CAPSD_SMSV4
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 02-JUN-2021, entry version 75.
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 4 (SMSV-4) (SMSV serotype 4).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Vesivirus.
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]
RP X-RAY CRYSTALLOGRAPHY (3.2 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 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}.
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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 PDBsum; 2GH8; -.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host cytoplasm;
KW T=3 icosahedral capsid protein; Virion.
FT PROPEP 1..152
FT /evidence="ECO:0000250"
FT /id="PRO_0000036884"
FT CHAIN 153..702
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036885"
FT SITE 152..153
FT /note="Cleavage; by calicivirin"
FT /evidence="ECO:0000250"
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"
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
