VMP1_DICDI
ID VMP1_DICDI Reviewed; 403 AA.
AC Q54NL4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Vacuole membrane protein 1 homolog {ECO:0000305};
DE AltName: Full=Transmembrane protein 49 homolog;
GN Name=vmp1 {ECO:0000303|PubMed:18550798,
GN ECO:0000312|dictyBase:DDB_G0285175}; Synonyms=tmem49;
GN ORFNames=DDB_G0285175;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18550798; DOI=10.1091/mbc.e08-01-0075;
RA Calvo-Garrido J., Carilla-Latorre S., Lazaro-Dieguez F., Egea G.,
RA Escalante R.;
RT "Vacuole membrane protein 1 is an endoplasmic reticulum protein required
RT for organelle biogenesis, protein secretion, and development.";
RL Mol. Biol. Cell 19:3442-3453(2008).
CC -!- FUNCTION: Phospholipid scramblase involved in lipid homeostasis and
CC membrane dynamics processes (By similarity). Required for autophagosome
CC formation: participates in early stages of autophagosome biogenesis at
CC the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets
CC of the ER as lipids are extracted (By similarity). In addition to
CC autophagy, involved in other processes in which phospholipid scramblase
CC activity is required (PubMed:18550798). {ECO:0000250|UniProtKB:Q96GC9,
CC ECO:0000269|PubMed:18550798}.
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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:18550798}.
CC -!- DISRUPTION PHENOTYPE: Mutant cells display defects in the protein
CC secretory pathway and in organelle biogenesis, and are deficient in
CC their ability to initiate development upon starvation. The contractile
CC vacuole, which is necessary to survive under hyperosmotic conditions,
CC is non-functional in mutant cells. {ECO:0000269|PubMed:18550798}.
CC -!- SIMILARITY: Belongs to the VMP1 family. {ECO:0000305}.
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DR EMBL; AAFI02000075; EAL64844.1; -; Genomic_DNA.
DR RefSeq; XP_638348.1; XM_633256.1.
DR AlphaFoldDB; Q54NL4; -.
DR STRING; 44689.DDB0234044; -.
DR PaxDb; Q54NL4; -.
DR PRIDE; Q54NL4; -.
DR EnsemblProtists; EAL64844; EAL64844; DDB_G0285175.
DR GeneID; 8624973; -.
DR KEGG; ddi:DDB_G0285175; -.
DR dictyBase; DDB_G0285175; vmp1.
DR eggNOG; KOG1109; Eukaryota.
DR HOGENOM; CLU_033298_0_1_1; -.
DR InParanoid; Q54NL4; -.
DR OMA; EEPYDKR; -.
DR PhylomeDB; Q54NL4; -.
DR PRO; PR:Q54NL4; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR GO; GO:0048102; P:autophagic cell death; IMP:dictyBase.
DR GO; GO:0000045; P:autophagosome assembly; IMP:dictyBase.
DR GO; GO:0006914; P:autophagy; IMP:dictyBase.
DR GO; GO:0033298; P:contractile vacuole organization; IMP:dictyBase.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:dictyBase.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:dictyBase.
DR GO; GO:0006887; P:exocytosis; IMP:dictyBase.
DR GO; GO:0007030; P:Golgi organization; IMP:dictyBase.
DR GO; GO:0006971; P:hypotonic response; IMP:dictyBase.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
DR InterPro; IPR032816; SNARE_assoc.
DR Pfam; PF09335; SNARE_assoc; 1.
PE 3: Inferred from homology;
KW Coiled coil; Endoplasmic reticulum; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..403
FT /note="Vacuole membrane protein 1 homolog"
FT /id="PRO_0000328112"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 7..33
FT /evidence="ECO:0000255"
SQ SEQUENCE 403 AA; 45612 MW; 2B2CE6159AC8105A CRC64;
MGKSNTIVLS NEKDIQLRIQ QLEERKEKRK NVKLLFSPIK TTKYFLYILK DTLVSGIRYF
QTRPFLLFFI ALFASLTFIA VYVPGEHQKY MGKYSDLISD CIWWVGLGVL SSIGLGTGLH
TFVLYLGPHI AKVTLAATEW NSVNFNVYGA NSFIQPATAM IGGVSFWMIL QKVQWAALFW
GAGTAIGELP PYFVARTARL KGLKLEQEKK LKEQQEKPID EKDQPKKGLL ERLSEKVPAL
IGNLGFFGIL AFASIPNPLF DLAGITCGHF LVPFWKFFGA TFIGKAVVKA HIQACFVILA
FNMETLTMVI SFIEDKIPFL KNKIQPILEK ERQKLNSTVS ANSPKSLVGL AWDCVLFLMI
SYFLMSIVDS SVQEYLIEKD NKKIELLKSK LEKQQPKETK KTK
