VMP1_XENLA
ID VMP1_XENLA Reviewed; 406 AA.
AC Q6INE8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Vacuole membrane protein 1 {ECO:0000305};
GN Name=vmp1 {ECO:0000250|UniProtKB:Q96GC9};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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. 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 -!- SIMILARITY: Belongs to the VMP1 family. {ECO:0000305}.
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DR EMBL; BC072335; AAH72335.1; -; mRNA.
DR RefSeq; NP_001085166.1; NM_001091697.1.
DR AlphaFoldDB; Q6INE8; -.
DR SMR; Q6INE8; -.
DR DNASU; 432249; -.
DR GeneID; 432249; -.
DR KEGG; xla:432249; -.
DR CTD; 432249; -.
DR Xenbase; XB-GENE-1000959; vmp1.L.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 432249; Expressed in zone of skin and 19 other tissues.
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: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:0042953; P:lipoprotein transport; ISS: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_0000284551"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..76
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..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 1..22
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; 46106 MW; C6E1D85E67F64E1E CRC64;
MAENGTDCEQ RRVGMPKEQN NGSFQDPSFM CNRKRRDREE RQSIVLWRKP LITLQYFILE
VLINLKEWSV RLWHRRMMVV SVLLLLAVLS VAYYIEGEHQ QCVQYIEKKC LWCAYWVGLG
ILSSVGLGTG LHTFLLYLGP HIASVTIAAY ECNSVNFPEP PYPDEIICPD EEGTEGAISL
WTIISKVRLE ACMWGAGTAI GELPPYFMAR AARLSGVETD DEEYAEFEEM LEHAQTAQDF
ATRAKLTVQN LVQKVGFLGI LACASIPNPL FDLAGITCGH FLVPFWTFFG ATLIGKAIIK
MHIQKLFVII TFSKHIVEQM VSLIGVIPSI GPSLQKPFQE YLEAQRKKLH HKGDSGTPQS
ENWLSWAFEK LVIIMVFYFI LSIINSMAQS YAKRVQQKKL SVEKTK
