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   02-OCT-2024, entry version 196.
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=7; 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}.
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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; 202.
DR   DIP; DIP-33176N; -.
DR   IntAct; Q9BR76; 64.
DR   MINT; Q9BR76; -.
DR   STRING; 9606.ENSP00000340211; -.
DR   GlyGen; Q9BR76; 2 sites, 1 O-linked glycan (2 sites).
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   jPOST; Q9BR76; -.
DR   MassIVE; Q9BR76; -.
DR   PaxDb; 9606-ENSP00000377471; -.
DR   PeptideAtlas; Q9BR76; -.
DR   ProteomicsDB; 78746; -.
DR   Pumba; Q9BR76; -.
DR   Antibodypedia; 4316; 273 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   AGR; HGNC:2253; -.
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; HPCAENV; -.
DR   OrthoDB; 5474889at2759; -.
DR   PhylomeDB; Q9BR76; -.
DR   TreeFam; TF314280; -.
DR   PathwayCommons; Q9BR76; -.
DR   SignaLink; Q9BR76; -.
DR   SIGNOR; Q9BR76; -.
DR   BioGRID-ORCS; 57175; 21 hits in 1158 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 158 other cell types or tissues.
DR   ExpressionAtlas; Q9BR76; baseline and differential.
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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR10856; CORONIN; 1.
DR   PANTHER; PTHR10856:SF24; CORONIN-1B; 1.
DR   Pfam; PF08953; DUF1899; 1.
DR   Pfam; PF00400; WD40; 3.
DR   Pfam; PF16300; WD40_4; 1.
DR   SMART; SM01166; DUF1899; 1.
DR   SMART; SM01167; DUF1900; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; WD40 repeat-like; 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   Proteomics identification; 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
//