COR1C_DANRE
ID COR1C_DANRE Reviewed; 474 AA.
AC B0R0D7; Q7ZW06;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Coronin-1C-A {ECO:0000305};
GN Name=coro1ca {ECO:0000312|ZFIN:ZDB-GENE-030114-6};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Ensembl:ENSDARP00000026454, ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB {ECO:0000312|EMBL:AAH45340.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH45340.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25074804; DOI=10.1242/jcs.154864;
RA Williamson R.C., Cowell C.A., Hammond C.L., Bergen D.J., Roper J.A.,
RA Feng Y., Rendall T.C., Race P.R., Bass M.D.;
RT "Coronin-1C and RCC2 guide mesenchymal migration by trafficking Rac1 and
RT controlling GEF exposure.";
RL J. Cell Sci. 127:4292-4307(2014).
CC -!- FUNCTION: Plays a role in directed cell migration by regulating the
CC activation and subcellular location of RAC1 (Probable). Increases the
CC presence of activated RAC1 at the leading edge of migrating cells.
CC Required for normal organization of the cytoskeleton, including the
CC actin cytoskeleton, microtubules and the vimentin intermediate
CC filaments. Plays a role in endoplasmic reticulum-associated endosome
CC fission: endosome membrane fission of early and late endosomes is
CC essential to separate regions destined for lysosomal degradation from
CC carriers to be recycled to the plasma membrane. Required for normal
CC cell proliferation, cell migration, and normal formation of
CC lamellipodia. Required for normal distribution of mitochondria within
CC cells (By similarity). {ECO:0000250|UniProtKB:Q9ULV4,
CC ECO:0000250|UniProtKB:Q9WUM4, ECO:0000305|PubMed:25074804}.
CC -!- SUBUNIT: Homotrimer (By similarity). Binds F-actin. Interacts with
CC RCC2. Interacts preferentially with nucleotide-free and GDP-bound RAC1.
CC Interacts with VIM (via head domain) (By similarity).
CC {ECO:0000250|UniProtKB:Q9ULV4, ECO:0000250|UniProtKB:Q9WUM4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9WUM4};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9WUM4}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q9WUM4}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q9WUM4}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q9WUM4}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9WUM4}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q9WUM4}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9ULV4}. Note=Colocalizes with the actin
CC cytoskeleton in the cytosol, and especially in the cell cortex (By
CC similarity). Colocalizes with F-actin at the leading edge of
CC lamellipodia (By similarity). Partially colocalizes with microtubules
CC and vimentin intermediate filaments (By similarity). Localizes to
CC endosome membrane tubules/buds (By similarity).
CC {ECO:0000250|UniProtKB:Q9ULV4, ECO:0000250|UniProtKB:Q9WUM4}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes subtle
CC defects in mesenchymal cell migration, but no gross anatomical defects.
CC The migration of neural crest cells towards the pharyngeal arches is
CC altered, resulting in no clear separation between the first and second
CC pharyngeal arch cells. {ECO:0000269|PubMed:25074804}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC {ECO:0000255|RuleBase:RU280818}.
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DR EMBL; AL845302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC045340; AAH45340.1; -; mRNA.
DR EMBL; BC165745; AAI65745.1; -; mRNA.
DR RefSeq; NP_958452.1; NM_201295.1.
DR AlphaFoldDB; B0R0D7; -.
DR SMR; B0R0D7; -.
DR STRING; 7955.ENSDARP00000026454; -.
DR PaxDb; B0R0D7; -.
DR PeptideAtlas; B0R0D7; -.
DR Ensembl; ENSDART00000004217; ENSDARP00000026454; ENSDARG00000035598.
DR Ensembl; ENSDART00000193141; ENSDARP00000153466; ENSDARG00000035598.
DR GeneID; 317741; -.
DR KEGG; dre:317741; -.
DR CTD; 317741; -.
DR ZFIN; ZDB-GENE-030114-6; coro1ca.
DR eggNOG; KOG0303; Eukaryota.
DR GeneTree; ENSGT00940000156488; -.
DR HOGENOM; CLU_026859_0_1_1; -.
DR InParanoid; B0R0D7; -.
DR OMA; NFQDDIY; -.
DR OrthoDB; 552726at2759; -.
DR PhylomeDB; B0R0D7; -.
DR TreeFam; TF314280; -.
DR PRO; PR:B0R0D7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000035598; Expressed in swim bladder and 46 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0140285; P:endosome fission; ISS:UniProtKB.
DR GO; GO:0097750; P:endosome membrane tubulation; ISS:UniProtKB.
DR GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR027333; CORO1C.
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:SF10; PTHR10856:SF10; 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 2: Evidence at transcript level;
KW Actin-binding; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endosome; Membrane; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..474
FT /note="Coronin-1C-A"
FT /id="PRO_0000445539"
FT REPEAT 79..119
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 129..169
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 173..212
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 216..259
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 264..304
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REGION 415..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..468
FT /evidence="ECO:0000255"
FT CONFLICT 181
FT /note="I -> V (in Ref. 2; AAH45340/AAI65745)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 53368 MW; 9F7406B3D43828D2 CRC64;
MFKRVVRQSK FRHVFGQAVK NDQCYDDIRV SRVTWDSAFC AVNPKFVALI VEASGGGAFM
VLPLHKTGRI DKAYPTVCGH TGPVLDIDWC PHNDQVIASG SEDCTVMVWQ IPENGLVTSM
SEPVVVLEGH SKRVGVVTWH PTARNVLLSA GCDNMIIIWN VGTGESMITL EDHHPDIIYS
ICWNRNGSLI CTACKDKKIR VIDPRKEEII AEKDKAHEGA RPMRAIFLSD GKVFTTGFSR
MSERQLALWD PENIDEPVAV HEMDTSNGVL LPFYDPDTNV VYLCGKGDSS IRYFEITDEA
PFVHYLNTFT TKEPQRGMGY MPKRGLDVNK CEIARFYKLH ERKCEPIIMT VPRKSDLFQD
DLYPDTAGPD APLEAEEWFE GKNGDPVLIS LKHGYIPGKN RDLKVVKKNI LDNKMSKNTE
NTTPAHKTAT STPSIKSEAK LEEVLKEIKS LRELVSSQEK RIGKLEEQLS KMDI
