VAMP4_BOVIN
ID VAMP4_BOVIN Reviewed; 141 AA.
AC Q32L97; A5PK89;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Vesicle-associated membrane protein 4;
DE Short=VAMP-4;
GN Name=VAMP4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus, and Hereford; TISSUE=Hypothalamus, and Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the pathway that functions to remove an inhibitor
CC (probably synaptotagmin-4) of calcium-triggered exocytosis during the
CC maturation of secretory granules. May be a marker for this sorting
CC pathway that is critical for remodeling the secretory response of
CC granule (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Identified in a complex containing STX6, STX12, VAMP4 and
CC VTI1A (By similarity). Interacts with BAIAP3; this interaction is
CC increased in the presence of calcium (By similarity).
CC {ECO:0000250|UniProtKB:O70480, ECO:0000250|UniProtKB:O75379}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
CC Note=Associated with trans Golgi network (TGN) and newly formed
CC immature secretory granules (ISG). Not found on the mature secretory
CC organelles (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; BC109690; AAI09691.1; -; mRNA.
DR EMBL; BC142401; AAI42402.1; -; mRNA.
DR RefSeq; NP_001069906.1; NM_001076438.2.
DR RefSeq; XP_005216973.1; XM_005216916.2.
DR RefSeq; XP_010811531.1; XM_010813229.2.
DR AlphaFoldDB; Q32L97; -.
DR SMR; Q32L97; -.
DR STRING; 9913.ENSBTAP00000027435; -.
DR PaxDb; Q32L97; -.
DR PRIDE; Q32L97; -.
DR Ensembl; ENSBTAT00000027435; ENSBTAP00000027435; ENSBTAG00000020591.
DR Ensembl; ENSBTAT00000069950; ENSBTAP00000073260; ENSBTAG00000020591.
DR Ensembl; ENSBTAT00000071023; ENSBTAP00000069106; ENSBTAG00000020591.
DR GeneID; 616923; -.
DR KEGG; bta:616923; -.
DR CTD; 8674; -.
DR VEuPathDB; HostDB:ENSBTAG00000020591; -.
DR VGNC; VGNC:36758; VAMP4.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000155005; -.
DR HOGENOM; CLU_149550_0_0_1; -.
DR InParanoid; Q32L97; -.
DR OMA; WWRGCKV; -.
DR OrthoDB; 1614157at2759; -.
DR TreeFam; TF313666; -.
DR Reactome; R-BTA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000020591; Expressed in occipital lobe and 105 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0090161; P:Golgi ribbon formation; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035493; P:SNARE complex assembly; IBA:GO_Central.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR042855; V_SNARE_CC.
DR InterPro; IPR042887; VAMP4.
DR PANTHER; PTHR46897; PTHR46897; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..141
FT /note="Vesicle-associated membrane protein 4"
FT /id="PRO_0000273716"
FT TOPO_DOM 1..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..141
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 52..112
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70480"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75379"
SQ SEQUENCE 141 AA; 16393 MW; 4DDB9682C63CF91E CRC64;
MPPKFKRHLN DDDVTGSVKS ERRNLLEDDS DEEEDFFLRG PSGPRFGPRN DKIKHVQNQV
DEVIDVMQEN ITKVIERGER LDELQDKSES LSDNATAFSN RSKQLRRQMW WRGCKIKAIM
ALVAVILLLV IIILIVVKYR T