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SFP47_SCHPO
ID   SFP47_SCHPO             Reviewed;         415 AA.
AC   O14259;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Ubp4-interactor sfp47;
GN   Name=sfp47; ORFNames=SPAC7D4.02c;
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-221; SER-226; THR-231 AND
RP   SER-235, AND 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   [4]
RP   INTERACTION WITH UBP4, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP   LOCATION, AND FUNCTION.
RX   PubMed=20838651; DOI=10.1371/journal.pbio.1000471;
RA   Kouranti I., McLean J.R., Feoktistova A., Liang P., Johnson A.E.,
RA   Roberts-Galbraith R.H., Gould K.L.;
RT   "A global census of fission yeast deubiquitinating enzyme localization and
RT   interaction networks reveals distinct compartmentalization profiles and
RT   overlapping functions in endocytosis and polarity.";
RL   PLoS Biol. 8:708-716(2010).
CC   -!- FUNCTION: Required for the regulation of activity and recruitment of
CC       ubp4 to endosomes. {ECO:0000269|PubMed:20838651}.
CC   -!- SUBUNIT: Interacts with ubp4. {ECO:0000269|PubMed:20838651}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372,
CC       ECO:0000269|PubMed:20838651}. Endosome {ECO:0000269|PubMed:20838651}.
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DR   EMBL; CU329670; CAB16719.2; -; Genomic_DNA.
DR   PIR; T39080; T39080.
DR   RefSeq; NP_593857.1; NM_001019286.2.
DR   AlphaFoldDB; O14259; -.
DR   BioGRID; 278568; 8.
DR   STRING; 4896.SPAC7D4.02c.1; -.
DR   iPTMnet; O14259; -.
DR   MaxQB; O14259; -.
DR   PaxDb; O14259; -.
DR   PRIDE; O14259; -.
DR   EnsemblFungi; SPAC7D4.02c.1; SPAC7D4.02c.1:pep; SPAC7D4.02c.
DR   GeneID; 2542091; -.
DR   KEGG; spo:SPAC7D4.02c; -.
DR   PomBase; SPAC7D4.02c; sfp47.
DR   VEuPathDB; FungiDB:SPAC7D4.02c; -.
DR   HOGENOM; CLU_662505_0_0_1; -.
DR   InParanoid; O14259; -.
DR   OMA; NRQKDGW; -.
DR   PRO; PR:O14259; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005768; C:endosome; IPI:PomBase.
DR   GO; GO:0030414; F:peptidase inhibitor activity; EXP:PomBase.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IPI:PomBase.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endosome; Phosphoprotein; Reference proteome; SH3 domain;
KW   Ubl conjugation pathway.
FT   CHAIN           1..415
FT                   /note="Ubp4-interactor sfp47"
FT                   /id="PRO_0000303943"
FT   DOMAIN          352..415
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         231
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   415 AA;  46782 MW;  F526360B7B9B7946 CRC64;
     MNSFSSNEYS TEISTEALNN WQQLVEQRIS LELEYAAKLA KLTKSIKAIK QCAPLNDLTK
     QVCVELMQCN KKHLEASRYF QTHVKEFMKE YVDRENKFSN ETISKSSAAA LMTSMENFIL
     FTNPVYHNKL QVPSKSDMEI ANSLKITQPA EKNSGTANPI SAYSLEHAEL DERNNQLSEA
     LSMLRLSPFV NNYYPSYQNR KDGKSLMENR GVVLSVDTVT SPISQSPKKL TPTTSPINST
     SLSFVDAKKP GSKWPSQYDF PKKTKSTEIP FKTLPSLNIN NERELTKHKL PIVKPKLAVF
     PSNQATASTL QLAPPPVQAI PTLRNPVNLD DKKESLLKYY ATHPTITPDG FPIFAYVRAL
     YAYKATLPSE IDLNVDDTLV VLNRQKDGWW KGLVVSPTVG RIGLFPSNYI EELEY
 
 
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