ID CAPSD_SMSV4 Reviewed; 703 AA. AC P36285; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 10-JUN-2026, entry version 80. DE RecName: Full=Capsid protein VP1; DE Short=CP; DE AltName: Full=Capsid protein; DE AltName: Full=Coat protein; DE Contains: DE RecName: Full=Capsid leader protein {ECO:0000250|UniProtKB:Q66915}; DE Short=LC {ECO:0000250|UniProtKB:Q66915}; DE Contains: DE RecName: Full=Mature capsid protein; GN ORFNames=ORF2; OS San Miguel sea lion virus serotype 4 (SMSV-4) (SMSV serotype 4). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Caliciviridae; Vesivirus; Vesivirus exanthema; OC Vesicular exanthema of swine virus. OX NCBI_TaxID=36407; 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). RN [2] {ECO:0007744|PDB:2GH8} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 153-703. RX PubMed=16702551; DOI=10.1073/pnas.0600421103; RA Chen R., Neill J.D., Estes M.K., Prasad B.V.V.; RT "X-ray structure of a native calicivirus: structural insights into RT antigenic diversity and host specificity."; RL Proc. Natl. Acad. Sci. U.S.A. 103:8048-8053(2006). 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 encapsulates the genomic RNA and is decorated with VP2 CC proteins. {ECO:0000250|UniProtKB:P27406}. CC -!- SUBUNIT: Homodimer (By similarity). Homomultimer (By similarity). CC Interacts with the minor capsid protein VP2 (By similarity). May bind CC to VP3 and Vpg proteins. {ECO:0000250|UniProtKB:P27406, CC ECO:0000250|UniProtKB:Q83884}. CC -!- SUBCELLULAR LOCATION: [Mature capsid protein]: Virion CC {ECO:0000250|UniProtKB:Q66915}. Host cytoplasm. CC -!- PTM: [Capsid protein VP1]: Cleaved by the viral protease to produce CC mature capsid protein. {ECO:0000250|UniProtKB:P27406}. 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; M87482; AAA16220.1; -; Unassigned_RNA. DR PIR; C48562; C48562. DR PDB; 2GH8; X-ray; 3.20 A; A/B/C=153-703. DR SMR; P36285; -. DR DIP; DIP-61173N; -. DR EvolutionaryTrace; P36285; -. 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. DR PDBsum; 2GH8; -. PE 1: Evidence at protein level; KW 3D-structure; Capsid protein; Host cytoplasm; KW T=3 icosahedral capsid protein; Virion. FT CHAIN 1..703 FT /note="Capsid protein VP1" FT /id="PRO_0000460238" FT CHAIN 1..152 FT /note="Capsid leader protein" FT /id="PRO_0000460239" FT CHAIN 153..702 FT /note="Mature capsid protein" FT /evidence="ECO:0000250" FT /id="PRO_0000036885" FT SITE 152..153 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000250|UniProtKB:Q66915" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 178..189 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 196..198 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 202..213 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 218..223 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 230..235 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 236..238 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 239..243 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 246..253 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 261..267 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 277..280 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 285..288 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 295..299 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 304..309 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 317..320 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 332..341 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 375..382 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 385..388 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 390..393 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 405..409 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 416..422 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 429..438 FT /evidence="ECO:0007829|PDB:2GH8" FT TURN 468..470 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 479..481 FT /evidence="ECO:0007829|PDB:2GH8" FT TURN 485..488 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 490..498 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 508..512 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 519..526 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 528..533 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 542..547 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 550..564 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 568..570 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 576..578 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 587..589 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 594..600 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 603..610 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 615..620 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 621..629 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 638..645 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 647..649 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 651..656 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 662..665 FT /evidence="ECO:0007829|PDB:2GH8" FT STRAND 678..686 FT /evidence="ECO:0007829|PDB:2GH8" FT HELIX 690..692 FT /evidence="ECO:0007829|PDB:2GH8" SQ SEQUENCE 703 AA; 77721 MW; C5DAD8223B261073 CRC64; MATTHTLLSF DDLEFLLHRK DLTDLYGERC GTLNLVINPY ELFLPDELDD DCCDDPFNCC FPDVYASIGT EYSYIDPPEL IHEEHCATNG TWPNGDPCEP ILPPFTITGT HHYYATKPGE VVSGILSKLG SSWDPSLRST ADVSNSFTFR AESDGPGSAE IVTEEQGTVV QQQPAPAPTA LATLATASTG KSVEQEWMTF FSYHTSINWS TVESQGKILY SQALNPSINP YLDHIAKLYS TWSGGIDVRF TVSGSGVFGG KLAALLVPPG VEPIESVSML QYPHVLFDAR QTEPVIFTIP DIRKTLFHSM DETDTTKLVI NPYENGVENK TTCSITVETR PSADFTFALL KPPGSLIKHG SIPSDLIPRN SAHWMGNRWW STISGFSVQP RVFQSNRHFD FDSTTTGWST PYYVPIEIKI QGKVGSNNKW FHVIDTDKAL VPGIPDGWPD TTIPDETKAT NGNFSYGESY RAGSTTIKPN ENSTHFKGTY ICGTLSTVEI PENDEQQIKT EAEKKSQTMY VVTADFKDTI VKPQHKISPQ KLVVYFDGPE KDLTMSATLS PLGYTLVDEQ PVGSVSSRVV RIATLPEAFT QGGNYPIFYV NKIKVGYFDR ATTNCYNSQI LMTSQRLAEG NYNLPPDSLA VYRITDSSSQ WFDIGINHDG FSYVGLSDLP NDLSFPLTST FMGVQLARVK LASKVKAHTI TAK //