Full text data of VTA1
VTA1
(C6orf55)
[Confidence: low (only semi-automatic identification from reviews)]
Vacuolar protein sorting-associated protein VTA1 homolog (Dopamine-responsive gene 1 protein; DRG-1; LYST-interacting protein 5; LIP5; SKD1-binding protein 1; SBP1)
Vacuolar protein sorting-associated protein VTA1 homolog (Dopamine-responsive gene 1 protein; DRG-1; LYST-interacting protein 5; LIP5; SKD1-binding protein 1; SBP1)
UniProt
Q9NP79
ID VTA1_HUMAN Reviewed; 307 AA.
AC Q9NP79; E1P594; Q5TGM1; Q6IAE8; Q9H0R2; Q9H3K9; Q9P0Q0;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 107.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shi J., Cai W., Xie Y.;
RT "Identification of dopamine responsive genes in glial cells by
RT subtractive hybridization.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Zheng Z.H., Gu S.H., Ying K., Lin Q., Dai J.L.,
RA Tang R., Dong H., Wu X.Z.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: 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 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.,
RA Hill J., 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.,
RA Goettlinger H.G., Kirchhausen T.;
RT "Targeting of AMSH to endosomes is required for epidermal growth
RT factor 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
RT implications for ESCRT-III disassembly.";
RL Mol. Biol. Cell 19:2661-2672(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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
RT interferon-induced gene ISG15.";
RL J. Virol. 85:7153-7161(2011).
CC -!- FUNCTION: Involved in the endosomal multivesicular bodies (MVB)
CC pathway. MVBs contain intraluminal vesicles (ILVs) that are
CC generated by invagination and scission from the limiting membrane
CC of the endosome and mostly are delivered to lysosomes enabling
CC degradation of membrane proteins, such as stimulated growth factor
CC receptors, lysosomal enzymes and lipids. Thought to be a cofactor
CC of VPS4A/B, which catalyzes disassembles membrane-associated
CC ESCRT-III assemblies. Involved in the sorting and down-regulation
CC of EGFR (By similarity). Involved in HIV-1 budding.
CC -!- SUBUNIT: Interacts with VPS4B. Interacts with CHMP1B. Interacts
CC with CHMP2A; the interaction probably involves the open
CC conformation of (polymerized) CHMP2A. Interacts with CHMP3.
CC Interacts with CHMP5; the interaction involves soluble CHMP5.
CC Interacts with IST1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral
CC membrane protein (Probable).
CC -!- SIMILARITY: Belongs to the VTA1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36148.1; Type=Frameshift; Positions=131, 140;
CC Sequence=AAG43125.1; Type=Frameshift; Positions=269;
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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; CR457207; CAG33488.1; -; mRNA.
DR EMBL; AL033522; CAI21072.1; -; 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 RefSeq; NP_001273300.1; NM_001286371.1.
DR RefSeq; NP_001273301.1; NM_001286372.1.
DR RefSeq; NP_057569.2; NM_016485.4.
DR UniGene; Hs.431367; -.
DR PDB; 2LXL; NMR; -; A=1-183.
DR PDB; 2LXM; NMR; -; A=1-168.
DR PDBsum; 2LXL; -.
DR PDBsum; 2LXM; -.
DR ProteinModelPortal; Q9NP79; -.
DR SMR; Q9NP79; 13-163.
DR IntAct; Q9NP79; 17.
DR MINT; MINT-1438279; -.
DR STRING; 9606.ENSP00000356602; -.
DR PhosphoSite; Q9NP79; -.
DR DMDM; 30580379; -.
DR PaxDb; Q9NP79; -.
DR PRIDE; Q9NP79; -.
DR DNASU; 51534; -.
DR Ensembl; ENST00000367630; ENSP00000356602; ENSG00000009844.
DR GeneID; 51534; -.
DR KEGG; hsa:51534; -.
DR UCSC; uc003qiw.3; human.
DR CTD; 51534; -.
DR GeneCards; GC06P142468; -.
DR H-InvDB; HIX0006262; -.
DR HGNC; HGNC:20954; VTA1.
DR HPA; HPA030968; -.
DR MIM; 610902; gene.
DR neXtProt; NX_Q9NP79; -.
DR PharmGKB; PA162408932; -.
DR eggNOG; NOG127441; -.
DR HOVERGEN; HBG050907; -.
DR InParanoid; Q9NP79; -.
DR KO; K12199; -.
DR OMA; LQYEDVG; -.
DR OrthoDB; EOG7JHM66; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR GeneWiki; VTA1; -.
DR GenomeRNAi; 51534; -.
DR NextBio; 55284; -.
DR PRO; PR:Q9NP79; -.
DR ArrayExpress; Q9NP79; -.
DR Bgee; Q9NP79; -.
DR CleanEx; HS_VTA1; -.
DR Genevestigator; Q9NP79; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.25.40.270; -; 1.
DR InterPro; IPR023175; VPS_Vta1/CALS_N-dom.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Endosome; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 307 Vacuolar protein sorting-associated
FT protein VTA1 homolog.
FT /FTId=PRO_0000089509.
FT REGION 2 186 Interaction with IST1.
FT REGION 2 75 Interaction with CHMP5.
FT REGION 198 307 Interaction with VPS4B (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 239 239 I -> M (in dbSNP:rs2232307).
FT /FTId=VAR_053917.
FT CONFLICT 14 14 F -> L (in Ref. 4; CAB66619).
FT CONFLICT 155 156 CL -> V (in Ref. 3; AAF36148).
FT CONFLICT 307 307 E -> D (in Ref. 6; CAG33488).
FT HELIX 12 14
FT STRAND 15 17
FT HELIX 18 30
FT HELIX 32 49
FT HELIX 56 74
FT HELIX 78 81
FT HELIX 83 106
FT HELIX 112 129
FT HELIX 136 157
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
//
ID VTA1_HUMAN Reviewed; 307 AA.
AC Q9NP79; E1P594; Q5TGM1; Q6IAE8; Q9H0R2; Q9H3K9; Q9P0Q0;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 107.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shi J., Cai W., Xie Y.;
RT "Identification of dopamine responsive genes in glial cells by
RT subtractive hybridization.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Zheng Z.H., Gu S.H., Ying K., Lin Q., Dai J.L.,
RA Tang R., Dong H., Wu X.Z.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: 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 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.,
RA Hill J., 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.,
RA Goettlinger H.G., Kirchhausen T.;
RT "Targeting of AMSH to endosomes is required for epidermal growth
RT factor 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
RT implications for ESCRT-III disassembly.";
RL Mol. Biol. Cell 19:2661-2672(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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
RT interferon-induced gene ISG15.";
RL J. Virol. 85:7153-7161(2011).
CC -!- FUNCTION: Involved in the endosomal multivesicular bodies (MVB)
CC pathway. MVBs contain intraluminal vesicles (ILVs) that are
CC generated by invagination and scission from the limiting membrane
CC of the endosome and mostly are delivered to lysosomes enabling
CC degradation of membrane proteins, such as stimulated growth factor
CC receptors, lysosomal enzymes and lipids. Thought to be a cofactor
CC of VPS4A/B, which catalyzes disassembles membrane-associated
CC ESCRT-III assemblies. Involved in the sorting and down-regulation
CC of EGFR (By similarity). Involved in HIV-1 budding.
CC -!- SUBUNIT: Interacts with VPS4B. Interacts with CHMP1B. Interacts
CC with CHMP2A; the interaction probably involves the open
CC conformation of (polymerized) CHMP2A. Interacts with CHMP3.
CC Interacts with CHMP5; the interaction involves soluble CHMP5.
CC Interacts with IST1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral
CC membrane protein (Probable).
CC -!- SIMILARITY: Belongs to the VTA1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36148.1; Type=Frameshift; Positions=131, 140;
CC Sequence=AAG43125.1; Type=Frameshift; Positions=269;
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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; CR457207; CAG33488.1; -; mRNA.
DR EMBL; AL033522; CAI21072.1; -; 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 RefSeq; NP_001273300.1; NM_001286371.1.
DR RefSeq; NP_001273301.1; NM_001286372.1.
DR RefSeq; NP_057569.2; NM_016485.4.
DR UniGene; Hs.431367; -.
DR PDB; 2LXL; NMR; -; A=1-183.
DR PDB; 2LXM; NMR; -; A=1-168.
DR PDBsum; 2LXL; -.
DR PDBsum; 2LXM; -.
DR ProteinModelPortal; Q9NP79; -.
DR SMR; Q9NP79; 13-163.
DR IntAct; Q9NP79; 17.
DR MINT; MINT-1438279; -.
DR STRING; 9606.ENSP00000356602; -.
DR PhosphoSite; Q9NP79; -.
DR DMDM; 30580379; -.
DR PaxDb; Q9NP79; -.
DR PRIDE; Q9NP79; -.
DR DNASU; 51534; -.
DR Ensembl; ENST00000367630; ENSP00000356602; ENSG00000009844.
DR GeneID; 51534; -.
DR KEGG; hsa:51534; -.
DR UCSC; uc003qiw.3; human.
DR CTD; 51534; -.
DR GeneCards; GC06P142468; -.
DR H-InvDB; HIX0006262; -.
DR HGNC; HGNC:20954; VTA1.
DR HPA; HPA030968; -.
DR MIM; 610902; gene.
DR neXtProt; NX_Q9NP79; -.
DR PharmGKB; PA162408932; -.
DR eggNOG; NOG127441; -.
DR HOVERGEN; HBG050907; -.
DR InParanoid; Q9NP79; -.
DR KO; K12199; -.
DR OMA; LQYEDVG; -.
DR OrthoDB; EOG7JHM66; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR GeneWiki; VTA1; -.
DR GenomeRNAi; 51534; -.
DR NextBio; 55284; -.
DR PRO; PR:Q9NP79; -.
DR ArrayExpress; Q9NP79; -.
DR Bgee; Q9NP79; -.
DR CleanEx; HS_VTA1; -.
DR Genevestigator; Q9NP79; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.25.40.270; -; 1.
DR InterPro; IPR023175; VPS_Vta1/CALS_N-dom.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Endosome; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 307 Vacuolar protein sorting-associated
FT protein VTA1 homolog.
FT /FTId=PRO_0000089509.
FT REGION 2 186 Interaction with IST1.
FT REGION 2 75 Interaction with CHMP5.
FT REGION 198 307 Interaction with VPS4B (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 239 239 I -> M (in dbSNP:rs2232307).
FT /FTId=VAR_053917.
FT CONFLICT 14 14 F -> L (in Ref. 4; CAB66619).
FT CONFLICT 155 156 CL -> V (in Ref. 3; AAF36148).
FT CONFLICT 307 307 E -> D (in Ref. 6; CAG33488).
FT HELIX 12 14
FT STRAND 15 17
FT HELIX 18 30
FT HELIX 32 49
FT HELIX 56 74
FT HELIX 78 81
FT HELIX 83 106
FT HELIX 112 129
FT HELIX 136 157
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
//
MIM
610902
*RECORD*
*FIELD* NO
610902
*FIELD* TI
*610902 CHROMOSOME 6 OPEN READING FRAME 55; C6ORF55
;;SKD1-BINDING PROTEIN 1; SBP1;;
read moreLYST-INTERACTING PROTEIN 5; LIP5;;
VTA1, YEAST, HOMOLOG OF; VTA1;;
DOPAMINE-RESPONSIVE GENE 1; DRG1
*FIELD* TX
DESCRIPTION
C6ORF55 encodes a protein involved in trafficking of the multivesicular
body, an endosomal compartment involved in sorting membrane proteins for
degradation in lysosomes (Ward et al., 2005).
CLONING
Using subtractive hybridization to identify genes upregulated by
dopamine in rat cerebral astrocytes, followed by screening a human fetal
brain cDNA library, Shi et al. (2001) cloned C6ORF55. The transcript
contains a novel (CAG)n repeat that encodes polyglutamines.
Using yeast 2-hybrid analysis to screen human cDNA libraries for genes
encoding LYST (606897)-interacting proteins, Tchernev et al. (2002)
cloned C6ORF55, which they called LIP5.
Using Skd1 (VPS4B; 609983) as bait in a yeast 2-hybrid screen of a mouse
brain cDNA library, Fujita et al. (2004) cloned C6orf55, which they
called Sbp1. By database analysis, they identified multiple human cDNAs
corresponding to SBP1, including 2 that encode 307- and 282-amino acid
proteins, designated DRG1 and LIP5, respectively, that are identical in
their first 157 amino acids but differ in their C termini. Fujita et al.
(2004) suggested that these cDNAs encode distinct proteins due to small
sequence alterations rather than alternative splicing. The deduced
309-amino acid mouse protein contains N- and C-terminal coiled-coil
domains. The N-terminal region of SBP1 is rich in basic amino acids,
whereas the C-terminal region is acidic. Northern blot analysis detected
Sbp1 expression in most mouse tissues examined, with highest levels in
heart, brain, liver, and kidney. Immunofluorescence analysis of HeLa
cells showed that endogenous human SBP1 localized to the cytosol.
By sequence analysis, Ward et al. (2005) determined that the LIP5 cDNA
encoding the 282-amino acid protein contains a frameshift, and that the
full-length LIP5 protein contains 307 amino acids. Cell fractionation of
COS-7 cells followed by Western blot analysis showed that epitope-tagged
LIP5 was primarily cytosolic.
GENE FUNCTION
By yeast 2-hybrid analysis and pull-down assays, Fujita et al. (2004)
showed that the C-terminal region of mouse Sbp1 bound Skd1. Expression
of an ATPase-negative mouse Skd1 mutant in HeLa cells redirected
endogenous SBP1 and SKD1 from the cytosol to an aberrant endosomal
structure derived from early and late endosomes and lysosomes. In
control HeLa cells, SKD1 existed as a monomer, and SBP1 formed an
oligomer protein complex. The ATPase-negative Skd1 mutant formed large
heterooligomers with endogenous SBP1 and SKD1 when expressed in HeLa
cells, suggesting that the ATPase activity of SKD1 is required for
disassembly of the SBP1/SKD1 complex.
Using affinity purification experiments, Ward et al. (2005) showed that
LIP5 specifically interacted with CHMP5 (610900). Depletion of LIP5 by
small-interfering RNA did not alter the distribution of early or late
endocytic markers in HeLa and 293T cells, but it altered EGFR (131550)
trafficking and reduced EGFR degradation in lysosomes. Depletion of LIP5
in 293T cells infected with human immunodeficiency virus (HIV)-1 reduced
release of infectious particles.
MAPPING
By genomic sequence analysis, Fujita et al. (2004) mapped the C6ORF55
gene to chromosome 6.
*FIELD* RF
1. Fujita, H.; Umezuki, Y.; Imamura, K.; Ishikawa, D.; Uchimura, S.;
Nara, A.; Yoshimori, T.; Hayashizaki, Y.; Kawai, J.; Ishidoh, K.;
Tanaka, Y.; Himeno, M.: Mammalian class E Vps proteins, SBP1 and
mVps2/CHMP2A, interact with and regulate the function of an AAA-ATPase
SKD1/Vps4B. J. Cell Sci. 117: 2997-3009, 2004.
2. Shi, J.; Cai, W.; Chen, X.; Ying, K.; Zhang, K.; Xie, Y.: Identification
of dopamine responsive mRNAs in glial cells by suppression subtractive
hybridization. Brain Res. 910: 29-37, 2001.
3. Tchernev, V. T.; Mansfield, T. A.; Giot, L.; Kumar, A. M.; Nandabalan,
K.; Li, Y.; Mishra, V. S.; Detter, J. C.; Rothberg, J. M.; Wallace,
M. R.; Southwick, F. S.; Kingsmore, S. F.: The Chediak-Higashi protein
interacts with SNARE complex and signal transduction proteins. Molec.
Med. 8: 56-64, 2002.
4. Ward, D. M.; Vaughn, M. B.; Shiflett, S. L.; White, P. L.; Pollock,
A. L.; Hill, J.; Schnegelberger, R.; Sundquist, W. I.; Kaplan, J.
: The role of LIP5 and CHMP5 in multivesicular body formation and
HIV-1 budding in mammalian cells. J. Biol. Chem. 280: 10548-10555,
2005.
*FIELD* CD
Patricia A. Hartz: 3/30/2007
*FIELD* ED
mgross: 03/30/2007
*RECORD*
*FIELD* NO
610902
*FIELD* TI
*610902 CHROMOSOME 6 OPEN READING FRAME 55; C6ORF55
;;SKD1-BINDING PROTEIN 1; SBP1;;
read moreLYST-INTERACTING PROTEIN 5; LIP5;;
VTA1, YEAST, HOMOLOG OF; VTA1;;
DOPAMINE-RESPONSIVE GENE 1; DRG1
*FIELD* TX
DESCRIPTION
C6ORF55 encodes a protein involved in trafficking of the multivesicular
body, an endosomal compartment involved in sorting membrane proteins for
degradation in lysosomes (Ward et al., 2005).
CLONING
Using subtractive hybridization to identify genes upregulated by
dopamine in rat cerebral astrocytes, followed by screening a human fetal
brain cDNA library, Shi et al. (2001) cloned C6ORF55. The transcript
contains a novel (CAG)n repeat that encodes polyglutamines.
Using yeast 2-hybrid analysis to screen human cDNA libraries for genes
encoding LYST (606897)-interacting proteins, Tchernev et al. (2002)
cloned C6ORF55, which they called LIP5.
Using Skd1 (VPS4B; 609983) as bait in a yeast 2-hybrid screen of a mouse
brain cDNA library, Fujita et al. (2004) cloned C6orf55, which they
called Sbp1. By database analysis, they identified multiple human cDNAs
corresponding to SBP1, including 2 that encode 307- and 282-amino acid
proteins, designated DRG1 and LIP5, respectively, that are identical in
their first 157 amino acids but differ in their C termini. Fujita et al.
(2004) suggested that these cDNAs encode distinct proteins due to small
sequence alterations rather than alternative splicing. The deduced
309-amino acid mouse protein contains N- and C-terminal coiled-coil
domains. The N-terminal region of SBP1 is rich in basic amino acids,
whereas the C-terminal region is acidic. Northern blot analysis detected
Sbp1 expression in most mouse tissues examined, with highest levels in
heart, brain, liver, and kidney. Immunofluorescence analysis of HeLa
cells showed that endogenous human SBP1 localized to the cytosol.
By sequence analysis, Ward et al. (2005) determined that the LIP5 cDNA
encoding the 282-amino acid protein contains a frameshift, and that the
full-length LIP5 protein contains 307 amino acids. Cell fractionation of
COS-7 cells followed by Western blot analysis showed that epitope-tagged
LIP5 was primarily cytosolic.
GENE FUNCTION
By yeast 2-hybrid analysis and pull-down assays, Fujita et al. (2004)
showed that the C-terminal region of mouse Sbp1 bound Skd1. Expression
of an ATPase-negative mouse Skd1 mutant in HeLa cells redirected
endogenous SBP1 and SKD1 from the cytosol to an aberrant endosomal
structure derived from early and late endosomes and lysosomes. In
control HeLa cells, SKD1 existed as a monomer, and SBP1 formed an
oligomer protein complex. The ATPase-negative Skd1 mutant formed large
heterooligomers with endogenous SBP1 and SKD1 when expressed in HeLa
cells, suggesting that the ATPase activity of SKD1 is required for
disassembly of the SBP1/SKD1 complex.
Using affinity purification experiments, Ward et al. (2005) showed that
LIP5 specifically interacted with CHMP5 (610900). Depletion of LIP5 by
small-interfering RNA did not alter the distribution of early or late
endocytic markers in HeLa and 293T cells, but it altered EGFR (131550)
trafficking and reduced EGFR degradation in lysosomes. Depletion of LIP5
in 293T cells infected with human immunodeficiency virus (HIV)-1 reduced
release of infectious particles.
MAPPING
By genomic sequence analysis, Fujita et al. (2004) mapped the C6ORF55
gene to chromosome 6.
*FIELD* RF
1. Fujita, H.; Umezuki, Y.; Imamura, K.; Ishikawa, D.; Uchimura, S.;
Nara, A.; Yoshimori, T.; Hayashizaki, Y.; Kawai, J.; Ishidoh, K.;
Tanaka, Y.; Himeno, M.: Mammalian class E Vps proteins, SBP1 and
mVps2/CHMP2A, interact with and regulate the function of an AAA-ATPase
SKD1/Vps4B. J. Cell Sci. 117: 2997-3009, 2004.
2. Shi, J.; Cai, W.; Chen, X.; Ying, K.; Zhang, K.; Xie, Y.: Identification
of dopamine responsive mRNAs in glial cells by suppression subtractive
hybridization. Brain Res. 910: 29-37, 2001.
3. Tchernev, V. T.; Mansfield, T. A.; Giot, L.; Kumar, A. M.; Nandabalan,
K.; Li, Y.; Mishra, V. S.; Detter, J. C.; Rothberg, J. M.; Wallace,
M. R.; Southwick, F. S.; Kingsmore, S. F.: The Chediak-Higashi protein
interacts with SNARE complex and signal transduction proteins. Molec.
Med. 8: 56-64, 2002.
4. Ward, D. M.; Vaughn, M. B.; Shiflett, S. L.; White, P. L.; Pollock,
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*FIELD* CD
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mgross: 03/30/2007