ID   SVIP_RAT                Reviewed;          76 AA.
AC   P0C0A9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Small VCP/p97-interacting protein;
GN   Name=Svip;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH VCP.
RC   TISSUE=Brain;
RX   PubMed=12529442; DOI=10.1091/mbc.02-07-0115;
RA   Nagahama M., Suzuki M., Hamada Y., Hatsuzawa K., Tani K., Yamamoto A.,
RA   Tagaya M.;
RT   "SVIP is a novel VCP/p97-interacting protein whose expression causes cell
RT   vacuolation.";
RL   Mol. Biol. Cell 14:262-273(2003).
CC   -!- FUNCTION: Overexpression causes the formation of large vacuoles that
CC       seemed to be derived from the endoplasmic reticulum.
CC       {ECO:0000269|PubMed:12529442}.
CC   -!- SUBUNIT: Interacts with VCP. {ECO:0000250|UniProtKB:Q8NHG7,
CC       ECO:0000269|PubMed:12529442}.
CC   -!- SUBCELLULAR LOCATION: Smooth endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Golgi apparatus membrane; Peripheral membrane
CC       protein. Cell membrane; Peripheral membrane protein. Membrane
CC       {ECO:0000250|UniProtKB:Q8NHG7}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q8NHG7}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the SVIP family. {ECO:0000305}.
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DR   RefSeq; NP_001258013.1; NM_001271084.1.
DR   AlphaFoldDB; P0C0A9; -.
DR   SMR; P0C0A9; -.
DR   STRING; 10116.ENSRNOP00000052878; -.
DR   PaxDb; P0C0A9; -.
DR   PRIDE; P0C0A9; -.
DR   GeneID; 499157; -.
DR   KEGG; rno:499157; -.
DR   UCSC; RGD:1565432; rat.
DR   CTD; 258010; -.
DR   RGD; 1565432; Svip.
DR   VEuPathDB; HostDB:ENSRNOG00000037137; -.
DR   eggNOG; ENOG502S5MU; Eukaryota.
DR   HOGENOM; CLU_174267_1_0_1; -.
DR   InParanoid; P0C0A9; -.
DR   OMA; CCGQSAE; -.
DR   PhylomeDB; P0C0A9; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:P0C0A9; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000037137; Expressed in pancreas and 20 other tissues.
DR   Genevisible; P0C0A9; RN.
DR   GO; GO:0031225; C:anchored component of membrane; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR   GO; GO:0043621; F:protein self-association; ISO:RGD.
DR   GO; GO:1903070; P:negative regulation of ER-associated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
DR   GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; ISO:RGD.
DR   GO; GO:1904240; P:negative regulation of VCP-NPL4-UFD1 AAA ATPase complex assembly; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR   GO; GO:1903061; P:positive regulation of protein lipidation; ISO:RGD.
DR   InterPro; IPR031632; SVIP.
DR   PANTHER; PTHR35269; PTHR35269; 1.
DR   Pfam; PF15811; SVIP; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Endoplasmic reticulum; Golgi apparatus; Lipoprotein;
KW   Membrane; Myristate; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHG7"
FT   CHAIN           2..76
FT                   /note="Small VCP/p97-interacting protein"
FT                   /id="PRO_0000072339"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          21..33
FT                   /note="VCP/p97-interacting motif (VIM)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHG7"
FT   COMPBIAS        20..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHG7"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHG7"
SQ   SEQUENCE   76 AA;  8248 MW;  485974815DBFD4FC CRC64;
     MGLCFPCPAE SAPPSPSPEE KRAKLAEAAE RRQKEAASRG ILDIQSVEAK KKKKEQLEKQ
     METSGPPAGG LRWTVS