COR1A_BOVIN
ID COR1A_BOVIN Reviewed; 461 AA.
AC Q92176; Q3SZF9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Coronin-1A;
DE AltName: Full=Coronin-like protein A;
DE Short=Clipin-A;
DE AltName: Full=Coronin-like protein p57;
DE AltName: Full=Tryptophan aspartate-containing coat protein;
DE Short=TACO;
GN Name=CORO1A; Synonyms=CORO1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Spleen;
RX PubMed=7758584; DOI=10.1016/0014-5793(95)00393-n;
RA Suzuki K., Nishihata J., Arai Y., Honma N., Yamamoto K., Irimura T.,
RA Toyoshima S.;
RT "Molecular cloning of a novel actin-binding protein, p57, with a WD repeat
RT and a leucine zipper motif.";
RL FEBS Lett. 364:283-288(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be a crucial component of the cytoskeleton of highly
CC motile cells, functioning both in the invagination of large pieces of
CC plasma membrane, as well as in forming protrusions of the plasma
CC membrane involved in cell locomotion. In mycobacteria-infected
CC macrophages, its retention on the phagosomal membrane prevents fusion
CC between phagosomes and lysosomes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cell cortex {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250}. Note=In non-infected macrophages, associated with the
CC cortical microtubule network. In mycobacteria-infected macrophages,
CC becomes progressively relocalized and retained around the mycobacterial
CC phagosomes. Retention on the phagosomal membrane is strictly dependent
CC on mycobacterial viability and not due to impaired acidification (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, thymus, spleen, bone marrow and
CC lymph node. Low in lung and gut.
CC -!- PTM: phosphorylation at Thr-412 by PKC strongly down-regulates the
CC association with actin. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated by RNF128 with 'Lys-48'-linked chains, leading
CC to proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
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DR EMBL; D44496; BAA07939.1; -; mRNA.
DR EMBL; BT025463; ABF57419.1; -; mRNA.
DR EMBL; BC102876; AAI02877.1; -; mRNA.
DR PIR; S65666; S65666.
DR RefSeq; NP_776946.1; NM_174521.2.
DR RefSeq; XP_005224888.1; XM_005224831.3.
DR RefSeq; XP_005224890.1; XM_005224833.3.
DR AlphaFoldDB; Q92176; -.
DR SMR; Q92176; -.
DR STRING; 9913.ENSBTAP00000051462; -.
DR PaxDb; Q92176; -.
DR PeptideAtlas; Q92176; -.
DR PRIDE; Q92176; -.
DR Ensembl; ENSBTAT00000011382; ENSBTAP00000011382; ENSBTAG00000008631.
DR Ensembl; ENSBTAT00000051969; ENSBTAP00000051462; ENSBTAG00000008631.
DR GeneID; 282196; -.
DR KEGG; bta:282196; -.
DR CTD; 11151; -.
DR VEuPathDB; HostDB:ENSBTAG00000008631; -.
DR VGNC; VGNC:27620; CORO1A.
DR eggNOG; KOG0303; Eukaryota.
DR GeneTree; ENSGT00940000160628; -.
DR HOGENOM; CLU_026859_0_1_1; -.
DR InParanoid; Q92176; -.
DR OMA; MVMVWEI; -.
DR OrthoDB; 552726at2759; -.
DR TreeFam; TF314280; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000008631; Expressed in blood and 103 other tissues.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0001891; C:phagocytic cup; IEA:Ensembl.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; IEA:Ensembl.
DR GO; GO:0032036; F:myosin heavy chain binding; IEA:Ensembl.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0061502; P:early endosome to recycling endosome transport; IEA:Ensembl.
DR GO; GO:0010631; P:epithelial cell migration; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0030595; P:leukocyte chemotaxis; IEA:Ensembl.
DR GO; GO:0043320; P:natural killer cell degranulation; IEA:Ensembl.
DR GO; GO:0051126; P:negative regulation of actin nucleation; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0031339; P:negative regulation of vesicle fusion; IEA:Ensembl.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0001845; P:phagolysosome assembly; IEA:Ensembl.
DR GO; GO:0050918; P:positive chemotaxis; IEA:Ensembl.
DR GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR GO; GO:0072679; P:thymocyte migration; IEA:Ensembl.
DR GO; GO:0032796; P:uropod organization; IEA:Ensembl.
DR GO; GO:0006906; P:vesicle fusion; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR029508; CORO1A.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR015049; Trimer_CC.
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:SF18; PTHR10856:SF18; 1.
DR Pfam; PF08953; DUF1899; 1.
DR Pfam; PF08954; Trimer_CC; 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; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P31146"
FT CHAIN 2..461
FT /note="Coronin-1A"
FT /id="PRO_0000050919"
FT REPEAT 13..63
FT /note="WD 1"
FT REPEAT 73..110
FT /note="WD 2"
FT REPEAT 123..160
FT /note="WD 3"
FT REPEAT 164..204
FT /note="WD 4"
FT REPEAT 207..251
FT /note="WD 5"
FT REPEAT 258..296
FT /note="WD 6"
FT REPEAT 302..349
FT /note="WD 7"
FT REGION 404..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..460
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P31146"
FT MOD_RES 2
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P31146"
FT MOD_RES 412
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P31146"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O89053"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O89053"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31146"
SQ SEQUENCE 461 AA; 50979 MW; 1721A5D093C1130A CRC64;
MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQNTWDSGFC AVNPKFVALI CEASGGGAFL
VLPLGKTGRV DKNVPMVCGH TAPVLDIAWC PHNDNVIASG SEDCSVMVWE IPDGGLTLPL
REPVVTLEGH TKRVGIVAWH PTAQNVLLSA GCDNVILVWD VGTGVAVLTL GSDVHPDTIY
SVDWSRDGAL ICTSCRDKRV RIIEPRKGTI VAEKDRPHEG TRPVRAVFVS DGKILTTGFS
RMSERQVALW DTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE
APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERKCEPIAM TVPRKSDLFQ
EDLYPPTAGP DAALTAEEWL GGRDAGPLLI SLKDGYVPPK SRELRVNRGL DTGRKRTTPE
ASGAPSSDAI SRLEEEMRKL QATVQELQKR LDRLEETVQA K
