LY)"
FT VARIANT 29
FT /note="V -> A (in strain: Isolate Shanghai QXC1)"
FT VARIANT 101
FT /note="M -> K (in strain: Isolate HKU-39849)"
FT VARIANT 129
FT /note="L -> F (in strain: Isolate TWK)"
FT VARIANT 136
FT /note="K -> Q (in strain: Isolate BJ01)"
FT VARIANT 171
FT /note="E -> A (in strain: Isolate GD01)"
FT VARIANT 193
FT /note="R -> W (in strain: Isolate GD01)"
FT VARIANT 222
FT /note="D -> N (in strain: Isolate Shanghai QXC1)"
FT MUTAGEN 27
FT /note="S->G: Complete loss of O-glycosylation; when
FT associated with A-28; A-32 and A-34."
FT /evidence="ECO:0000269|PubMed:16474139"
FT MUTAGEN 28
FT /note="T->A: Complete loss of O-glycosylation; when
FT associated with A-27; A-32 and A-34."
FT /evidence="ECO:0000269|PubMed:16474139"
FT MUTAGEN 32
FT /note="T->A: Complete loss of O-glycosylation; when
FT associated with A-27; A-28 and A-34."
FT /evidence="ECO:0000269|PubMed:16474139"
FT MUTAGEN 34
FT /note="T->A: Complete loss of O-glycosylation; when
FT associated with A-27; A-28 and A-32."
FT /evidence="ECO:0000269|PubMed:16474139"
FT MUTAGEN 81
FT /note="C->A: No effect on polymerization."
FT /evidence="ECO:0000269|PubMed:16894145"
FT MUTAGEN 117
FT /note="C->A: No effect on polymerization."
FT /evidence="ECO:0000269|PubMed:16894145"
FT MUTAGEN 121
FT /note="C->A: No effect on polymerization."
FT /evidence="ECO:0000269|PubMed:16894145"
FT MUTAGEN 127
FT /note="C->A: No effect on polymerization."
FT /evidence="ECO:0000269|PubMed:16894145"
FT MUTAGEN 130
FT /note="C->A: No effect on polymerization."
FT /evidence="ECO:0000269|PubMed:16894145"
FT MUTAGEN 133
FT /note="C->A: Almost complete loss of polymerization
FT ability."
FT /evidence="ECO:0000269|PubMed:16894145"
FT MUTAGEN 148
FT /note="C->A: No effect on polymerization."
FT /evidence="ECO:0000269|PubMed:16894145"
FT MUTAGEN 157
FT /note="C->A: No effect on polymerization."
FT /evidence="ECO:0000269|PubMed:16894145"
SQ SEQUENCE 274 AA; 30903 MW; E48C7D44A4DE34FE CRC64;
MDLFMRFFTL GSITAQPVKI DNASPASTVH ATATIPLQAS LPFGWLVIGV AFLAVFQSAT
KIIALNKRWQ LALYKGFQFI CNLLLLFVTI YSHLLLVAAG MEAQFLYLYA LIYFLQCINA
CRIIMRCWLC WKCKSKNPLL YDANYFVCWH THNYDYCIPY NSVTDTIVVT EGDGISTPKL
KEDYQIGGYS EDRHSGVKDY VVVHGYFTEV YYQLESTQIT TDTGIENATF FIFNKLVKDP
PNVQIHTIDG SSGVANPAMD PIYDEPTTTT SVPL
