VMP1_DANRE
ID VMP1_DANRE Reviewed; 406 AA.
AC Q6NYY9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Vacuole membrane protein 1 {ECO:0000305};
GN Name=vmp1 {ECO:0000303|PubMed:31526472};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31526472; DOI=10.7554/elife.48834;
RA Morishita H., Zhao Y.G., Tamura N., Nishimura T., Kanda Y., Sakamaki Y.,
RA Okazaki M., Li D., Mizushima N.;
RT "A critical role of VMP1 in lipoprotein secretion.";
RL Elife 8:0-0(2019).
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. In addition to
CC autophagy, involved in other processes in which phospholipid scramblase
CC activity is required. Modulates ER contacts with lipid droplets,
CC mitochondria and endosomes. {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 -!- 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 -!- DISRUPTION PHENOTYPE: Mutants show larval lethality around 9 days post
CC fertilization and defects in autophagy. They also have lipoprotein
CC accumulation in the intestine and liver. {ECO:0000269|PubMed:31526472}.
CC -!- SIMILARITY: Belongs to the VMP1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC066412; AAH66412.1; -; mRNA.
DR RefSeq; NP_996943.1; NM_207060.1.
DR AlphaFoldDB; Q6NYY9; -.
DR STRING; 7955.ENSDARP00000004153; -.
DR PaxDb; Q6NYY9; -.
DR GeneID; 336789; -.
DR KEGG; dre:336789; -.
DR CTD; 81671; -.
DR ZFIN; ZDB-GENE-030131-8733; vmp1.
DR eggNOG; KOG1109; Eukaryota.
DR InParanoid; Q6NYY9; -.
DR OrthoDB; 822110at2759; -.
DR PhylomeDB; Q6NYY9; -.
DR PRO; PR:Q6NYY9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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; IEA:UniProtKB-SubCell.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017128; F:phospholipid scramblase activity; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:ZFIN.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0042953; P:lipoprotein transport; IMP:UniProtKB.
PE 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..406
FT /note="Vacuole membrane protein 1"
FT /id="PRO_0000284550"
FT TOPO_DOM 1..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..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..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..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..316
FT /note="VTT domain"
FT /evidence="ECO:0000250|UniProtKB:Q96GC9"
SQ SEQUENCE 406 AA; 45705 MW; CD22F8E492A9249E CRC64;
MAANGAECEQ PQKRLGPKDK QNGSSTDSSL RERKQLDREE RLSLVLWKRP FITLQYFFLE
TAITLKEWTW KLWQRRGVVF LTVVLFSLFS LAYSIEGAHQ EYVQHLEKKF LWCAYWVGLG
ILSSVGLGTG LHTFLLYLGP HIASVTLAAY ECGSVNFPEP PYPAQIVCPE DEALQESISL
WTIMSKVRLE ACMWGAGTAI GELPPYFMAR AARMSGADPD DEDYEEFEEM LEHSQSAQDF
ASRAKLAVQN MVQKVGFFGI LACASIPNPL FDLAGITCGH FLIPFWTFFG ATLIGKAIIK
MHIQKLFVII TFSKHIVEQM VSLIGVIPGV GASLQKPFRE YLEAQRTKLH NPAGDGAAAG
ESWLSWVFEK VVLVMVCYFI LSIINSMAQS YAKRLQQKKY SEEKTK
