COR1B_HUMAN
ID COR1B_HUMAN Reviewed; 489 AA.
AC Q9BR76; B2RD45;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Coronin-1B;
DE AltName: Full=Coronin-2;
GN Name=CORO1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH ACTR2; ARPC1B AND ARPC2,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2, AND MUTAGENESIS OF SER-2.
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=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] MET-411.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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, ECO:0000269|PubMed:16027158}.
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 -!- INTERACTION:
CC Q9BR76; O15144: ARPC2; NbExp=2; IntAct=EBI-351152, EBI-352356;
CC Q9BR76; Q9ULV4: CORO1C; NbExp=3; IntAct=EBI-351152, EBI-351384;
CC Q9BR76; Q969G2: LHX4; NbExp=3; IntAct=EBI-351152, EBI-2865388;
CC Q9BR76; Q8WYL5: SSH1; NbExp=3; IntAct=EBI-351152, EBI-1222387;
CC Q9BR76; P54274: TERF1; NbExp=2; IntAct=EBI-351152, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16027158}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:16027158}. Note=Localized to the leading edge in
CC fibroblasts, as well as weakly along actin stress fibers.
CC {ECO:0000269|PubMed:16027158}.
CC -!- PTM: Phosphorylation by PKC on Ser-2 regulates the interaction with the
CC Arp2/3 complex and cell motility in fibroblasts. Phosphorylation does
CC not seem to affect subcellular location. {ECO:0000269|PubMed:16027158}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK315399; BAG37792.1; -; mRNA.
DR EMBL; CH471076; EAW74623.1; -; Genomic_DNA.
DR EMBL; BC006449; AAH06449.1; -; mRNA.
DR CCDS; CCDS8164.1; -.
DR RefSeq; NP_001018080.1; NM_001018070.2.
DR RefSeq; NP_065174.1; NM_020441.2.
DR AlphaFoldDB; Q9BR76; -.
DR SMR; Q9BR76; -.
DR BioGRID; 121425; 158.
DR DIP; DIP-33176N; -.
DR IntAct; Q9BR76; 57.
DR MINT; Q9BR76; -.
DR STRING; 9606.ENSP00000377471; -.
DR GlyGen; Q9BR76; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BR76; -.
DR MetOSite; Q9BR76; -.
DR PhosphoSitePlus; Q9BR76; -.
DR SwissPalm; Q9BR76; -.
DR BioMuta; CORO1B; -.
DR DMDM; 21263481; -.
DR CPTAC; CPTAC-339; -.
DR CPTAC; CPTAC-340; -.
DR EPD; Q9BR76; -.
DR jPOST; Q9BR76; -.
DR MassIVE; Q9BR76; -.
DR MaxQB; Q9BR76; -.
DR PaxDb; Q9BR76; -.
DR PeptideAtlas; Q9BR76; -.
DR PRIDE; Q9BR76; -.
DR ProteomicsDB; 78746; -.
DR Antibodypedia; 4316; 245 antibodies from 29 providers.
DR DNASU; 57175; -.
DR Ensembl; ENST00000341356.10; ENSP00000340211.5; ENSG00000172725.14.
DR Ensembl; ENST00000393893.5; ENSP00000377471.1; ENSG00000172725.14.
DR GeneID; 57175; -.
DR KEGG; hsa:57175; -.
DR MANE-Select; ENST00000341356.10; ENSP00000340211.5; NM_020441.3; NP_065174.1.
DR UCSC; uc001olk.2; human.
DR CTD; 57175; -.
DR DisGeNET; 57175; -.
DR GeneCards; CORO1B; -.
DR HGNC; HGNC:2253; CORO1B.
DR HPA; ENSG00000172725; Low tissue specificity.
DR MIM; 609849; gene.
DR neXtProt; NX_Q9BR76; -.
DR OpenTargets; ENSG00000172725; -.
DR PharmGKB; PA26769; -.
DR VEuPathDB; HostDB:ENSG00000172725; -.
DR eggNOG; KOG0303; Eukaryota.
DR GeneTree; ENSGT00940000159031; -.
DR HOGENOM; CLU_026859_0_1_1; -.
DR InParanoid; Q9BR76; -.
DR OMA; YVPTKQR; -.
DR OrthoDB; 552726at2759; -.
DR PhylomeDB; Q9BR76; -.
DR TreeFam; TF314280; -.
DR PathwayCommons; Q9BR76; -.
DR SignaLink; Q9BR76; -.
DR SIGNOR; Q9BR76; -.
DR BioGRID-ORCS; 57175; 20 hits in 1080 CRISPR screens.
DR GenomeRNAi; 57175; -.
DR Pharos; Q9BR76; Tbio.
DR PRO; PR:Q9BR76; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BR76; protein.
DR Bgee; ENSG00000172725; Expressed in mucosa of transverse colon and 156 other tissues.
DR ExpressionAtlas; Q9BR76; baseline and differential.
DR Genevisible; Q9BR76; HS.
DR GO; GO:0005884; C:actin filament; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA: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; IDA:CACAO.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:CACAO.
DR GO; GO:0090135; P:actin filament branching; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IMP:UniProtKB.
DR GO; GO:0035767; P:endothelial cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA: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; IDA:UniProtKB.
DR GO; GO:1902463; P:protein localization to cell leading edge; IDA:UniProtKB.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IC:UniProtKB.
DR GO; GO:0031529; P:ruffle organization; IDA:UniProtKB.
DR GO; GO:0042060; P:wound healing; IDA:UniProtKB.
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..489
FT /note="Coronin-1B"
FT /id="PRO_0000050922"
FT REPEAT 18..72
FT /note="WD 1"
FT REPEAT 73..122
FT /note="WD 2"
FT REPEAT 123..166
FT /note="WD 3"
FT REPEAT 167..210
FT /note="WD 4"
FT REPEAT 211..256
FT /note="WD 5"
FT REPEAT 257..296
FT /note="WD 6"
FT REGION 408..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 449..474
FT /evidence="ECO:0000255"
FT COMPBIAS 426..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:16027158"
FT VARIANT 411
FT /note="V -> M (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs756117196)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035877"
FT VARIANT 476
FT /note="R -> L (in dbSNP:rs2286624)"
FT /id="VAR_053389"
FT MUTAGEN 2
FT /note="S->A: Stronger interaction with the Arp2/3 complex.
FT Does not affect homo-oligomerization. Enhanced ruffling in
FT response to phorbol 12-myristate 13-acetate (PMA) and
FT increased speed in fibroblasts."
FT /evidence="ECO:0000269|PubMed:16027158"
FT MUTAGEN 2
FT /note="S->D: Weaker interaction with the Arp2/3 complex.
FT Does not affect homo-oligomerization. Attenuated PMA-
FT induced ruffling and slower speed in fibroblasts."
FT /evidence="ECO:0000269|PubMed:16027158"
SQ SEQUENCE 489 AA; 54235 MW; A6012FDA683ECB59 CRC64;
MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV IVEASGGGAF
LVLPLSKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS GSEDCTVMVW QIPENGLTSP
LTEPVVVLEG HTKRVGIIAW HPTARNVLLS AGCDNVVLIW NVGTAEELYR LDSLHPDLIY
NVSWNHNGSL FCSACKDKSV RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS
RMSERQLALW DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITEE
PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM TVPRKSDLFQ
DDLYPDTAGP EAALEAEEWV SGRDADPILI SLREAYVPSK QRDLKISRRN VLSDSRPAMA
PGSSHLGAPA STTTAADATP SGSLARAGEA GKLEEVMQEL RALRALVKEQ GDRICRLEEQ
LGRMENGDA
