VMP1_BOVIN
ID VMP1_BOVIN Reviewed; 406 AA.
AC Q0VCK9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Vacuole membrane protein 1 {ECO:0000305};
GN Name=VMP1 {ECO:0000250|UniProtKB:Q96GC9};
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=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phospholipid scramblase involved in lipid homeostasis and
CC membrane dynamics processes. Has phospholipid scramblase activity
CC toward cholesterol and phosphatidylserine, as well as
CC phosphatidylethanolamine and phosphatidylcholine. Required for
CC autophagosome formation: participates in early stages of autophagosome
CC biogenesis at the endoplasmic reticulum (ER) membrane by
CC reequilibrating the leaflets of the ER as lipids are extracted by ATG2
CC (ATG2A or ATG2B) to mediate autophagosome assembly. Regulates ATP2A2
CC activity to control ER-isolation membrane contacts for autophagosome
CC formation. In addition to autophagy, involved in other processes in
CC which phospholipid scramblase activity is required. Modulates ER
CC contacts with lipid droplets, mitochondria and endosomes. Plays an
CC essential role in formation of cell junctions (By similarity). Upon
CC stress such as bacterial and viral infection, promotes formation of
CC cytoplasmic vacuoles followed by cell death. Involved in the
CC cytoplasmic vacuolization of acinar cells during the early stage of
CC acute pancreatitis (By similarity). {ECO:0000250|UniProtKB:Q91ZQ0,
CC ECO:0000250|UniProtKB:Q96GC9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q96GC9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC ChEBI:CHEBI:16113; Evidence={ECO:0000250|UniProtKB:Q96GC9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q96GC9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q96GC9};
CC -!- SUBUNIT: Interacts with BECN1 (By similarity). Interacts with TJP1.
CC Interacts with TP53INP2. Interacts with TMEM41B. Interacts with ATP2A2,
CC PLN and SLN; competes with PLN and SLN to prevent them from forming an
CC inhibitory complex with ATP2A2. Interacts with ATG2A (By similarity).
CC {ECO:0000250|UniProtKB:Q91ZQ0, ECO:0000250|UniProtKB:Q96GC9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250|UniProtKB:Q91ZQ0}; Multi-pass
CC membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96GC9}; Multi-pass membrane protein
CC {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q91ZQ0}; Multi-
CC pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96GC9}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The VTT domain was previously called the SNARE-assoc domain. As
CC there is no evidence that this domain associates with SNARE proteins,
CC it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain.
CC {ECO:0000250|UniProtKB:Q96GC9}.
CC -!- SIMILARITY: Belongs to the VMP1 family. {ECO:0000305}.
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DR EMBL; BC120116; AAI20117.1; -; mRNA.
DR RefSeq; NP_001068836.1; NM_001075368.2.
DR RefSeq; XP_005219942.1; XM_005219885.3.
DR RefSeq; XP_005219943.1; XM_005219886.3.
DR RefSeq; XP_005219944.1; XM_005219887.3.
DR AlphaFoldDB; Q0VCK9; -.
DR STRING; 9913.ENSBTAP00000015439; -.
DR PaxDb; Q0VCK9; -.
DR PRIDE; Q0VCK9; -.
DR Ensembl; ENSBTAT00000015439; ENSBTAP00000015439; ENSBTAG00000011623.
DR Ensembl; ENSBTAT00000082600; ENSBTAP00000065456; ENSBTAG00000011623.
DR GeneID; 508631; -.
DR KEGG; bta:508631; -.
DR CTD; 81671; -.
DR VEuPathDB; HostDB:ENSBTAG00000011623; -.
DR VGNC; VGNC:36806; VMP1.
DR eggNOG; KOG1109; Eukaryota.
DR GeneTree; ENSGT00390000007230; -.
DR HOGENOM; CLU_033298_0_1_1; -.
DR InParanoid; Q0VCK9; -.
DR OMA; EEPYDKR; -.
DR OrthoDB; 822110at2759; -.
DR TreeFam; TF313699; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000011623; Expressed in neutrophil and 105 other tissues.
DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0000407; C:phagophore assembly site; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017128; F:phospholipid scramblase activity; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0042953; P:lipoprotein transport; ISS:UniProtKB.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; ISS:UniProtKB.
DR GO; GO:0140056; P:organelle localization by membrane tethering; ISS:UniProtKB.
DR GO; GO:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; ISS:UniProtKB.
PE 2: Evidence at transcript level;
KW Acetylation; Autophagy; Cell adhesion; Cell membrane;
KW Endoplasmic reticulum; Lipid transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96GC9"
FT CHAIN 2..406
FT /note="Vacuole membrane protein 1"
FT /id="PRO_0000284545"
FT TOPO_DOM 2..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..77
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 173..316
FT /note="VTT domain"
FT /evidence="ECO:0000250|UniProtKB:Q96GC9"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96GC9"
SQ SEQUENCE 406 AA; 46182 MW; D51936DDC2B7CDD3 CRC64;
MAENGQNCDQ RRVAMNKEQY NGNFTDPSSV NEKKRRDREE RQNIVLWRQP LITLQYFSLE
TLVILKEWTS KLWHRQSIVV SFLLLLAVLT ATYYVEGAHQ QYVQRIEKQF LLYAYWIGLG
ILSSVGLGTG LHTFLLYLGP HIASVTLAAY ECNSVNFPEP PYPDQIICPD EEGTEGTISL
WSIISKVRIE ACMWGIGTAI GELPPYFMAR AARLSGAEPD DEEYQEFEEM LEHAETAQDF
ASRAKLAVQN LVQKVGFFGI LACASIPNPL FDLAGITCGH FLVPFWTFFG ATLIGKAIIK
MHIQKLFVIV AFSKHIVEQM VAFIGAVPGI GPSLQKPFQE YLEAQRQKLH HRSEMGTPQG
ENWLSWMFEK LVVVMVCYFI LSIINSMAQS YAKRIQQRLD PKEKTK
