COR1B_MOUSE
ID COR1B_MOUSE Reviewed; 484 AA.
AC Q9WUM3; Q3UEB1; Q9CVA2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Coronin-1B;
DE AltName: Full=Coronin-2;
GN Name=Coro1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9778037; DOI=10.1089/dna.1998.17.779;
RA Okumura M., Kung C., Wong S., Rodgers M., Thomas M.L.;
RT "Definition of family of coronin-related proteins conserved between humans
RT and mice: close genetic linkage between coronin-2 and CD45-associated
RT protein.";
RL DNA Cell Biol. 17:779-787(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 34-46; 135-145 AND 423-456, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP TISSUE SPECIFICITY, AND 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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16027158}.
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; AF143956; AAD32704.1; -; mRNA.
DR EMBL; AK008947; BAB25985.1; -; mRNA.
DR EMBL; AK149639; BAE29000.1; -; mRNA.
DR CCDS; CCDS29418.1; -.
DR RefSeq; NP_035908.1; NM_011778.2.
DR RefSeq; XP_006531804.1; XM_006531741.2.
DR RefSeq; XP_006531805.1; XM_006531742.1.
DR AlphaFoldDB; Q9WUM3; -.
DR SMR; Q9WUM3; -.
DR BioGRID; 204713; 15.
DR IntAct; Q9WUM3; 2.
DR STRING; 10090.ENSMUSP00000008893; -.
DR iPTMnet; Q9WUM3; -.
DR PhosphoSitePlus; Q9WUM3; -.
DR SwissPalm; Q9WUM3; -.
DR EPD; Q9WUM3; -.
DR jPOST; Q9WUM3; -.
DR MaxQB; Q9WUM3; -.
DR PaxDb; Q9WUM3; -.
DR PRIDE; Q9WUM3; -.
DR ProteomicsDB; 283608; -.
DR Antibodypedia; 4316; 245 antibodies from 29 providers.
DR DNASU; 23789; -.
DR Ensembl; ENSMUST00000008893; ENSMUSP00000008893; ENSMUSG00000024835.
DR GeneID; 23789; -.
DR KEGG; mmu:23789; -.
DR UCSC; uc008fyy.1; mouse.
DR CTD; 57175; -.
DR MGI; MGI:1345963; Coro1b.
DR VEuPathDB; HostDB:ENSMUSG00000024835; -.
DR eggNOG; KOG0303; Eukaryota.
DR GeneTree; ENSGT00940000159031; -.
DR HOGENOM; CLU_026859_0_1_1; -.
DR InParanoid; Q9WUM3; -.
DR OMA; YVPTKQR; -.
DR OrthoDB; 552726at2759; -.
DR PhylomeDB; Q9WUM3; -.
DR TreeFam; TF314280; -.
DR BioGRID-ORCS; 23789; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Coro1b; mouse.
DR PRO; PR:Q9WUM3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9WUM3; protein.
DR Bgee; ENSMUSG00000024835; Expressed in ileum and 70 other tissues.
DR ExpressionAtlas; Q9WUM3; baseline and differential.
DR Genevisible; Q9WUM3; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0071933; F:Arp2/3 complex binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0090135; P:actin filament branching; ISO:MGI.
DR GO; GO:0051017; P:actin filament bundle assembly; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:MGI.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISO:MGI.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; ISO:MGI.
DR GO; GO:2000393; P:negative regulation of lamellipodium morphogenesis; ISO:MGI.
DR GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; ISO:MGI.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; ISO:MGI.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:MGI.
DR GO; GO:1902463; P:protein localization to cell leading edge; ISO:MGI.
DR GO; GO:0031529; P:ruffle organization; ISO:MGI.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
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;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..484
FT /note="Coronin-1B"
FT /id="PRO_0000050923"
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..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 444..482
FT /evidence="ECO:0000255"
FT COMPBIAS 412..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BR76"
FT CONFLICT 393
FT /note="R -> G (in Ref. 2; BAB25985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 53912 MW; 9631CC02E7EAC72F CRC64;
MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV IVEASGGGAF
MVLPLNKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS GSEDCTVMVW QIPENGLTSP
LTEPVVVLEG HTKRVGIITW HPTARNVLLS AGCDNVVLIW NVGTAEELYR LDSLHPDLIY
NVSWNHNGSL FCSACKDKSV RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS
RMSERQLALW DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITDE
PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM TVPRKSDLFQ
DDLYPDTAGP EAALEAEDWV SGQDANPILI SLREAYVPSK QRDLKVSRRN VLSDSRPASY
SRSGASTATA VTDVPSGNLA GAGEAGKLEE VMQELRALRM LVKEQGERIS RLEEQLGRME
NGDT
