VPS5_SCHPO
ID VPS5_SCHPO Reviewed; 576 AA.
AC Q9C0U7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Vacuolar protein sorting-associated protein vps5;
GN Name=vps5; ORFNames=SPCPJ732.01;
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 CHARACTERIZATION.
RX PubMed=15189449; DOI=10.1111/j.1356-9597.2004.00744.x;
RA Koga T., Onishi M., Nakamura Y., Hirata A., Nakamura T., Shimoda C.,
RA Iwaki T., Takegawa K., Fukui Y.;
RT "Sorting nexin homologues are targets of phosphatidylinositol 3-phosphate
RT in sporulation of Schizosaccharomyces pombe.";
RL Genes Cells 9:561-574(2004).
RN [3]
RP FUNCTION.
RX PubMed=16622069; DOI=10.1099/mic.0.28627-0;
RA Iwaki T., Hosomi A., Tokudomi S., Kusunoki Y., Fujita Y., Giga-Hama Y.,
RA Tanaka N., Takegawa K.;
RT "Vacuolar protein sorting receptor in Schizosaccharomyces pombe.";
RL Microbiology 152:1523-1532(2006).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55 AND SER-332, AND
RP IDENTIFICATION BY 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: Required for efficient sporulation target of PtdIns(3)P in
CC vesicle transport required for onset of the forespore membrane
CC formation. {ECO:0000269|PubMed:16622069}.
CC -!- FUNCTION: Plays a role in vesicular protein sorting. Required for the
CC endosome-to-Golgi retrieval of the vacuolar protein sorting receptor
CC pep1/vps10. Component of the membrane-associated retromer complex which
CC is essential in endosome-to-Golgi retrograde transport. The vps29-
CC vps26-vps35 subcomplex may be involved in cargo selection.
CC {ECO:0000269|PubMed:16622069}.
CC -!- SUBUNIT: Component of the retromer complex which consists of vps29,
CC vps26, vps35, vps5 and vps17. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Golgi
CC apparatus {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; CU329672; CAC34987.1; -; Genomic_DNA.
DR RefSeq; NP_587929.1; NM_001022920.2.
DR AlphaFoldDB; Q9C0U7; -.
DR SMR; Q9C0U7; -.
DR BioGRID; 276113; 147.
DR STRING; 4896.SPCPJ732.01.1; -.
DR iPTMnet; Q9C0U7; -.
DR MaxQB; Q9C0U7; -.
DR PaxDb; Q9C0U7; -.
DR PRIDE; Q9C0U7; -.
DR EnsemblFungi; SPCPJ732.01.1; SPCPJ732.01.1:pep; SPCPJ732.01.
DR GeneID; 2539552; -.
DR KEGG; spo:SPCPJ732.01; -.
DR PomBase; SPCPJ732.01; vps5.
DR VEuPathDB; FungiDB:SPCPJ732.01; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_014571_2_0_1; -.
DR InParanoid; Q9C0U7; -.
DR OMA; TWLESAI; -.
DR PhylomeDB; Q9C0U7; -.
DR PRO; PR:Q9C0U7; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005768; C:endosome; IMP:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0030904; C:retromer complex; IMP:PomBase.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISM:PomBase.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IMP:PomBase.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:PomBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:PomBase.
DR CDD; cd07627; BAR_Vps5p; 1.
DR CDD; cd06861; PX_Vps5p; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035803; BAR_Vps5.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR037868; PX_Vps5.
DR InterPro; IPR028648; Vps5-like.
DR InterPro; IPR015404; Vps5_C.
DR PANTHER; PTHR10555:SF170; PTHR10555:SF170; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Sporulation; Transport.
FT CHAIN 1..576
FT /note="Vacuolar protein sorting-associated protein vps5"
FT /id="PRO_0000213803"
FT DOMAIN 200..317
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 244
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 576 AA; 64230 MW; D8CC2B20CA3D09AD CRC64;
MLGHNIYEED DAFNPFADSV SPLNPPKTDQ EPSAEGVEEE SPNVQASPPK THIYTSPRKR
SVNLKSLPFE TLTLDSAPLG PLQFSDAPSM APENNRLEVG LNTKINPLKG SSPALNADFS
ANKPWISEVN SFSPSPIGAT ENPTIPNSEQ TVDTLDAASS SAPNFTHTVS SASSQKQGST
SLTDTENQKA HPAAAPQSLT PFYIQVHDPH TVKEITKSHT VYSVSTRLEE HNQPSVSNVT
VQRRYNDFAF LYQLLSNNHP GCIIPPIPEK QVVGRFDDEF IEQRRAALEV MLRKISAHPV
LRDDYSFKLF LEAETFDPRM THRTTLIESS SSPLRSGPST SGLLDSFTSA FHTSGSSKFS
EQDPILIEAK DTLDSLETQL KSVYHALLLS IDQRIQFASA IHDFGEAVGN LSLVDLEPTL
SSKFDGLSQL QVELRFVQER KVAQDNLTLG TTLEEYIRYV ESAKNAFTTR QKLWQTWQSS
VQAVSRAKTQ LEKCKKQAKS QQKSLPYLEE QYEKYRAKAA DLEKEFSEST TLLKRDLSSL
TTSRVDDLKA SVETWLESAI ESQKEIIERW ESFLDQ
