VPS53_SCHPO
ID VPS53_SCHPO Reviewed; 756 AA.
AC P87129;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Vacuolar protein sorting-associated protein 53;
DE AltName: Full=GARP complex subunit vps53;
GN Name=vps53; ORFNames=SPAC3A12.15;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in retrograde transport from early and late
CC endosomes to late Golgi, leading to the membrane fusion between late
CC Golgi and endosomal vesicles. {ECO:0000250}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS53 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB08743.1; -; Genomic_DNA.
DR PIR; T38683; T38683.
DR RefSeq; NP_593341.1; NM_001018773.2.
DR AlphaFoldDB; P87129; -.
DR STRING; 4896.SPAC3A12.15.1; -.
DR iPTMnet; P87129; -.
DR MaxQB; P87129; -.
DR PaxDb; P87129; -.
DR PRIDE; P87129; -.
DR EnsemblFungi; SPAC3A12.15.1; SPAC3A12.15.1:pep; SPAC3A12.15.
DR GeneID; 2542930; -.
DR KEGG; spo:SPAC3A12.15; -.
DR PomBase; SPAC3A12.15; vps53.
DR VEuPathDB; FungiDB:SPAC3A12.15; -.
DR eggNOG; KOG2180; Eukaryota.
DR HOGENOM; CLU_007339_1_0_1; -.
DR InParanoid; P87129; -.
DR OMA; YKFAEAK; -.
DR PhylomeDB; P87129; -.
DR PRO; PR:P87129; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000938; C:GARP complex; ISO:PomBase.
DR GO; GO:0006896; P:Golgi to vacuole transport; ISO:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:PomBase.
DR Gene3D; 1.10.357.110; -; 1.
DR InterPro; IPR039766; Vps53.
DR InterPro; IPR038260; Vps53_C_sf.
DR InterPro; IPR007234; Vps53_N.
DR PANTHER; PTHR12820; PTHR12820; 1.
DR Pfam; PF04100; Vps53_N; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Endosome; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..756
FT /note="Vacuolar protein sorting-associated protein 53"
FT /id="PRO_0000116639"
FT COILED 44..130
FT /evidence="ECO:0000255"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 756 AA; 87506 MW; F45BF6355AF31B48 CRC64;
MSNGNDNSLI IKNIGNNEFK FVETLHELLP EDITYDDLGS LRLSLSERLQ ESVKKLDANK
KTYEDAKLSM GEKMDDLNSS IVSLLQELST LQSVAENTQS SIVQMTSEIK NLDFAKQNLA
TSMTMLKRLQ MLVTAYEKLR TLRQNQKFGE AISLMQATLQ LLNFFKKYRS VERIASLSRS
ISEFQKSFYE QVFDTFQSQF KKESGMRGGF SPSSVQYLNE LCRFIDIFAG DPPESVIRWY
CRHQLEDFMK VFRENEEAGS LENLPRRYTW FKKLLQTYDQ LHKPIFPPHW KVDFRLYEVF
CEETKNDLSK LLKDDRLSLQ VFVASLEQTL EFESFIDHRF YNTKSRFNSN FEPKERQAYN
ALSSVFEPHY TLYFNQQSQE FSILFENFAL EKQTSTDESS QVLSSSIKLF QAYRKTLTQF
VRLTRSSPLV GLKNLFIKWL RRYTQVELLD YQESSTFKDI AIRLNTAEYI YRTTIELEKR
FQEISNKEFK DKMSFSEVLE VISSSRGTLL KFATGKFENV LNSDLEPLSK MDLKNIETVG
DQSSYVGGAV QNMTAKASEF LSVVDLNMFA RNFCDRSCES FTRQFLNAIY LAKPISEVGA
EQLLLDLYSF KNALLKLPDL KQDYSITDSY INHLTIFMGY IETVLKTLLT PASPKAGFIQ
SYIFLVKDRS VTNFTVLLEL KGVGKSDISS FLQQFSDFVK KTPQLEESSP IFKYLTINTA
VEQAATRSRL SLDLAPESSR TLQNLGRLFT SKKKHV
