ID   CORO_SCHPO              Reviewed;         601 AA.
AC   O13923;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 146.
DE   RecName: Full=Coronin-like protein crn1;
GN   Name=crn1; ORFNames=SPAC23C4.02;
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-500; SER-501 AND SER-553, 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).
CC   -!- SUBUNIT: Binds to F-actin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16873.1; -; Genomic_DNA.
DR   PIR; T38258; T38258.
DR   RefSeq; NP_593175.1; NM_001018571.2.
DR   AlphaFoldDB; O13923; -.
DR   SMR; O13923; -.
DR   BioGRID; 278448; 19.
DR   STRING; 4896.SPAC23C4.02.1; -.
DR   iPTMnet; O13923; -.
DR   MaxQB; O13923; -.
DR   PaxDb; O13923; -.
DR   PRIDE; O13923; -.
DR   EnsemblFungi; SPAC23C4.02.1; SPAC23C4.02.1:pep; SPAC23C4.02.
DR   GeneID; 2541961; -.
DR   KEGG; spo:SPAC23C4.02; -.
DR   PomBase; SPAC23C4.02; crn1.
DR   VEuPathDB; FungiDB:SPAC23C4.02; -.
DR   eggNOG; KOG0303; Eukaryota.
DR   HOGENOM; CLU_026859_3_1_1; -.
DR   InParanoid; O13923; -.
DR   OMA; NFQDDIY; -.
DR   PhylomeDB; O13923; -.
DR   PRO; PR:O13923; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR   GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR   GO; GO:0051286; C:cell tip; IDA:PomBase.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:PomBase.
DR   GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR   GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0051017; P:actin filament bundle assembly; NAS:PomBase.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0030041; P:actin filament polymerization; NAS:PomBase.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR10856; PTHR10856; 1.
DR   Pfam; PF08953; DUF1899; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM01166; DUF1899; 1.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Phosphoprotein; Reference proteome; Repeat;
KW   WD repeat.
FT   CHAIN           1..601
FT                   /note="Coronin-like protein crn1"
FT                   /id="PRO_0000050939"
FT   REPEAT          79..119
FT                   /note="WD 1"
FT   REPEAT          132..172
FT                   /note="WD 2"
FT   REPEAT          174..213
FT                   /note="WD 3"
FT   REPEAT          220..260
FT                   /note="WD 4"
FT   REPEAT          266..306
FT                   /note="WD 5"
FT   REGION          361..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          556..600
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        436..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         500
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         553
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   601 AA;  67015 MW;  231096AE76CADE4D CRC64;
     MSGRFVRASK YRHIFGQTCK KELCYDNIKL SNNAWDSNLL SVNPFYLSVN WNAGAGGALA
     VIPLNERGKL PDQVNLFRGH TAAVLDTDWN PFHDQVLASG GDDSKIMIWK VPEDYTVMEP
     YEDVHPIAEL KGHSRKVGLV QYHPTAANVL ASSSADNTIK LWDCEKGVAH VSLKMDVMCQ
     SMSFNADGTR LVTTSRDKKV RVWDPRTDKP VSVGNGHAGA KNPRVVWLGS LDRFATTGFS
     KMSDRQIALW DPTNLSEPIG GFTTLDTGSG ILMPFWDDGT KVIYLAGKGD GNIRYYEYEN
     DVFHYLSEFK SVDPQRGIAF LPKRGVNVSE NEVMRAYKSV NDSIIEPISF IVPRRSESFQ
     SDIYPPAPSG KPSLTAEEWA SGKDAQPDLL DMSTLYESKG TVEKAVSATV PSAGAQVQKH
     NEEKVETPKP EAQPVSKPKE SAEEQKPSKE PEVKPTTPSA SKVEEPSKKR DEDNHQKEET
     VTQPKREKTP VEKSFPKPAS SPVTFSEDVK KEPSEEKKLE VSDEAPKAAP LAESKKVEEK
     EPFYVSKDKK DISAVNLADL NKRFEGFEKR YEEELAIRDW KIAQLEDKLA KLTEAIKEKC
     N