COR1B_RAT
ID COR1B_RAT Reviewed; 484 AA.
AC O89046;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Coronin-1B;
DE AltName: Full=Coronin-2;
GN Name=Coro1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Male D.K., Politopoulou G.;
RT "A cell surface form of rat coronin.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH ACTR2; ARPC1B AND ARPC2.
RX PubMed=16027158; DOI=10.1074/jbc.m504146200;
RA Cai L., Holoweckyj N., Schaller M.D., Bear J.E.;
RT "Phosphorylation of coronin 1B by protein kinase C regulates interaction
RT with Arp2/3 and cell motility.";
RL J. Biol. Chem. 280:31913-31923(2005).
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. Binds actin (By similarity). {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: Phosphorylation on Ser-2 regulates the interaction with the Arp2/3
CC complex and cell motility in fibroblasts. Phosphorylation does not seem
CC to affect subcellular location (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
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DR EMBL; AJ006064; CAA06836.1; -; mRNA.
DR RefSeq; NP_062095.1; NM_019222.1.
DR AlphaFoldDB; O89046; -.
DR SMR; O89046; -.
DR BioGRID; 248116; 1.
DR IntAct; O89046; 3.
DR MINT; O89046; -.
DR STRING; 10116.ENSRNOP00000035020; -.
DR iPTMnet; O89046; -.
DR PhosphoSitePlus; O89046; -.
DR SwissPalm; O89046; -.
DR jPOST; O89046; -.
DR PaxDb; O89046; -.
DR PRIDE; O89046; -.
DR GeneID; 29474; -.
DR KEGG; rno:29474; -.
DR UCSC; RGD:2382; rat.
DR CTD; 57175; -.
DR RGD; 2382; Coro1b.
DR eggNOG; KOG0303; Eukaryota.
DR InParanoid; O89046; -.
DR PhylomeDB; O89046; -.
DR PRO; PR:O89046; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005884; C:actin filament; ISO:RGD.
DR GO; GO:0031252; C:cell leading edge; IDA:RGD.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0071933; F:Arp2/3 complex binding; IPI:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0090135; P:actin filament branching; ISO:RGD.
DR GO; GO:0051017; P:actin filament bundle assembly; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:RGD.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISO:RGD.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; ISO:RGD.
DR GO; GO:2000393; P:negative regulation of lamellipodium morphogenesis; IMP:UniProtKB.
DR GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; IMP:UniProtKB.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; ISO:RGD.
DR GO; GO:0070528; P:protein kinase C signaling; IDA:RGD.
DR GO; GO:1902463; P:protein localization to cell leading edge; ISO:RGD.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IC:UniProtKB.
DR GO; GO:0031529; P:ruffle organization; ISO:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
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..484
FT /note="Coronin-1B"
FT /id="PRO_0000050925"
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 COILED 447..481
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BR76"
SQ SEQUENCE 484 AA; 53845 MW; 746EDF119680EBBF CRC64;
MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV IVEASGGGAF
MVLPLNKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS GSEDCTVMVW QIPENGLTSP
LTEPVVVLEG HTKRVGIITW HPTARNVLLS AGCDNVVLIW NVGTAEELYR LDSLHPDLIY
NVSWNHNGSL FCTACKDKSV RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTAGFS
RMSERQLALW DPENFEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITDE
PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM TVPRKSDLFQ
DDLYPDTAGP DAALEAEDWV SGQDADPILI SLREAYVPSK QRDLKVSRRN VLSDSKPAGY
SRSGVSTATA ITDIPSGNLA GSGEAGKLEE VMHGLRALRV LVKEQGERIS RLEEHLGRME
NGDT
