VTA1_SCHPO
ID VTA1_SCHPO Reviewed; 389 AA.
AC O13703;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Vacuolar protein sorting-associated protein vts1;
DE AltName: Full=VPS20-associated protein 1;
GN Name=vts1; Synonyms=new6; ORFNames=SPAC13F5.04c, SPAC13F5.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP IDENTIFICATION.
RX PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA Hagan I.M., Miller C.J.;
RT "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT additional genes required for growth and viability.";
RL Genetics 187:1207-1217(2011).
CC -!- FUNCTION: Has a role in the formation of the multivesicular body (MVB).
CC Required for the sorting of lipids to form intralumenal vesicles and
CC for fluid-phase transport to the vacuole. Required for sorting several
CC plasma membrane proteins into the MVB (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (in cytoplasm). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06263}.
CC Endosome membrane {ECO:0000250|UniProtKB:Q06263}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q06263}.
CC -!- SIMILARITY: Belongs to the VTA1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11767.2; -; Genomic_DNA.
DR PIR; T37629; T37629.
DR RefSeq; NP_593652.2; NM_001019084.2.
DR AlphaFoldDB; O13703; -.
DR SMR; O13703; -.
DR BioGRID; 279336; 9.
DR STRING; 4896.SPAC13F5.04c.1; -.
DR iPTMnet; O13703; -.
DR MaxQB; O13703; -.
DR PaxDb; O13703; -.
DR PRIDE; O13703; -.
DR EnsemblFungi; SPAC13F5.04c.1; SPAC13F5.04c.1:pep; SPAC13F5.04c.
DR GeneID; 2542892; -.
DR KEGG; spo:SPAC13F5.04c; -.
DR PomBase; SPAC13F5.04c; -.
DR VEuPathDB; FungiDB:SPAC13F5.04c; -.
DR eggNOG; KOG0917; Eukaryota.
DR HOGENOM; CLU_877604_0_0_1; -.
DR InParanoid; O13703; -.
DR OMA; AYWCEYH; -.
DR Reactome; R-SPO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR PRO; PR:O13703; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005771; C:multivesicular body; ISO:PomBase.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; ISO:PomBase.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cytoplasm; Endosome; Lipid transport; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..389
FT /note="Vacuolar protein sorting-associated protein vts1"
FT /id="PRO_0000372360"
FT REGION 149..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 42305 MW; E807E2D5065EB384 CRC64;
MIQIDTIPKE LQSIQPFVRR FNELEAHNPV IAYWSLYWAA QMALSSSHGV SNECKDFLLS
LIEHLEDLRK NLGENENVSD ETSAKAYVES FSLEVLVQAE RNSKNGKPDV QAYLAARDFL
ELSRIWGPPT EQITKSIKFC KLRALQVANP QRKAKTPSNH ATEELQQSST NSTTLPTQEA
AVETNASASH ETSFALPTTS PAASLSISPT KSAAVSSEPN VEADVKSLSS TPAAPQLNSP
SHSYEPTTFP STTSITENLP TIDPTRSTRS SSHIQSLSPE SKQTSDGHRP PSPTSITTTS
TSIDPSVAFS SKSTLATTRT NAPLSRPSQP TKASPLNKFS ALEAIQSARS HARYAYSALD
YEDTTTAIHH LKSALKLLEE EEQGNHTAD