ID   CSH3_SCHPO              Reviewed;         296 AA.
AC   O43125;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Protein csh3;
GN   Name=csh3; ORFNames=SPBC119.05c;
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 [MRNA].
RA   Kawamukai M.;
RT   "S.pombe SH3 domain containing protein.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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).
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DR   EMBL; AB011825; BAA25107.1; -; mRNA.
DR   EMBL; CU329671; CAA17920.1; -; Genomic_DNA.
DR   PIR; T43336; T43336.
DR   RefSeq; NP_595286.1; NM_001021193.2.
DR   AlphaFoldDB; O43125; -.
DR   SMR; O43125; -.
DR   BioGRID; 276489; 6.
DR   IntAct; O43125; 1.
DR   STRING; 4896.SPBC119.05c.1; -.
DR   iPTMnet; O43125; -.
DR   MaxQB; O43125; -.
DR   PaxDb; O43125; -.
DR   PRIDE; O43125; -.
DR   EnsemblFungi; SPBC119.05c.1; SPBC119.05c.1:pep; SPBC119.05c.
DR   GeneID; 2539945; -.
DR   KEGG; spo:SPBC119.05c; -.
DR   PomBase; SPBC119.05c; -.
DR   VEuPathDB; FungiDB:SPBC119.05c; -.
DR   eggNOG; KOG3601; Eukaryota.
DR   HOGENOM; CLU_940602_0_0_1; -.
DR   InParanoid; O43125; -.
DR   OMA; WKGRNER; -.
DR   PhylomeDB; O43125; -.
DR   Reactome; R-SPO-437239; Recycling pathway of L1.
DR   Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-SPO-9013424; RHOV GTPase cycle.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:O43125; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISO:PomBase.
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; SSF50044; SSF50044; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome; SH3 domain.
FT   CHAIN           1..296
FT                   /note="Protein csh3"
FT                   /id="PRO_0000079396"
FT   DOMAIN          140..199
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          46..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..218
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   296 AA;  31737 MW;  2155ED0CCFD6F6F1 CRC64;
     MDHKNYLNHV IRGIYNDFQF LVDEGVVERS ALDWVHANIH LQDGPASPVT APAAQPVESS
     VPLPLPKRKS SVEKRAGSVA SAVAAMSLSQ NSGEKRTPEE PRKLPGVPAP QKQSEASSVN
     SSTEKLPPPP SYPGPNTAHK NVERVLAMYD FPGPDAGDLG FHAGEVIIVL EHVNNDWWRG
     ELNGKEGIFP SNYVRLLEDS AVKAQPPPPP PQQNYPPAAS SSAPPMQYQQ TAYPPQQAPY
     PPVQAYPQAP QQPIVVAQPT EHKHSSTFKK IGSGLGSAFV FGAGATAGAD LVNSIF