VMP1_RAT
ID VMP1_RAT Reviewed; 406 AA.
AC Q91ZQ0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Vacuole membrane protein 1 {ECO:0000305};
GN Name=Vmp1 {ECO:0000303|PubMed:11785947, ECO:0000312|RGD:70367};
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, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Pancreas;
RX PubMed=11785947; DOI=10.1006/bbrc.2001.6244;
RA Dusetti N.J., Jiang Y., Vaccaro M.I., Tomasini R., Azizi Samir A.,
RA Calvo E.L., Ropolo A., Fiedler F., Mallo G.V., Dagorn J.-C., Iovanna J.L.;
RT "Cloning and expression of the rat vacuole membrane protein 1 (VMP1), a new
RT gene activated in pancreas with acute pancreatitis, which promotes vacuole
RT formation.";
RL Biochem. Biophys. Res. Commun. 290:641-649(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=12649568; DOI=10.1159/000069150;
RA Vaccaro M.I., Grasso D., Ropolo A., Iovanna J.L., Cerquetti M.C.;
RT "VMP1 expression correlates with acinar cell cytoplasmic vacuolization in
RT arginine-induced acute pancreatitis.";
RL Pancreatology 3:69-74(2003).
RN [4]
RP FUNCTION.
RX PubMed=15367889; DOI=10.1097/00006676-200410000-00008;
RA Jiang P.H., Motoo Y., Vaccaro M.I., Iovanna J.L., Okada G., Sawabu N.;
RT "Expression of vacuole membrane protein 1 (VMP1) in spontaneous chronic
RT pancreatitis in the WBN/Kob rat.";
RL Pancreas 29:225-230(2004).
RN [5]
RP FUNCTION, INTERACTION WITH BECN1, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=17940279; DOI=10.1074/jbc.m706956200;
RA Ropolo A., Grasso D., Pardo R., Sacchetti M.L., Archange C., Lo Re A.,
RA Seux M., Nowak J., Gonzalez C.D., Iovanna J.L., Vaccaro M.I.;
RT "The pancreatitis-induced vacuole membrane protein 1 triggers autophagy in
RT mammalian cells.";
RL J. Biol. Chem. 282:37124-37133(2007).
CC -!- FUNCTION: Phospholipid scramblase involved in lipid homeostasis and
CC membrane dynamics processes (By similarity). Has phospholipid
CC scramblase activity toward cholesterol and phosphatidylserine, as well
CC as phosphatidylethanolamine and phosphatidylcholine (By similarity).
CC Required for autophagosome formation: participates in early stages of
CC autophagosome 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 (By similarity).
CC Regulates ATP2A2 activity to control ER-isolation membrane contacts for
CC autophagosome formation (PubMed:17940279). In addition to autophagy,
CC involved in other processes in which phospholipid scramblase activity
CC is required (By similarity). Modulates ER contacts with lipid droplets,
CC mitochondria and endosomes (By similarity). Plays an essential role in
CC formation of cell junctions (By similarity). Upon stress such as
CC bacterial and viral infection, promotes formation of cytoplasmic
CC vacuoles followed by cell death (PubMed:11785947, PubMed:12649568,
CC PubMed:15367889). Involved in the cytoplasmic vacuolization of acinar
CC cells during the early stage of acute pancreatitis (PubMed:11785947,
CC PubMed:12649568, PubMed:15367889). {ECO:0000250|UniProtKB:Q96GC9,
CC ECO:0000269|PubMed:11785947, ECO:0000269|PubMed:12649568,
CC ECO:0000269|PubMed:15367889, ECO:0000269|PubMed:17940279}.
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 (PubMed:17940279). 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:Q96GC9, ECO:0000269|PubMed:17940279}.
CC -!- INTERACTION:
CC Q91ZQ0; Q14457: BECN1; Xeno; NbExp=6; IntAct=EBI-11163586, EBI-949378;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:11785947}; Multi-pass membrane
CC protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q96GC9};
CC Multi-pass membrane protein {ECO:0000255}. Vacuole membrane
CC {ECO:0000269|PubMed:17940279}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96GC9}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalizes with MAP1LC3A and BECN1.
CC {ECO:0000269|PubMed:17940279}.
CC -!- TISSUE SPECIFICITY: Highly expressed in intestine, kidney, ovary and
CC placenta, moderately expressed in liver, lung, stomach, thymus, brain,
CC and testis and slightly expressed in control thyroid and retina.
CC Strongly expressed in pancreas (acinar cells) during acute
CC pancreatitis. {ECO:0000269|PubMed:11785947}.
CC -!- INDUCTION: Overexpressed only in pancreas during acute pancreatitis.
CC Up-regulated by starvation. Up-regulated following MTOR-inhibition by
CC rapamycin. {ECO:0000269|PubMed:17940279}.
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; AF411216; AAL05859.1; -; mRNA.
DR EMBL; BC061721; AAH61721.1; -; mRNA.
DR PIR; JC7798; JC7798.
DR RefSeq; NP_620194.1; NM_138839.2.
DR RefSeq; XP_006247140.1; XM_006247078.3.
DR RefSeq; XP_006247141.1; XM_006247079.3.
DR AlphaFoldDB; Q91ZQ0; -.
DR BioGRID; 251330; 2.
DR IntAct; Q91ZQ0; 6.
DR STRING; 10116.ENSRNOP00000005658; -.
DR iPTMnet; Q91ZQ0; -.
DR PhosphoSitePlus; Q91ZQ0; -.
DR jPOST; Q91ZQ0; -.
DR PaxDb; Q91ZQ0; -.
DR PRIDE; Q91ZQ0; -.
DR Ensembl; ENSRNOT00000005658; ENSRNOP00000005658; ENSRNOG00000003967.
DR GeneID; 192129; -.
DR KEGG; rno:192129; -.
DR CTD; 81671; -.
DR RGD; 70367; Vmp1.
DR eggNOG; KOG1109; Eukaryota.
DR GeneTree; ENSGT00390000007230; -.
DR HOGENOM; CLU_033298_0_1_1; -.
DR InParanoid; Q91ZQ0; -.
DR OMA; EEPYDKR; -.
DR OrthoDB; 822110at2759; -.
DR PhylomeDB; Q91ZQ0; -.
DR TreeFam; TF313699; -.
DR PRO; PR:Q91ZQ0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003967; Expressed in duodenum and 20 other tissues.
DR Genevisible; Q91ZQ0; RN.
DR GO; GO:0000421; C:autophagosome membrane; IDA: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:0000407; C:phagophore assembly site; ISO:RGD.
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; IDA:GO_Central.
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; ISO:RGD.
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 1: Evidence at protein 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_0000284549"
FT TOPO_DOM 2..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..316
FT /note="VTT domain"
FT /evidence="ECO:0000250|UniProtKB:Q96GC9"
FT REGION 378..406
FT /note="Required for interaction with BECN1"
FT /evidence="ECO:0000269|PubMed:17940279"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96GC9"
SQ SEQUENCE 406 AA; 45901 MW; B87BDD5E8D06D722 CRC64;
MAENGTNCDQ RRGAMSKEQH NGSFTDPSSV NEKKRRDREE RQNIVLWRQP LITLQYFSLE
TLVVLKEWTS KLWHRQSMVV SFFLLLAALV ATYYVEGAHQ QYVQRIEKQF LLYAYWIGLG
ILSSVGLGTG LHTFLLYLGP HIASVTLAAY ECNSVNFPEP PYPDQIICPD EEGTEGAISL
WSIISKVRIE ACMWGIGTAI GELPPYFMAR AARLSGAEPD DEEYQEFEEM LEHAETAQDF
ASRAKLAVQK LVQKVGFFGI LACASIPNPL FDLAGITCGH FLVPFWTFFG ATLIGKAIIK
MHIQKIFVIV TFSKHIVEQM VAFIGAVPGI GPSLQKPFQE YLEAQRQKLH HRSEAGTAQG
ENWLSWTFEK LVVAMVCYFI LSIINSMAQS YAKRIQQRLN SEEKTK
