ID C6GHB7_9ALPC Unreviewed; 1465 AA.
AC C6GHB7;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-NOV-2024, entry version 47.
DE RecName: Full=Spike glycoprotein {ECO:0000256|HAMAP-Rule:MF_04200};
DE Short=S glycoprotein {ECO:0000256|HAMAP-Rule:MF_04200};
DE AltName: Full=E2 {ECO:0000256|HAMAP-Rule:MF_04200};
DE AltName: Full=Peplomer protein {ECO:0000256|HAMAP-Rule:MF_04200};
GN Name=S {ECO:0000256|HAMAP-Rule:MF_04200};
OS Feline coronavirus UU4.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus; Alphacoronavirus 1.
OX NCBI_TaxID=454952 {ECO:0000313|EMBL:ACT10887.1, ECO:0000313|Proteomes:UP000155736};
RN [1] {ECO:0000313|EMBL:ACT10887.1, ECO:0000313|Proteomes:UP000155736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UU4 {ECO:0000313|EMBL:ACT10887.1};
RA Spiro D., Halpin R., Wang S., Hostetler J., Hine E., Overton L.,
RA Tsitrin T., Katzel D., Sarmiento M., Sitz J., Amedeo P., Caler E.,
RA Lorenzi H., Schobel S., Sundaram J., Chang H.W., Egberink H.F.,
RA Rottier P.J.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:6JX7}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.31 ANGSTROMS) OF 16-1406, AND DISULFIDE
RP BONDS.
RX PubMed=31900356; DOI=10.1073/pnas.1908898117;
RA Yang T.J., Chang Y.C., Ko T.P., Draczkowski P., Chien Y.C., Chang Y.C.,
RA Wu K.P., Khoo K.H., Chang H.W., Hsu S.D.;
RT "Cryo-EM analysis of a feline coronavirus spike protein reveals a unique
RT structure and camouflaging glycans.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:1438-1446(2020).
CC -!- FUNCTION: S1 region attaches the virion to the cell membrane by
CC interacting with the host receptor, initiating the infection. Binding
CC to the receptor probably induces conformational changes in the S
CC glycoprotein unmasking the fusion peptide of S2 region and activating
CC membranes fusion. S2 region belongs to the class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral and
CC target cell membrane fusion, the coiled coil regions (heptad repeats)
CC regions assume a trimer-of-hairpins structure, positioning the fusion
CC peptide in close proximity to the C-terminal region of the ectodomain.
CC The formation of this structure appears to drive apposition and
CC subsequent fusion of viral and target cell membranes.
CC {ECO:0000256|HAMAP-Rule:MF_04200}.
CC -!- SUBUNIT: Homotrimer. During virus morphogenesis, found in a complex
CC with M and HE proteins. Interacts with host receptor.
CC {ECO:0000256|HAMAP-Rule:MF_04200}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000256|ARBA:ARBA00034689, ECO:0000256|HAMAP-
CC Rule:MF_04200}; Single-pass type I membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_04200}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04200};
CC Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04200}.
CC Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC compartment, where it participates in virus particle assembly.
CC {ECO:0000256|HAMAP-Rule:MF_04200}.
CC -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval signal.
CC {ECO:0000256|HAMAP-Rule:MF_04200}.
CC -!- SIMILARITY: Belongs to the alphacoronaviruses spike protein family.
CC {ECO:0000256|HAMAP-Rule:MF_04200}.
CC -!- CAUTION: In contrast to serogroups 2 and 3, S glycoprotein from
CC serogroup 1 is not cleaved into S1 and S2. {ECO:0000256|HAMAP-
CC Rule:MF_04200}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04200}.
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DR EMBL; FJ938054; ACT10887.1; -; Genomic_RNA.
DR PDB; 6JX7; EM; 3.31 A; A/B/C=16-1406.
DR SMR; C6GHB7; -.
DR Proteomes; UP000155736; Genome.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:UniProtKB-UniRule.
DR CDD; cd22377; TGEV-like_Spike_SD1-2_S1-S2_S2; 1.
DR Gene3D; 1.20.5.300; -; 2.
DR Gene3D; 2.60.40.3130; -; 1.
DR HAMAP; MF_04200; ALPHA_CORONA_SPIKE; 1.
DR InterPro; IPR042552; ALPHA_CORONA_SPIKE.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR002551; Spike_S1_CoV.
DR InterPro; IPR002552; Spike_S2_CoV.
DR InterPro; IPR043614; Spike_S2_CoV_C.
DR InterPro; IPR044873; Spike_S2_CoV_HR1.
DR InterPro; IPR044874; Spike_S2_CoV_HR2.
DR Pfam; PF01600; CoV_S1; 1.
DR Pfam; PF19209; CoV_S1_C; 1.
DR Pfam; PF01601; CoV_S2; 1.
DR Pfam; PF19214; CoV_S2_C; 1.
DR SUPFAM; SSF111474; Coronavirus S2 glycoprotein; 2.
DR PROSITE; PS51923; COV_S2_HR1; 1.
DR PROSITE; PS51924; COV_S2_HR2; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6JX7};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_04200};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP-
KW Rule:MF_04200};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP-
KW Rule:MF_04200};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW Rule:MF_04200};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04200};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_04200};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_04200};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_04200};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804,
KW ECO:0000256|HAMAP-Rule:MF_04200};
KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879, ECO:0000256|HAMAP-
KW Rule:MF_04200};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04200};
KW Virulence {ECO:0000256|ARBA:ARBA00023026, ECO:0000256|HAMAP-Rule:MF_04200};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296,
KW ECO:0000256|HAMAP-Rule:MF_04200}.
FT TRANSMEM 1407..1426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1055..1174
FT /note="Coronavirus spike (S) glycoprotein S2 subunit heptad
FT repeat 1 (HR1) region profile"
FT /evidence="ECO:0000259|PROSITE:PS51923"
FT DOMAIN 1319..1418
FT /note="Coronavirus spike (S) glycoprotein S2 subunit heptad
FT repeat 2 (HR2) region profile"
FT /evidence="ECO:0000259|PROSITE:PS51924"
FT REGION 1041..1061
FT /note="Fusion peptide"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04200"
FT COILED 1122..1166
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04200"
FT COILED 1354..1396
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04200"
FT MOTIF 1461..1465
FT /note="KxHxx"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04200"
FT DISULFID 155..178
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 269..274
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 322..344
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 387..415
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 501..510
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 595..644
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 627..654
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 702..753
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 820..832
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 889..911
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 894..900
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 1003..1014
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 1205..1216
FT /evidence="ECO:0007829|PDB:6JX7"
FT DISULFID 1255..1302
FT /evidence="ECO:0007829|PDB:6JX7"
SQ SEQUENCE 1465 AA; 163564 MW; 21CD6A6101807C9B CRC64;
MILLILALLS IASSEDAPHG VTLPHFNTSH NNSKFELNFY NFLQTWDIPP NTETILGGYL
PYCDHEDNCG WYNFVYNNKV GPNAKYSYIN TQNLNIPNVH GVYFDVREHN SDGVWDQIDR
VGLLIAIHGT SHYSLLMVLQ DGVEASQPHV AVKICHWNPG NISTYHQFDV NLGDGGQCVF
NQRFSLDTVL TANDFYGFQW TDTYVDIYLG GTITKVWVVN DWSVVEASIS SHWNALNYGY
YIQFVNRTTY YAYNSTGGSN YTHLQLTECH TDYCAGYAKN VFVPIDGKIP EGFSFSNWFL
LTDKSTLVQG RVLSSQPVFV QCLRPVPTWS NNTAVVHFKN DVFCPNVTAD VLRFNLNFSD
TDVYTDSTTD DQLHFTFEDN TTASITCYSS ANVTDNQPAS GSISHTPFVS NSYLCFANFS
HSSVSRQFLG ILPPTVREFA FGRDGSIFVN GYKYFSLQPI KSVNFSISSV ENYGFWTIAY
TNYTDVMVDV NGTVITRLFY CDSPLNRIKC QQLKHELPDG FYSASMLVKK DLPKTFVTMP
QFYNWMNVTL HVVLNDIEKK ADIILAGAPE LASLADIHFE IAQANGSVVN VTSVCVQARQ
LALFYKYTSL QGLYTYSNLV QLQNYDCPFS PQQFNNYLQF ETLCFDVSPA VAGCKWSLVH
DVKWRTQFAT ITVSYKDGAM ITTMPKAQLG FQDISNIVKD ECTDYNIYGF QGTGIIRSTT
SRLVAGLYYT SASGDLLGFK ISTTGEIFTV VPCDLTAQAA VINDEIVGAI TATNQTDLFE
FVNHTWSRSA RGSSPSTVNT YTMPQFYYIT KWNNGTSSNC TSVITYSSFA ICNTGEIKYV
NVTHVEIVDD SVGVIKPVST GNITIPKNFT VAVQAEYVQI QVKPVAVDCA KYVCNGNRHC
LNLLTQYTSA CQTIENSLNL GARLESLMLN DMITVSDRSL EFATVDKFNT TALGGEKLGG
LYFDGLSSLL PPRVGMRSAV EDLLFNKVVT SGLGTVDDDY KKCSAGTDVA DLVCAQYYNG
IMVLPGVVDY NKMAMYTASL IGGMALGSIT SAVAVPFSMQ VQARLNYVAL QTDVLQENQK
ILANAFNNAI GNITLALGKV SNAITTVSDG FNSMASALTK IQSVVNQQGE ALSHLISQLQ
KNFQAISSSI AEIYNRLEKV EADAQVDRLI TGRLAALNAY VAQTLTQYAE VKASRQLAME
KVNECVKSQS DRYGFCGNGT HLFSLVNSAP DGLLFFHTVL LPTEWEEVTA WSGICVNDTY
AYLLKDFDHS IFSYNGTYMV TPRNMFQPRK PQMSDFVQIT SCEVTFLNTT HTTFQEIVID
YIDINKTIAD MLEQYHSNYT TPELDLQLEI FNQTKLNLTA EIDQLEQRAD NLTNIAHELQ
QYIDNLNKTI VDLEWLNRIE TYVKWPWYVW LLIGLVVVFC IPLLLFCCLS TGCCGCFGCL
GSCCHSLCSR RQFESYEPIE KVHVH
//
