ID   VMP1_XENTR              Reviewed;         406 AA.
AC   Q68EQ9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Vacuole membrane protein 1 {ECO:0000305};
GN   Name=vmp1 {ECO:0000250|UniProtKB:Q96GC9};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-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; BC080142; AAH80142.1; -; mRNA.
DR   RefSeq; NP_001007877.1; NM_001007876.1.
DR   AlphaFoldDB; Q68EQ9; -.
DR   STRING; 8364.ENSXETP00000023484; -.
DR   PaxDb; Q68EQ9; -.
DR   GeneID; 493262; -.
DR   KEGG; xtr:493262; -.
DR   CTD; 81671; -.
DR   Xenbase; XB-GENE-1000954; vmp1.
DR   eggNOG; KOG1109; Eukaryota.
DR   InParanoid; Q68EQ9; -.
DR   OrthoDB; 822110at2759; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; 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; IBA:GO_Central.
DR   GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
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_0000284552"
FT   TOPO_DOM        1..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..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..35
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;  46051 MW;  82F8AB7EF959845A CRC64;
     MAENGTDCEQ RRVGMAKEQN NGSFQDPSFL SDRKSRDREE RQSIVLWRKP LITLQYFILE
     VLITLKDWSI RLWHRRMMVV SVLLLLAVLS VVYYIEGTHQ QYVQYVEKKC LWCAYWVGLG
     ILSSVGLGTG LHTFLLYLGP HIASVTIAAY ECNSVNFPEP PYPDEIICPD EEGTEGAISL
     WTIISKVRLE ACMWGAGTAI GELPPYFMAR AARLSGVETD DEEYAEFEEM LEHAQTAQDF
     ATRAKLAVQN LVQKVGFLGI LACASIPNPL FDLAGITCGH FLVPFWTFFG ATLIGKAIIK
     MHIQKLFVII TFSKHIVEQM VSLIGVIPSI GPSLQKPFQE YLEAQRKKLH HKEDSGAPQS
     ENWLSWAFEK LVIIMVFYFI LSIINSMAQS YAKRVQQRKL SVEKTK