COR1A_RAT
ID COR1A_RAT Reviewed; 461 AA.
AC Q91ZN1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Coronin-1A;
DE AltName: Full=Coronin-like protein A;
DE Short=Clipin-A;
DE AltName: Full=Tryptophan aspartate-containing coat protein;
DE Short=TACO;
GN Name=Coro1a; Synonyms=Coro1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Spleen;
RA Suzuki K., Takeshita F., Nakata N., Makino M.;
RT "Molecular cloning of rat Coro1a.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344; TISSUE=Brain;
RA Kohchi C., Inagawa H., Makino K., Terada H., Soma G.;
RT "A new therapeutic strategy of mycobacterium infection by use of anti-TACO
RT sequence.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 21-66; 187-196; 215-233; 344-354; 384-393; 417-432 AND
RP 439-446, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000250}.
CC -!- SUBUNIT: Binds actin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC Cytoplasmic vesicle, phagosome membrane {ECO:0000250}.
CC -!- PTM: phosphorylation at Ser-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; AF416730; AAL18695.1; -; mRNA.
DR EMBL; AF495469; AAM18515.1; -; mRNA.
DR EMBL; BC086971; AAH86971.1; -; mRNA.
DR RefSeq; NP_569095.1; NM_130411.2.
DR RefSeq; XP_017444198.1; XM_017588709.1.
DR AlphaFoldDB; Q91ZN1; -.
DR SMR; Q91ZN1; -.
DR BioGRID; 250886; 1.
DR STRING; 10116.ENSRNOP00000026496; -.
DR iPTMnet; Q91ZN1; -.
DR PhosphoSitePlus; Q91ZN1; -.
DR World-2DPAGE; 0004:Q91ZN1; -.
DR jPOST; Q91ZN1; -.
DR PaxDb; Q91ZN1; -.
DR PRIDE; Q91ZN1; -.
DR Ensembl; ENSRNOT00000026496; ENSRNOP00000026496; ENSRNOG00000019430.
DR GeneID; 155151; -.
DR KEGG; rno:155151; -.
DR UCSC; RGD:620009; rat.
DR CTD; 11151; -.
DR RGD; 620009; Coro1a.
DR eggNOG; KOG0303; Eukaryota.
DR GeneTree; ENSGT00940000160628; -.
DR HOGENOM; CLU_026859_0_1_1; -.
DR InParanoid; Q91ZN1; -.
DR OMA; MVMVWEI; -.
DR OrthoDB; 552726at2759; -.
DR PhylomeDB; Q91ZN1; -.
DR TreeFam; TF314280; -.
DR PRO; PR:Q91ZN1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019430; Expressed in thymus and 19 other tissues.
DR Genevisible; Q91ZN1; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005884; C:actin filament; ISO:RGD.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0001891; C:phagocytic cup; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0032426; C:stereocilium tip; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0032036; F:myosin heavy chain binding; ISO:RGD.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:RGD.
DR GO; GO:0071353; P:cellular response to interleukin-4; ISO:RGD.
DR GO; GO:0061502; P:early endosome to recycling endosome transport; ISO:RGD.
DR GO; GO:0010631; P:epithelial cell migration; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0030595; P:leukocyte chemotaxis; ISO:RGD.
DR GO; GO:0043320; P:natural killer cell degranulation; ISO:RGD.
DR GO; GO:0051126; P:negative regulation of actin nucleation; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0031339; P:negative regulation of vesicle fusion; ISO:RGD.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; ISO:RGD.
DR GO; GO:0001845; P:phagolysosome assembly; ISO:RGD.
DR GO; GO:0050918; P:positive chemotaxis; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISO:RGD.
DR GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; ISO:RGD.
DR GO; GO:0030217; P:T cell differentiation; NAS:RGD.
DR GO; GO:0043029; P:T cell homeostasis; ISO:RGD.
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; ISO:RGD.
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_0000270800"
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 407..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 425..461
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="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:O89053"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O89053"
SQ SEQUENCE 461 AA; 51065 MW; EE1094B3CF302000 CRC64;
MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQTTWDSGFC AVNPKFMALI CEASGGGAFL
VLPLGKTGRV DKNVPLVCGH TAPVLDIAWC PHNDNVIASG SEDCTVMVWE IPDGGLVLPL
REPVVTLEGH TKRVGIVAWH PTAQNVLLSA GCDNVILVWD VGTGAAVLTL GPDVHPDTIY
SVDWSRDGAL ICTSCRDKRV RVIEPRKGTV VAEKERPHEG TRPVHAVFVS EGKILTTGFS
RMSERQVALW DTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE
APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERKCEPIAM TVPRKSDLFQ
EDLYPPTAGP DPALTAEEWL SGRDAGPLLI SLKDGYVPPK SRELRVNRGL DSARRRATPE
PSSTLSSDTV SRLEEDVRNL NAIVQKLQER LDRLEETVQA K
