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 27-MAR-2024, entry version 121.
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; 284812.O14259; -.
DR iPTMnet; O14259; -.
DR MaxQB; O14259; -.
DR PaxDb; 4896-SPAC7D4-02c-1; -.
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; QKDGWWK; -.
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 CDD; cd00174; SH3; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167:SF114; CAP, ISOFORM AC; 1.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 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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