ID   YIE2_SCHPO              Reviewed;         430 AA.
AC   Q9URW6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=SH3 domain-containing protein PJ696.02;
GN   ORFNames=SPAPJ696.02;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285; THR-316; SER-318;
RP   SER-324; TYR-325; SER-326; SER-354 AND SER-406, AND IDENTIFICATION BY MASS
RP   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   -!- SIMILARITY: Belongs to the SH3YL1 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB62422.1; -; Genomic_DNA.
DR   PIR; T50296; T50296.
DR   RefSeq; NP_593048.1; NM_001018447.2.
DR   AlphaFoldDB; Q9URW6; -.
DR   SMR; Q9URW6; -.
DR   BioGRID; 279729; 4.
DR   STRING; 284812.Q9URW6; -.
DR   iPTMnet; Q9URW6; -.
DR   MaxQB; Q9URW6; -.
DR   PaxDb; 4896-SPAPJ696-02-1; -.
DR   EnsemblFungi; SPAPJ696.02.1; SPAPJ696.02.1:pep; SPAPJ696.02.
DR   GeneID; 2543305; -.
DR   KEGG; spo:SPAPJ696.02; -.
DR   PomBase; SPAPJ696.02; -.
DR   VEuPathDB; FungiDB:SPAPJ696.02; -.
DR   eggNOG; KOG1843; Eukaryota.
DR   HOGENOM; CLU_015320_2_0_1; -.
DR   InParanoid; Q9URW6; -.
DR   OMA; QRTIQHE; -.
DR   PhylomeDB; Q9URW6; -.
DR   PRO; PR:Q9URW6; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR   GO; GO:0051666; P:actin cortical patch localization; IBA:GO_Central.
DR   GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; ISO:PomBase.
DR   CDD; cd11842; SH3_Ysc84p_like; 1.
DR   CDD; cd11525; SYLF_SH3YL1_like; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR033643; SYLF_SH3YL1-like.
DR   InterPro; IPR007461; Ysc84_actin-binding.
DR   PANTHER; PTHR15629:SF2; SH3 DOMAIN-CONTAINING YSC84-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR15629; SH3YL1 PROTEIN; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF04366; Ysc84; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN           1..430
FT                   /note="SH3 domain-containing protein PJ696.02"
FT                   /id="PRO_0000303942"
FT   DOMAIN          371..430
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          237..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         316
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         325
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   430 AA;  46374 MW;  AC300C08C29D946F CRC64;
     MGLHNPLPSS LKSECKKAGK ILTSFVDPRQ TLGAQEVIPP SVLTNAKGLV IMTVLKAGFL
     FSGRIGSGLI VARLDDGTWS APSAVMTGGM GVGAQIGSEL TDFVIILNSK AAVQTFARLG
     SITLGGNLSI AAGPLGRNAE AGGGASVGGM APMFSYSKTK GLFAGVSLEG SVLVERRDAN
     RSLYRGDITA KRLLSGQVAQ PAAADPLYRV LNSKIFNLNR GDEGDIYNDV PIYADDEPED
     IWGPSSKSTK RRDSADRSSS YSRRGDSYRS NRSRAHDDDD EDDYSFSRSK SLSRKTAGGS
     LRSSKMDNRR SKYADTPSPR RSRSYSDEDE ESVYSSDVST ESSSQFSSRS SEYSKPSRPT
     APKPKFKQDS LGPNQARAMY SFAGEQPGDL SFQKGDIIDI VERSGSHDDW WTGRIGYREG
     IFPANYVKLS
//