VTA1_HUMAN
ID VTA1_HUMAN Reviewed; 307 AA.
AC Q9NP79; B4DW55; E1P594; E7ETQ7; Q5TGM1; Q6IAE8; Q9H0R2; Q9H3K9; Q9P0Q0;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Vacuolar protein sorting-associated protein VTA1 homolog;
DE AltName: Full=Dopamine-responsive gene 1 protein;
DE Short=DRG-1;
DE AltName: Full=LYST-interacting protein 5;
DE Short=LIP5;
DE AltName: Full=SKD1-binding protein 1;
DE Short=SBP1;
GN Name=VTA1; Synonyms=C6orf55; ORFNames=HSPC228, My012;
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 Shi J., Cai W., Xie Y.;
RT "Identification of dopamine responsive genes in glial cells by subtractive
RT hybridization.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Zheng Z.H., Gu S.H., Ying K., Lin Q., Dai J.L., Tang R.,
RA Dong H., Wu X.Z.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Synovial cell;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Urinary bladder;
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 [10]
RP PROTEIN SEQUENCE OF 2-15 AND 30-39, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (OCT-2008) to UniProtKB.
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHMP5.
RX PubMed=15644320; DOI=10.1074/jbc.m413734200;
RA Ward D.M., Vaughn M.B., Shiflett S.L., White P.L., Pollock A.L., Hill J.,
RA Schnegelberger R., Sundquist W.I., Kaplan J.;
RT "The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1
RT budding in mammalian cells.";
RL J. Biol. Chem. 280:10548-10555(2005).
RN [12]
RP INTERACTION WITH CHMP5.
RX PubMed=17261583; DOI=10.1074/jbc.m611635200;
RA Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G.,
RA Kirchhausen T.;
RT "Targeting of AMSH to endosomes is required for epidermal growth factor
RT receptor degradation.";
RL J. Biol. Chem. 282:9805-9812(2007).
RN [13]
RP INTERACTION WITH CHMP1B; CHMP2A; CHMP3; CHMP5 AND VPS4B.
RX PubMed=18385515; DOI=10.1091/mbc.e07-12-1263;
RA Shim S., Merrill S.A., Hanson P.I.;
RT "Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications
RT for ESCRT-III disassembly.";
RL Mol. Biol. Cell 19:2661-2672(2008).
RN [14]
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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP INTERACTION WITH IST1.
RX PubMed=19129480; DOI=10.1091/mbc.e08-05-0474;
RA Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M.,
RA Ameer-Beg S., Bowers K., Martin-Serrano J.;
RT "Essential role of hIST1 in cytokinesis.";
RL Mol. Biol. Cell 20:1374-1387(2009).
RN [16]
RP INTERACTION WITH IST1.
RX PubMed=19129479; DOI=10.1091/mbc.e08-05-0475;
RA Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M.,
RA Sundquist W.I.;
RT "Biochemical analyses of human IST1 and its function in cytokinesis.";
RL Mol. Biol. Cell 20:1360-1373(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP INTERACTION WITH CHMP2A; CHMP3 AND CHMP5.
RX PubMed=21543490; DOI=10.1128/jvi.02610-10;
RA Kuang Z., Seo E.J., Leis J.;
RT "Mechanism of inhibition of retrovirus release from cells by interferon-
RT induced gene ISG15.";
RL J. Virol. 85:7153-7161(2011).
RN [19]
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=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in the endosomal multivesicular bodies (MVB)
CC pathway. MVBs contain intraluminal vesicles (ILVs) that are generated
CC by invagination and scission from the limiting membrane of the endosome
CC and mostly are delivered to lysosomes enabling degradation of membrane
CC proteins, such as stimulated growth factor receptors, lysosomal enzymes
CC and lipids. Thought to be a cofactor of VPS4A/B, which catalyzes
CC disassembles membrane-associated ESCRT-III assemblies. Involved in the
CC sorting and down-regulation of EGFR (By similarity). Involved in HIV-1
CC budding. {ECO:0000250, ECO:0000269|PubMed:15644320}.
CC -!- SUBUNIT: Interacts with VPS4B. Interacts with CHMP1B. Interacts with
CC CHMP2A; the interaction probably involves the open conformation of
CC (polymerized) CHMP2A. Interacts with CHMP3. Interacts with CHMP5; the
CC interaction involves soluble CHMP5. Interacts with IST1.
CC {ECO:0000269|PubMed:15644320, ECO:0000269|PubMed:17261583,
CC ECO:0000269|PubMed:18385515, ECO:0000269|PubMed:19129479,
CC ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:21543490}.
CC -!- INTERACTION:
CC Q9NP79; P24863: CCNC; NbExp=3; IntAct=EBI-740160, EBI-395261;
CC Q9NP79; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-740160, EBI-1057156;
CC Q9NP79; Q7LBR1: CHMP1B; NbExp=3; IntAct=EBI-740160, EBI-2118090;
CC Q9NP79; Q9NZZ3: CHMP5; NbExp=3; IntAct=EBI-740160, EBI-751303;
CC Q9NP79; Q15561: TEAD4; NbExp=4; IntAct=EBI-740160, EBI-747736;
CC Q9NP79; Q05516: ZBTB16; NbExp=4; IntAct=EBI-740160, EBI-711925;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15644320}. Endosome
CC membrane {ECO:0000305|PubMed:15644320}; Peripheral membrane protein
CC {ECO:0000305|PubMed:15644320}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NP79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP79-2; Sequence=VSP_056727, VSP_056728;
CC -!- SIMILARITY: Belongs to the VTA1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36148.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG43125.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF271994; AAF76210.1; -; mRNA.
DR EMBL; AF060225; AAG43125.1; ALT_FRAME; mRNA.
DR EMBL; AF151062; AAF36148.1; ALT_FRAME; mRNA.
DR EMBL; AL136684; CAB66619.1; -; mRNA.
DR EMBL; AK000051; BAA90909.1; -; mRNA.
DR EMBL; AK301376; BAG62917.1; -; mRNA.
DR EMBL; CR457207; CAG33488.1; -; mRNA.
DR EMBL; AL033522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47883.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47885.1; -; Genomic_DNA.
DR EMBL; BC005937; AAH05937.1; -; mRNA.
DR EMBL; BC006989; AAH06989.1; -; mRNA.
DR EMBL; BC022536; AAH22536.1; -; mRNA.
DR CCDS; CCDS5197.1; -. [Q9NP79-1]
DR CCDS; CCDS69214.1; -. [Q9NP79-2]
DR RefSeq; NP_001273300.1; NM_001286371.1.
DR RefSeq; NP_001273301.1; NM_001286372.1. [Q9NP79-2]
DR RefSeq; NP_057569.2; NM_016485.4. [Q9NP79-1]
DR PDB; 2LXL; NMR; -; A=1-183.
DR PDB; 2LXM; NMR; -; A=1-168.
DR PDB; 4TXP; X-ray; 3.01 A; A/B/C=1-162.
DR PDB; 4TXQ; X-ray; 2.21 A; A/B=1-162.
DR PDB; 4TXR; X-ray; 1.00 A; A=1-162.
DR PDB; 4U7E; X-ray; 1.60 A; B=1-162.
DR PDBsum; 2LXL; -.
DR PDBsum; 2LXM; -.
DR PDBsum; 4TXP; -.
DR PDBsum; 4TXQ; -.
DR PDBsum; 4TXR; -.
DR PDBsum; 4U7E; -.
DR AlphaFoldDB; Q9NP79; -.
DR BMRB; Q9NP79; -.
DR SMR; Q9NP79; -.
DR BioGRID; 119595; 79.
DR IntAct; Q9NP79; 34.
DR STRING; 9606.ENSP00000356602; -.
DR GlyGen; Q9NP79; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NP79; -.
DR MetOSite; Q9NP79; -.
DR PhosphoSitePlus; Q9NP79; -.
DR SwissPalm; Q9NP79; -.
DR BioMuta; VTA1; -.
DR DMDM; 30580379; -.
DR EPD; Q9NP79; -.
DR jPOST; Q9NP79; -.
DR MassIVE; Q9NP79; -.
DR MaxQB; Q9NP79; -.
DR PaxDb; Q9NP79; -.
DR PeptideAtlas; Q9NP79; -.
DR PRIDE; Q9NP79; -.
DR ProteomicsDB; 18265; -.
DR ProteomicsDB; 81922; -. [Q9NP79-1]
DR Antibodypedia; 33094; 138 antibodies from 23 providers.
DR DNASU; 51534; -.
DR Ensembl; ENST00000367630.9; ENSP00000356602.3; ENSG00000009844.16. [Q9NP79-1]
DR Ensembl; ENST00000452973.6; ENSP00000395767.2; ENSG00000009844.16. [Q9NP79-2]
DR GeneID; 51534; -.
DR KEGG; hsa:51534; -.
DR MANE-Select; ENST00000367630.9; ENSP00000356602.3; NM_016485.5; NP_057569.2.
DR UCSC; uc003qiw.5; human. [Q9NP79-1]
DR CTD; 51534; -.
DR DisGeNET; 51534; -.
DR GeneCards; VTA1; -.
DR HGNC; HGNC:20954; VTA1.
DR HPA; ENSG00000009844; Low tissue specificity.
DR MIM; 610902; gene.
DR neXtProt; NX_Q9NP79; -.
DR OpenTargets; ENSG00000009844; -.
DR PharmGKB; PA162408932; -.
DR VEuPathDB; HostDB:ENSG00000009844; -.
DR eggNOG; KOG0917; Eukaryota.
DR GeneTree; ENSGT00390000011342; -.
DR HOGENOM; CLU_030378_1_1_1; -.
DR InParanoid; Q9NP79; -.
DR OMA; AYWCEYH; -.
DR OrthoDB; 1450538at2759; -.
DR PhylomeDB; Q9NP79; -.
DR TreeFam; TF105917; -.
DR PathwayCommons; Q9NP79; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR SignaLink; Q9NP79; -.
DR BioGRID-ORCS; 51534; 38 hits in 1077 CRISPR screens.
DR ChiTaRS; VTA1; human.
DR GeneWiki; VTA1; -.
DR GenomeRNAi; 51534; -.
DR Pharos; Q9NP79; Tbio.
DR PRO; PR:Q9NP79; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NP79; protein.
DR Bgee; ENSG00000009844; Expressed in cortical plate and 191 other tissues.
DR ExpressionAtlas; Q9NP79; baseline and differential.
DR Genevisible; Q9NP79; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:1904903; P:ESCRT III complex disassembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:0036258; P:multivesicular body assembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0046755; P:viral budding; IMP:UniProtKB.
DR Gene3D; 1.25.40.270; -; 1.
DR InterPro; IPR044538; Vta1-like.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR InterPro; IPR041212; Vta1_C.
DR PANTHER; PTHR46009; PTHR46009; 1.
DR Pfam; PF04652; Vta1; 1.
DR Pfam; PF18097; Vta1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..307
FT /note="Vacuolar protein sorting-associated protein VTA1
FT homolog"
FT /id="PRO_0000089509"
FT REGION 2..186
FT /note="Interaction with IST1"
FT REGION 2..75
FT /note="Interaction with CHMP5"
FT REGION 179..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..307
FT /note="Interaction with VPS4B"
FT /evidence="ECO:0000250"
FT COMPBIAS 184..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..69
FT /note="MAALAPLPPLPAQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSK
FT TPECRKFLSKLMDQLEA -> MTSETLWWLIT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056727"
FT VAR_SEQ 234..260
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056728"
FT VARIANT 239
FT /note="I -> M (in dbSNP:rs2232307)"
FT /id="VAR_053917"
FT CONFLICT 14
FT /note="F -> L (in Ref. 4; CAB66619)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..156
FT /note="CL -> V (in Ref. 3; AAF36148)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="A -> V (in Ref. 5; BAG62917)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="E -> D (in Ref. 6; CAG33488)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:4U7E"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:4TXR"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:4TXR"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:4TXR"
FT HELIX 32..49
FT /evidence="ECO:0007829|PDB:4TXR"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4TXR"
FT HELIX 54..73
FT /evidence="ECO:0007829|PDB:4TXR"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:4TXR"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:4TXR"
FT HELIX 83..106
FT /evidence="ECO:0007829|PDB:4TXR"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:4TXR"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4TXR"
FT HELIX 136..158
FT /evidence="ECO:0007829|PDB:4TXR"
SQ SEQUENCE 307 AA; 33879 MW; C7DE611E50B58BF9 CRC64;
MAALAPLPPL PAQFKSIQHH LRTAQEHDKR DPVVAYYCRL YAMQTGMKID SKTPECRKFL
SKLMDQLEAL KKQLGDNEAI TQEIVGCAHL ENYALKMFLY ADNEDRAGRF HKNMIKSFYT
ASLLIDVITV FGELTDENVK HRKYARWKAT YIHNCLKNGE TPQAGPVGIE EDNDIEENED
AGAASLPTQP TQPSSSSTYD PSNMPSGNYT GIQIPPGAHA PANTPAEVPH STGVASNTIQ
PTPQTIPAID PALFNTISQG DVRLTPEDFA RAQKYCKYAG SALQYEDVST AVQNLQKALK
LLTTGRE
