VTA1_MOUSE
ID VTA1_MOUSE Reviewed; 309 AA.
AC Q9CR26;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Vacuolar protein sorting-associated protein VTA1 homolog;
DE AltName: Full=SKD1-binding protein 1;
DE Short=SBP1;
GN Name=Vta1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP FUNCTION, INTERACTION WITH VPS4B, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15173323; DOI=10.1242/jcs.01170;
RA Fujita H., Umezuki Y., Imamura K., Ishikawa D., Uchimura S., Nara A.,
RA Yoshimori T., Hayashizaki Y., Kawai J., Ishidoh K., Tanaka Y., Himeno M.;
RT "Mammalian class E Vps proteins, SBP1 and mVps2/CHMP2A, interact with and
RT regulate the function of an AAA-ATPase SKD1/Vps4B.";
RL J. Cell Sci. 117:2997-3009(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC Involved in the sorting and down-regulation of EGFR. {ECO:0000250,
CC ECO:0000269|PubMed:15173323}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15173323}. Endosome
CC membrane {ECO:0000269|PubMed:15173323}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15173323}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, liver,
CC kidney, spleen, lung and heart (at protein level).
CC {ECO:0000269|PubMed:15173323}.
CC -!- SIMILARITY: Belongs to the VTA1 family. {ECO:0000305}.
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DR EMBL; AK002611; BAB22228.1; -; mRNA.
DR EMBL; AK009227; BAB26150.1; -; mRNA.
DR EMBL; BC026752; AAH26752.1; -; mRNA.
DR CCDS; CCDS23705.1; -.
DR RefSeq; NP_079694.2; NM_025418.3.
DR AlphaFoldDB; Q9CR26; -.
DR BMRB; Q9CR26; -.
DR SMR; Q9CR26; -.
DR BioGRID; 211293; 12.
DR DIP; DIP-54810N; -.
DR IntAct; Q9CR26; 3.
DR STRING; 10090.ENSMUSP00000119829; -.
DR iPTMnet; Q9CR26; -.
DR PhosphoSitePlus; Q9CR26; -.
DR CPTAC; non-CPTAC-3754; -.
DR EPD; Q9CR26; -.
DR jPOST; Q9CR26; -.
DR MaxQB; Q9CR26; -.
DR PaxDb; Q9CR26; -.
DR PeptideAtlas; Q9CR26; -.
DR PRIDE; Q9CR26; -.
DR ProteomicsDB; 297614; -.
DR Antibodypedia; 33094; 138 antibodies from 23 providers.
DR DNASU; 66201; -.
DR Ensembl; ENSMUST00000154132; ENSMUSP00000119829; ENSMUSG00000019868.
DR GeneID; 66201; -.
DR KEGG; mmu:66201; -.
DR UCSC; uc007ell.1; mouse.
DR CTD; 51534; -.
DR MGI; MGI:1913451; Vta1.
DR VEuPathDB; HostDB:ENSMUSG00000019868; -.
DR eggNOG; KOG0917; Eukaryota.
DR GeneTree; ENSGT00390000011342; -.
DR InParanoid; Q9CR26; -.
DR OMA; AYWCEYH; -.
DR OrthoDB; 1450538at2759; -.
DR PhylomeDB; Q9CR26; -.
DR TreeFam; TF105917; -.
DR Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 66201; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Vta1; mouse.
DR PRO; PR:Q9CR26; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CR26; protein.
DR Bgee; ENSMUSG00000019868; Expressed in animal zygote and 258 other tissues.
DR ExpressionAtlas; Q9CR26; baseline and differential.
DR Genevisible; Q9CR26; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0071985; P:multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0046755; P:viral budding; ISO:MGI.
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 Acetylation; Cytoplasm; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NP79"
FT CHAIN 2..309
FT /note="Vacuolar protein sorting-associated protein VTA1
FT homolog"
FT /id="PRO_0000089510"
FT REGION 2..186
FT /note="Interaction with IST1"
FT /evidence="ECO:0000250"
FT REGION 2..75
FT /note="Interaction with CHMP5"
FT /evidence="ECO:0000250"
FT REGION 173..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..309
FT /note="Interaction with VPS4B"
FT /evidence="ECO:0000269|PubMed:15173323"
FT COMPBIAS 182..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP79"
SQ SEQUENCE 309 AA; 33913 MW; 2D37B56A571A0157 CRC64;
MAALAPLPPL PAQFKSIQHH LRTAQEHDKR DPVVAYYCRL YAMQTGMKID SKTPECRKFL
SKLMDQLEAL KKQLGDNEAV TQEIVGCAHL ENYALKMFLY ADNEDRAGRF HKNMIKSFYT
ASLLIDVITV FGELTDENVK HRKYARWKAT YIHNCLKNGE TPQAGPVGIE EENDVEENED
VGATSLPTQP PQPSSSSAYD PSNLAPGSYS GIQIPPGAHA PANTPAEVPH STGVTSNAVQ
PSPQTVPAAP AVDPDLYTAS QGDIRLTPED FARAQKYCKY AGSALQYEDV GTAVQNLQKA
LRLLTTGRE
