ID   VPS35_SCHPO             Reviewed;         836 AA.
AC   O74552; P78830;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 2.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Vacuolar protein sorting-associated protein 35;
GN   Name=vps35; ORFNames=SPCC777.13;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 330-836.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [4]
RP   FUNCTION.
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   [5]
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   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-318 AND SER-783, 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).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=20537132; DOI=10.1186/gb-2010-11-6-r60;
RA   Han T.X., Xu X.Y., Zhang M.J., Peng X., Du L.L.;
RT   "Global fitness profiling of fission yeast deletion strains by barcode
RT   sequencing.";
RL   Genome Biol. 11:R60.1-R60.13(2010).
CC   -!- FUNCTION: Plays a role in vesicular protein sorting. Required for the
CC       endosome-to-Golgi retrieval of the vacuolar protein sorting receptor
CC       vps10. Required to form proper forespore membranes.
CC       {ECO:0000269|PubMed:15189449, ECO:0000269|PubMed:16622069}.
CC   -!- SUBUNIT: Component of the retromer complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Leads to sensitivity to thiabendazole and
CC       microtubule depolymerizing drugs. {ECO:0000269|PubMed:20537132}.
CC   -!- SIMILARITY: Belongs to the VPS35 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA20717.2; -; Genomic_DNA.
DR   EMBL; D89178; BAA13840.1; -; mRNA.
DR   PIR; T11719; T11719.
DR   RefSeq; NP_588260.2; NM_001023250.2.
DR   AlphaFoldDB; O74552; -.
DR   SMR; O74552; -.
DR   BioGRID; 276025; 287.
DR   STRING; 4896.SPCC777.13.1; -.
DR   iPTMnet; O74552; -.
DR   MaxQB; O74552; -.
DR   PaxDb; O74552; -.
DR   PRIDE; O74552; -.
DR   EnsemblFungi; SPCC777.13.1; SPCC777.13.1:pep; SPCC777.13.
DR   GeneID; 2539462; -.
DR   KEGG; spo:SPCC777.13; -.
DR   PomBase; SPCC777.13; vps35.
DR   VEuPathDB; FungiDB:SPCC777.13; -.
DR   eggNOG; KOG1107; Eukaryota.
DR   HOGENOM; CLU_005836_0_0_1; -.
DR   InParanoid; O74552; -.
DR   OMA; WWVVENP; -.
DR   Reactome; R-SPO-3238698; WNT ligand biogenesis and trafficking.
DR   PRO; PR:O74552; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005768; C:endosome; IMP:PomBase.
DR   GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR   GO; GO:0030904; C:retromer complex; IMP:PomBase.
DR   GO; GO:0030906; C:retromer, cargo-selective complex; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:PomBase.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:PomBase.
DR   Gene3D; 1.25.40.660; -; 1.
DR   InterPro; IPR005378; Vps35.
DR   InterPro; IPR042491; Vps35_C.
DR   PANTHER; PTHR11099; PTHR11099; 1.
DR   Pfam; PF03635; Vps35; 1.
DR   PIRSF; PIRSF009375; Retromer_Vps35; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..836
FT                   /note="Vacuolar protein sorting-associated protein 35"
FT                   /id="PRO_0000065898"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         783
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        388
FT                   /note="S -> P (in Ref. 3; BAA13840)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   836 AA;  96408 MW;  FBB26C7CABF7DADB CRC64;
     MNGINTANEE ITRSLEESLN ICKQSSRLMQ RNLQTGRLMD AFRNCSISLV EMRNSALTPK
     QYYELYMFNM ESLRLLGGTL LETHLNGTHN LMDLYELVQY AGSIVPRLYL MITVGSAYLE
     TPNALVREIM NDLLDMCRGV QHPLRGLFLR HYLLTQTRKG LPLGSEDEED ASRKGTVLDS
     VKFLVINFTE MNKLWVRIQH LGPIKEFSKR TQERNELKVL VGLNLVRLSQ LNLDIDTYRD
     HVLPAIIEQI IECRDSLAQE YLVEVICQAF SDNMHLQTLD TYFGTVIKLS PSVNVTQLVV
     AMLNRLTDYV QREYESDSSN EDESETVTEK LGDIKINEEV QQKDEQECPG DKVIPPEYAI
     QEVLWSHVVE VIQSRSGLPL DCIVSILSSI LNFFLRCYPY KPQYADRVFQ YINEHIINQP
     SLRSALHERP LQKSLCAILL LPLTYFPSFS YCLELQNFLP VFNAQDPNLR YDIARMIVQK
     IIEKGHSLSE LTEAQELLGF VSVIIEKKGV DSLDDLQNVA LMVHYLNNDD PQIQIEILRS
     LKDTFIKAGE NVKYLLPVVV NRCIFLARNF RIFKCMDWAE KVRLLWEFVN TCINVLYKNG
     DSLELCLALY LSAAEMADQE NYPDFAYEFF TQAFSIYEES VLDSELQYQQ LLMIIGKLQK
     TRNFSVDDYD TLITKCTLYA SKLLKKPDQC CGIYLASHLW WQVASGEDSR PFQDPKRVLE
     CLQKSLKIAD ACMDQLTSLK LFINILERYF YYYDQHCESI IAKHISGLID LTEQNMRSIL
     ISSPADLIAS DPRAYASSIW EVANVSVIDS LKNHLERATA YAEKRSEDER WSSIFQ