CORO_YEAST
ID CORO_YEAST Reviewed; 651 AA.
AC Q06440; D6VZ64;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Coronin-like protein;
GN Name=CRN1; OrderedLocusNames=YLR429W; ORFNames=L9576.2;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-517, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; SER-454 AND THR-529, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454 AND SER-456, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454; SER-456; THR-517;
RP SER-573 AND SER-579, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- SUBUNIT: Binds to F-actin. {ECO:0000250}.
CC -!- INTERACTION:
CC Q06440; P60010: ACT1; NbExp=3; IntAct=EBI-4950, EBI-2169;
CC Q06440; P68135: ACTA1; Xeno; NbExp=3; IntAct=EBI-4950, EBI-367540;
CC -!- MISCELLANEOUS: Present with 2900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
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DR EMBL; U20939; AAB67503.1; -; Genomic_DNA.
DR EMBL; AY693023; AAT93042.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09730.1; -; Genomic_DNA.
DR PIR; S53415; S53415.
DR RefSeq; NP_013533.1; NM_001182317.1.
DR AlphaFoldDB; Q06440; -.
DR SMR; Q06440; -.
DR BioGRID; 31688; 187.
DR DIP; DIP-2722N; -.
DR IntAct; Q06440; 23.
DR MINT; Q06440; -.
DR STRING; 4932.YLR429W; -.
DR iPTMnet; Q06440; -.
DR MaxQB; Q06440; -.
DR PaxDb; Q06440; -.
DR PRIDE; Q06440; -.
DR EnsemblFungi; YLR429W_mRNA; YLR429W; YLR429W.
DR GeneID; 851148; -.
DR KEGG; sce:YLR429W; -.
DR SGD; S000004421; CRN1.
DR VEuPathDB; FungiDB:YLR429W; -.
DR eggNOG; KOG0303; Eukaryota.
DR HOGENOM; CLU_026859_3_2_1; -.
DR InParanoid; Q06440; -.
DR OMA; NFQDDIY; -.
DR BioCyc; YEAST:G3O-32488-MON; -.
DR PRO; PR:Q06440; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06440; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:SGD.
DR GO; GO:0008017; F:microtubule binding; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:SGD.
DR GO; GO:0007015; P:actin filament organization; IMP:SGD.
DR GO; GO:0007017; P:microtubule-based process; IPI:SGD.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
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; IPR019775; WD40_repeat_CS.
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; 3.
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..651
FT /note="Coronin-like protein"
FT /id="PRO_0000050940"
FT REPEAT 79..110
FT /note="WD 1"
FT REPEAT 138..169
FT /note="WD 2"
FT REPEAT 180..210
FT /note="WD 3"
FT REPEAT 226..257
FT /note="WD 4"
FT REGION 408..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 618..650
FT /evidence="ECO:0000255"
FT COMPBIAS 425..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 517
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 651 AA; 72553 MW; E4A3AC8CF5112001 CRC64;
MSGKFVRASK YRHVFGQAAK KELQYEKLKV TNNAWDSNLL KTNGKFIAVN WNASGGGAFA
VIPIEEVGKA PDQVPLFRGH TAQVLDTDFD PFNDHRIASG SDDSKIGIWD IPENYKFHDH
VDEDGEPIDI KPVKFLTGHA RKVGHVLYHP VAENVLASSS GDYTVKLWNV ETGKDMITLK
HPDMVTSMSF SYDGNYLATV ARDKKLRVWN IREEKIVSEG PAHTGAKNQR VVWLGNSDRL
ATTGFSKLSD RQIGIWDAFN IEKGDLGGFY TVDQSSGILM PFYDEGNKIL YLVGKGDGNI
RYYEFQNDEL FELSEFQSTE AQRGFAVAPK RMVNVKENEV LKGFKTVVDQ RIEPVSFFVP
RRSEEFQEDI YPDAPSNKPA LTAEEWFSGK SVEGPILVSM RSIYDGSAPS FHEAKRPQQP
TTQETALEEK KEQPKVEKPI SESEKEVKQE APKSPSPLKS ASSSSTINHV LKEDNSINKL
LKKSSDIDQV NNAEDPSRDT SGWEEADDEP APIKIETPVT PTETKKDRTP KVEPSKELKP
EPVSIATDRK QEQSLPQEEK SSEKTKSPEQ EKSATPPSSI TAAKTAITAS SKEEPSAART
SPKSLGLKKS VEKLSTLVLQ LEDVVDKLTK ANLDKDERLL KLEQKIGELS K
