ID   COR1B_RABIT             Reviewed;         486 AA.
AC   Q9XS70;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Coronin-1B;
DE   AltName: Full=Coronin-like protein pp66;
DE   AltName: Full=Coroninse;
GN   Name=CORO1B;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], BINDING TO ACTIN, AND PHOSPHORYLATION.
RC   STRAIN=New Zealand white; TISSUE=Gastric mucosa;
RX   PubMed=9915840; DOI=10.1074/jbc.274.5.3017;
RA   Parente J.A. Jr., Chen X., Zhou C., Petropoulos A.C., Chew C.S.;
RT   "Isolation, cloning, and characterization of a new mammalian coronin family
RT   member, coroninse, which is regulated within the protein kinase C signaling
RT   pathway.";
RL   J. Biol. Chem. 274:3017-3025(1999).
CC   -!- FUNCTION: Regulates leading edge dynamics and cell motility in
CC       fibroblasts. May be involved in cytokinesis and signal transduction (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms homooligomers, but does not form complexes with the
CC       other coronins. Interacts with Arp2/3 complex components, including
CC       ACTR2, ARPC1B and ARPC2 (By similarity). Binds actin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9BR76}. Cytoplasm, cytoskeleton, stress fiber
CC       {ECO:0000250|UniProtKB:Q9BR76}. Note=Localized to the leading edge in
CC       fibroblasts, as well as weakly along actin stress fibers.
CC       {ECO:0000250|UniProtKB:Q9BR76}.
CC   -!- PTM: Phosphorylated in vivo by PKC in response to cholinergic
CC       stimulation. Phosphorylation on Ser-2 regulates the interaction with
CC       the Arp2/3 complex and cell motility in fibroblasts. Phosphorylation
CC       does not seem to affect subcellular location (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BR76}.
CC   -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
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DR   EMBL; AF056312; AAD23736.1; -; mRNA.
DR   RefSeq; NP_001076156.1; NM_001082687.1.
DR   AlphaFoldDB; Q9XS70; -.
DR   SMR; Q9XS70; -.
DR   GeneID; 100009415; -.
DR   KEGG; ocu:100009415; -.
DR   CTD; 57175; -.
DR   InParanoid; Q9XS70; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR027340; Coro1b.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
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   PANTHER; PTHR10856:SF24; PTHR10856:SF24; 1.
DR   Pfam; PF08953; DUF1899; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM01166; DUF1899; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..486
FT                   /note="Coronin-1B"
FT                   /id="PRO_0000050924"
FT   REPEAT          80..120
FT                   /note="WD 1"
FT   REPEAT          130..170
FT                   /note="WD 2"
FT   REPEAT          174..213
FT                   /note="WD 3"
FT   REPEAT          217..260
FT                   /note="WD 4"
FT   REPEAT          265..305
FT                   /note="WD 5"
FT   REGION          404..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          446..484
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BR76"
SQ   SEQUENCE   486 AA;  53609 MW;  726E125D024987E8 CRC64;
     MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV IVEASGGGAF
     LVLPLSKTGR IDKAYPTVCG HTGPVLDIEW CPHNDGVIAS GSEDCTVMVW QIPEDGLTSP
     LTEPVVVLEG HTKRVGIVTW HPTARNVLLS AGCDNVVLIW NVGTAEELYR LDSLHPDLIY
     NVSWNRNGSL FCSACKDKSV RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS
     RMSERQLALW DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITDE
     PPYIHFLNTF TSKEPQRGVG SMPKRGLEVS KCEIARFYKL HERKCEPIVM TVPRKSDLFQ
     DDLYPDTAGP EAALEAEEWV SGRDAGPVLI SLREAYVPSK QRDLKVSRRN VLSDSRPTSA
     ARPAAPAPAA PAPAAAASSS LSGAGEAGKL EEVMRELRAL RALVKEQGER IGRLEEQLGR
     VENGDA