ID   CAPSD_SMSV1             Reviewed;         702 AA.
AC   P36284;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-NOV-2023, entry version 70.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
DE   AltName: Full=VP1;
DE   Flags: Precursor;
GN   ORFNames=ORF2;
OS   San Miguel sea lion virus serotype 1 (SMSV-1) (SMSV serotype 1).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Vesivirus;
OC   Vesicular exanthema of swine virus.
OX   NCBI_TaxID=36406;
OH   NCBI_TaxID=9702; Otariidae (fur seals & sea lions).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1529644; DOI=10.1016/0168-1702(92)90008-w;
RA   Neill J.D.;
RT   "Nucleotide sequence of the capsid protein gene of two serotypes of San
RT   Miguel sea lion virus: identification of conserved and non-conserved amino
RT   acid sequences among calicivirus capsid proteins.";
RL   Virus Res. 24:211-222(1992).
CC   -!- FUNCTION: Capsid protein self assembles to form an icosahedral capsid
CC       with a T=3 symmetry, about 38 nm in diameter, and consisting of 180
CC       capsid proteins. A smaller form of capsid with a diameter of 23 nm
CC       might be capsid proteins assembled as icosahedron with T=1 symmetry.
CC       The capsid encapsulate the genomic RNA and VP2 proteins. Attaches
CC       virion to target cells by binding to feline junctional adhesion
CC       molecule A (F11R) and/or to alpha-2,6-linked sialic acid. Once
CC       attached, the virion is endocytosed. Acidification of the endosome
CC       induces conformational change of capsid protein thereby injecting virus
CC       genomic RNA into host cytoplasm (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimerizes, then multimerizes. May bind to VP3 and Vpg
CC       proteins (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC   -!- PTM: Cleaved by virus calcivirin to produce mature capsid protein.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the caliciviridae capsid protein family.
CC       {ECO:0000305}.
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; M87481; AAA16217.1; -; Unassigned_DNA.
DR   PIR; A48562; A48562.
DR   SMR; P36284; -.
DR   Proteomes; UP000007224; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   CDD; cd00205; rhv_like; 1.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR004005; Calicivirus_coat.
DR   InterPro; IPR033703; Rhv-like.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF00915; Calici_coat; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host cytoplasm; T=3 icosahedral capsid protein; Virion.
FT   PROPEP          1..152
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036882"
FT   CHAIN           153..702
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036883"
FT   SITE            152..153
FT                   /note="Cleavage; by 3C-like protease"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   702 AA;  77850 MW;  E6E5A58523DEE3D7 CRC64;
     MATTHTLLSF DDLEFLLHKK DLTDLYGERC GTLNLVINPY DLFLPDDLDD DWCDDPFNCC
     FSDVYTSIGT EYSYIDPPDL IYEEHCATNG HWPDGTPCEP ILPPFVIEGT HHYYATKPGE
     AVSGILSKLG SAWDPDLQST VDTKPDFVFR AESDGPGGAD IVTEEQGTVV QQQPVPAQSA
     LTTLAAASTG KTVDCEWTTF FSYHTAVNWS TTEAQGKILF SRALSPELNP YLRHISSLYS
     TWSGGIDVRF TVSGSGVFGG KLAALIVPPG IEPVESPTML QYPHVLFDAR QTEPVIFTIP
     DIRKTLYHSM DDTDTTRLVI MVYNELINPY EQSEPKSSCS ITVETRPSSD FTFSLLKPPG
     SLLKHGSIPS DLIPRNSRHW MGNRWWSTID GFVVQPRVFQ SNRHFDFDST TTGWSTPYYI
     PIEVTLEKLD RGGQYFKVTD TEKSLVPGLP DGWPDTTIPT AMTASNGNYD YTVAEYRITN
     NGTHFKGFYI MGNLTTKVKG SDNLGETQQT SRTLFASVGN YKDQNTINPT HKITSNSLVV
     YDANNVSAAT AKTTTWHSTM SHLGYVLVDE SPVGSDSTKV VRIATLPEAF TNGGNFPVFF
     TNKIQIGHFD RAHTKCFNSQ VLMTSQKLAE NHYTLPPDSL LVYRITDAAS SWFDLGINHD
     GFSYVGISTI PELDFPLTFN LHGVQLAKVK LASKVKTSKT TI
//