ID   CAPSD_MEVA              Reviewed;         722 AA.
AC   P27437;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   23-FEB-2022, entry version 78.
DE   RecName: Full=Capsid protein VP1;
DE   AltName: Full=Coat protein VP1;
DE   Contains:
DE     RecName: Full=Capsid protein VP2;
DE     AltName: Full=Coat protein VP2;
OS   Mink enteritis virus (strain Abashiri) (MEV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC   Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX   NCBI_TaxID=10793;
OH   NCBI_TaxID=452646; Neovison vison (American mink) (Mustela vison).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2016597; DOI=10.1099/0022-1317-72-4-867;
RA   Kariatsumari T., Horiuchi M., Hama E., Yaguchi K., Ishigurio N., Goto H.,
RA   Shinagawa M.;
RT   "Construction and nucleotide sequence analysis of an infectious DNA clone
RT   of the autonomous parvovirus, mink enteritis virus.";
RL   J. Gen. Virol. 72:867-875(1991).
CC   -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC       with a T=1 symmetry, about 22 nm in diameter, and consisting of 60
CC       copies of two size variants of the capsid proteins, VP1 and VP2, which
CC       differ by the presence of an N-terminal extension in the minor protein
CC       VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are
CC       responsible for the attachment to host cell receptors. This attachment
CC       induces virion internalization predominantly through clathrin-dependent
CC       endocytosis. Binding to the host receptors also induces capsid
CC       rearrangements leading to surface exposure of VP1 N-terminus,
CC       specifically its phospholipase A2-like region and putative nuclear
CC       localization signal(s). VP1 N-terminus might serve as a lipolytic
CC       enzyme to breach the endosomal membrane during entry into host cell and
CC       might contribute to virus transport to the nucleus (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000305}.
CC   -!- DOMAIN: The N-terminus of VP1 is sequestered within the mature capsid.
CC       It contains a phospholipase A2-like region and putative nuclear
CC       localization signals.
CC   -!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; D00765; BAA00663.1; -; Genomic_DNA.
DR   PIR; B38350; VCPVME.
DR   SMR; P27437; -.
DR   Proteomes; UP000007717; Genome.
DR   GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.30.10; -; 1.
DR   InterPro; IPR016184; Capsid/spike_ssDNA_virus.
DR   InterPro; IPR001403; Parvovirus_coat.
DR   InterPro; IPR013607; Phospholipase_A2-like.
DR   InterPro; IPR036952; VP1/VP2.
DR   Pfam; PF00740; Parvo_coat; 1.
DR   Pfam; PF08398; Phospholip_A2_4; 1.
DR   SUPFAM; SSF88645; SSF88645; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW   Host-virus interaction; T=1 icosahedral capsid protein;
KW   Viral attachment to host cell; Viral penetration into host cytoplasm;
KW   Viral penetration via permeabilization of host membrane; Virion;
KW   Virus endocytosis by host; Virus entry into host cell.
FT   CHAIN           1..722
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000039415"
FT   CHAIN           139..722
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000039416"
FT   REGION          14..59
FT                   /note="Phospholipase A2-like"
FT                   /evidence="ECO:0000250"
FT   REGION          90..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   722 AA;  79823 MW;  9DADBCAB2EF9F622 CRC64;
     MCFFIGLVPP GYKYLGPGNS LDQGEPTNPS DAAAKEHDEA YAAYLRSGKN PYLYFSPADQ
     RFIDQTKDAT DWGGKIGHYF FRAKKAIAPV LTDTPDHPST SRPTKPTKRS KPPPHIFINL
     AKKKKAGAGQ VKRDNLAPMS DGAVQPDGGQ PAVRNERATG SGNGSGGGGG GGSGGVGIST
     GTFNNQTEFK FLENGWVEIT ANSSRLVHLN MPESENYKRV VVNNMDKTAV KGNMALDDTH
     VQIVTPWSLV DANAWGVWFN PGDWQLIVNT MSELHLVSFE QEIFNVVLKT VSESATQPPT
     KVYNNDLTAS LMVALDSNNT MPFTPAAMRS ETLGFYPWKP TIPTPWRYYF QWDRTLIPSH
     TGTSGTPTNI YHGTDPDDVQ FYTIENSVPV HLLRTGDEFA TGTFFFDCKP CRLTHTWQTN
     RALGLPPFLN SLPQSEGATN FGDIGVQQDK RRGVTQMGNT DYITEATIMR PAEVGYSAPY
     YSFEASTQGP FKTPIAAGRG GAQTDENQAA DGDPRYAFGR QHGQKTTTTG ETPERFTYIA
     HQDTGRYPAG DWIQNINFNL PVTNDNVLLP TDPIGGKTGI NYTNIFNTYG PLTALNNVPP
     VYPNGQIWDK EFDTDLKPRL HVNAPFVCQN NCPGQLFVKV APNLTNEYDP DASANMSRIV
     TYSDFWWKGK LVFKAKLRAS HTWNPIQQMS INVDNQFNYL PNNIGAMKIV YEKSQLAPRK
     LY