VMP1_HUMAN
ID VMP1_HUMAN Reviewed; 406 AA.
AC Q96GC9; B4DVV9; Q9H0P4; Q9P089;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Vacuole membrane protein 1 {ECO:0000305};
DE AltName: Full=Transmembrane protein 49;
GN Name=VMP1 {ECO:0000303|PubMed:28890335, ECO:0000312|HGNC:HGNC:29559};
GN Synonyms=TDC1 {ECO:0000303|Ref.1}, TMEM49 {ECO:0000312|HGNC:HGNC:29559};
GN ORFNames=HSPC292;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wu G., Couch F.J.;
RT "Gene Tdc1 is a transmembrane domain containing gene that amplified and
RT overexpressed in human breast cancer.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yamazaki S., Muta T., Takeshige K.;
RT "A novel lipopolysaccharide-inducible gene (#25).";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 243-406 (ISOFORM 1).
RC TISSUE=Blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, INTERACTION WITH TJP1, AND SUBCELLULAR LOCATION.
RX PubMed=17724469; DOI=10.1038/sj.onc.1210743;
RA Sauermann M., Sahin O., Sultmann H., Hahne F., Blaszkiewicz S., Majety M.,
RA Zatloukal K., Fuzesi L., Poustka A., Wiemann S., Arlt D.;
RT "Reduced expression of vacuole membrane protein 1 affects the invasion
RT capacity of tumor cells.";
RL Oncogene 27:1320-1326(2008).
RN [10]
RP INTERACTION WITH TP53INP2.
RX PubMed=19056683; DOI=10.1091/mbc.e08-07-0671;
RA Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P., Pebusque M.J.,
RA Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.;
RT "The TP53INP2 protein is required for autophagy in mammalian cells.";
RL Mol. Biol. Cell 20:870-881(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATP2A1; PLN; SLN; ATP2A2
RP AND ATP2A3, AND MUTAGENESIS OF GLY-197 AND GLY-279.
RX PubMed=28890335; DOI=10.1016/j.molcel.2017.08.005;
RA Zhao Y.G., Chen Y., Miao G., Zhao H., Qu W., Li D., Wang Z., Liu N., Li L.,
RA Chen S., Liu P., Feng D., Zhang H.;
RT "The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates SERCA Activity
RT to Control ER-Isolation Membrane Contacts for Autophagosome Formation.";
RL Mol. Cell 67:974.e6-989.e6(2017).
RN [13]
RP FUNCTION, INTERACTION WITH TMEM41B, AND REGION VTT DOMAIN.
RX PubMed=30093494; DOI=10.1083/jcb.201804132;
RA Morita K., Hama Y., Izume T., Tamura N., Ueno T., Yamashita Y.,
RA Sakamaki Y., Mimura K., Morishita H., Shihoya W., Nureki O., Mano H.,
RA Mizushima N.;
RT "Genome-wide CRISPR screen identifies TMEM41B as a gene required for
RT autophagosome formation.";
RL J. Cell Biol. 217:3817-3828(2018).
RN [14]
RP FUNCTION.
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).
RN [15]
RP FUNCTION.
RX PubMed=30933966; DOI=10.1371/journal.pbio.2007044;
RA Shoemaker C.J., Huang T.Q., Weir N.R., Polyakov N.J., Schultz S.W.,
RA Denic V.;
RT "CRISPR screening using an expanded toolkit of autophagy reporters
RT identifies TMEM41B as a novel autophagy factor.";
RL PLoS Biol. 17:E2007044-E2007044(2019).
RN [16]
RP FUNCTION (MICROBIAL INFECTION), AND DOMAIN (MICROBIAL INFECTION).
RX PubMed=33338421; DOI=10.1016/j.cell.2020.12.005;
RA Hoffmann H.H., Schneider W.M., Rozen-Gagnon K., Miles L.A., Schuster F.,
RA Razooky B., Jacobson E., Wu X., Yi S., Rudin C.M., MacDonald M.R.,
RA McMullan L.K., Poirier J.T., Rice C.M.;
RT "TMEM41B Is a Pan-flavivirus Host Factor.";
RL Cell 0:0-0(2020).
RN [17]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33929485; DOI=10.1083/jcb.202103105;
RA Li Y.E., Wang Y., Du X., Zhang T., Mak H.Y., Hancock S.E., McEwen H.,
RA Pandzic E., Whan R.M., Aw Y.C., Lukmantara I.E., Yuan Y., Dong X., Don A.,
RA Turner N., Qi S., Yang H.;
RT "TMEM41B and VMP1 are scramblases and regulate the distribution of
RT cholesterol and phosphatidylserine.";
RL J. Cell Biol. 220:0-0(2021).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH ATG2A.
RX PubMed=33850023; DOI=10.1073/pnas.2101562118;
RA Ghanbarpour A., Valverde D.P., Melia T.J., Reinisch K.M.;
RT "A model for a partnership of lipid transfer proteins and scramblases in
RT membrane expansion and organelle biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Phospholipid scramblase involved in lipid homeostasis and
CC membrane dynamics processes (PubMed:33929485, PubMed:33850023). Has
CC phospholipid scramblase activity toward cholesterol and
CC phosphatidylserine, as well as phosphatidylethanolamine and
CC phosphatidylcholine (PubMed:33929485, PubMed:33850023). 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 (PubMed:28890335,
CC PubMed:30093494, PubMed:30933966, PubMed:33929485, PubMed:33850023).
CC Regulates ATP2A2 activity to control ER-isolation membrane contacts for
CC autophagosome formation (PubMed:28890335). In addition to autophagy,
CC involved in other processes in which phospholipid scramblase activity
CC is required (PubMed:31526472, PubMed:33850023). Modulates ER contacts
CC with lipid droplets, mitochondria and endosomes (PubMed:28890335).
CC Plays an essential role in formation of cell junctions
CC (PubMed:17724469). Upon stress such as bacterial and viral infection,
CC promotes formation of cytoplasmic vacuoles followed by cell death (By
CC similarity). Involved in the cytoplasmic vacuolization of acinar cells
CC during the early stage of acute pancreatitis (By similarity).
CC {ECO:0000250|UniProtKB:Q91ZQ0, ECO:0000269|PubMed:17724469,
CC ECO:0000269|PubMed:28890335, ECO:0000269|PubMed:30093494,
CC ECO:0000269|PubMed:30933966, ECO:0000269|PubMed:31526472,
CC ECO:0000269|PubMed:33850023, ECO:0000269|PubMed:33929485}.
CC -!- FUNCTION: (Microbial infection) Host factor required for infection by
CC all flaviviruses tested such as Zika virus and Yellow fever virus
CC (PubMed:33338421). Probably required post-entry of the virus to
CC facilitate the ER membrane remodeling necessary to form replication
CC organelles (PubMed:33338421). {ECO:0000269|PubMed:33338421}.
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:0000269|PubMed:33929485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC ChEBI:CHEBI:16113; Evidence={ECO:0000269|PubMed:33929485};
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:0000269|PubMed:33850023,
CC ECO:0000269|PubMed:33929485};
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:0000269|PubMed:33850023,
CC ECO:0000269|PubMed:33929485};
CC -!- SUBUNIT: Interacts with BECN1 (By similarity). Interacts with TJP1
CC (PubMed:17724469). Interacts with TP53INP2 (PubMed:19056683). Interacts
CC with TMEM41B (PubMed:30093494). Interacts with ATP2A2, PLN and SLN;
CC competes with PLN and SLN to prevent them from forming an inhibitory
CC complex with ATP2A2 (PubMed:28890335). Interacts with ATG2A
CC (PubMed:33850023). {ECO:0000250|UniProtKB:Q91ZQ0,
CC ECO:0000269|PubMed:17724469, ECO:0000269|PubMed:19056683,
CC ECO:0000269|PubMed:28890335, ECO:0000269|PubMed:30093494,
CC ECO:0000269|PubMed:33850023}.
CC -!- INTERACTION:
CC Q96GC9; Q14457: BECN1; NbExp=3; IntAct=EBI-2800296, EBI-949378;
CC Q96GC9; P00387: CYB5R3; NbExp=3; IntAct=EBI-2800296, EBI-1046040;
CC Q96GC9; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2800296, EBI-781551;
CC Q96GC9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2800296, EBI-18304435;
CC Q96GC9; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2800296, EBI-16439278;
CC Q96GC9; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-2800296, EBI-2823239;
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:0000269|PubMed:17724469}; 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:0000269|PubMed:17724469, ECO:0000269|PubMed:28890335}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96GC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96GC9-2; Sequence=VSP_056106;
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:0000305|PubMed:30093494}.
CC -!- DOMAIN: (Microbial infection) VTT domain is required for flavivirus
CC infection. {ECO:0000269|PubMed:33338421}.
CC -!- SIMILARITY: Belongs to the VMP1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/VMP1ID50079ch17q23.html";
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DR EMBL; AF214006; AAL36461.1; -; mRNA.
DR EMBL; AB047551; BAF47368.1; -; mRNA.
DR EMBL; AL136711; CAB66646.1; -; mRNA.
DR EMBL; AK301254; BAG62821.1; -; mRNA.
DR EMBL; CR533521; CAG38552.1; -; mRNA.
DR EMBL; AC004686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC040904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009758; AAH09758.1; -; mRNA.
DR EMBL; AF161410; AAF28970.1; -; mRNA.
DR CCDS; CCDS11619.1; -. [Q96GC9-1]
DR RefSeq; NP_001316323.1; NM_001329394.1. [Q96GC9-1]
DR RefSeq; NP_001316326.1; NM_001329397.1.
DR RefSeq; NP_001316331.1; NM_001329402.1. [Q96GC9-2]
DR RefSeq; NP_112200.2; NM_030938.4. [Q96GC9-1]
DR AlphaFoldDB; Q96GC9; -.
DR BioGRID; 123567; 192.
DR IntAct; Q96GC9; 109.
DR MINT; Q96GC9; -.
DR STRING; 9606.ENSP00000262291; -.
DR TCDB; 8.A.97.1.1; the epg-3/vmp1 (epg/vpm) family.
DR GlyGen; Q96GC9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96GC9; -.
DR PhosphoSitePlus; Q96GC9; -.
DR SwissPalm; Q96GC9; -.
DR BioMuta; VMP1; -.
DR DMDM; 74731809; -.
DR EPD; Q96GC9; -.
DR jPOST; Q96GC9; -.
DR MassIVE; Q96GC9; -.
DR MaxQB; Q96GC9; -.
DR PaxDb; Q96GC9; -.
DR PeptideAtlas; Q96GC9; -.
DR PRIDE; Q96GC9; -.
DR ProteomicsDB; 5298; -.
DR ProteomicsDB; 76615; -. [Q96GC9-1]
DR TopDownProteomics; Q96GC9-1; -. [Q96GC9-1]
DR Antibodypedia; 31116; 282 antibodies from 27 providers.
DR DNASU; 81671; -.
DR Ensembl; ENST00000262291.9; ENSP00000262291.3; ENSG00000062716.13. [Q96GC9-1]
DR GeneID; 81671; -.
DR KEGG; hsa:81671; -.
DR MANE-Select; ENST00000262291.9; ENSP00000262291.3; NM_030938.5; NP_112200.2.
DR UCSC; uc002ixu.5; human. [Q96GC9-1]
DR CTD; 81671; -.
DR DisGeNET; 81671; -.
DR GeneCards; VMP1; -.
DR HGNC; HGNC:29559; VMP1.
DR HPA; ENSG00000062716; Low tissue specificity.
DR MIM; 611753; gene.
DR neXtProt; NX_Q96GC9; -.
DR OpenTargets; ENSG00000062716; -.
DR PharmGKB; PA142670765; -.
DR VEuPathDB; HostDB:ENSG00000062716; -.
DR eggNOG; KOG1109; Eukaryota.
DR GeneTree; ENSGT00390000007230; -.
DR HOGENOM; CLU_033298_0_1_1; -.
DR InParanoid; Q96GC9; -.
DR OMA; EEPYDKR; -.
DR PhylomeDB; Q96GC9; -.
DR TreeFam; TF313699; -.
DR PathwayCommons; Q96GC9; -.
DR SignaLink; Q96GC9; -.
DR BioGRID-ORCS; 81671; 639 hits in 1088 CRISPR screens.
DR ChiTaRS; VMP1; human.
DR GeneWiki; TMEM49; -.
DR GenomeRNAi; 81671; -.
DR Pharos; Q96GC9; Tbio.
DR PRO; PR:Q96GC9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96GC9; protein.
DR Bgee; ENSG00000062716; Expressed in blood and 196 other tissues.
DR ExpressionAtlas; Q96GC9; baseline and differential.
DR Genevisible; Q96GC9; HS.
DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA: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:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0000407; C:phagophore assembly site; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017128; F:phospholipid scramblase activity; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IDA:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; IDA:UniProtKB.
DR GO; GO:0006914; P:autophagy; IDA:UniProtKB.
DR GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0042953; P:lipoprotein transport; IMP:UniProtKB.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IDA:UniProtKB.
DR GO; GO:0140056; P:organelle localization by membrane tethering; IDA:UniProtKB.
DR GO; GO:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; 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:0007744|PubMed:22814378"
FT CHAIN 2..406
FT /note="Vacuole membrane protein 1"
FT /id="PRO_0000284546"
FT TOPO_DOM 2..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..77
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..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..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..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:0000305|PubMed:30093494"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..192
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056106"
FT MUTAGEN 197
FT /note="G->R: Decreases interaction with ATP2A2."
FT /evidence="ECO:0000269|PubMed:28890335"
FT MUTAGEN 279
FT /note="G->E: Decreases interaction with ATP2A2."
FT /evidence="ECO:0000269|PubMed:28890335"
FT CONFLICT 179
FT /note="S -> F (in Ref. 3; CAB66646 and 5; CAG38552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 46238 MW; E9DDE63F80143091 CRC64;
MAENGKNCDQ RRVAMNKEHH NGNFTDPSSV NEKKRREREE RQNIVLWRQP LITLQYFSLE
ILVILKEWTS KLWHRQSIVV SFLLLLAVLI ATYYVEGVHQ QYVQRIEKQF LLYAYWIGLG
ILSSVGLGTG LHTFLLYLGP HIASVTLAAY ECNSVNFPEP PYPDQIICPD EEGTEGTISL
WSIISKVRIE ACMWGIGTAI GELPPYFMAR AARLSGAEPD DEEYQEFEEM LEHAESAQDF
ASRAKLAVQK LVQKVGFFGI LACASIPNPL FDLAGITCGH FLVPFWTFFG ATLIGKAIIK
MHIQKIFVII TFSKHIVEQM VAFIGAVPGI GPSLQKPFQE YLEAQRQKLH HKSEMGTPQG
ENWLSWMFEK LVVVMVCYFI LSIINSMAQS YAKRIQQRLN SEEKTK
