COR1A_HUMAN
ID COR1A_HUMAN Reviewed; 461 AA.
AC P31146; B2RBL1; Q2YD73;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 205.
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 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 [MRNA].
RC TISSUE=Peripheral blood leukocyte;
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 [MRNA].
RC TISSUE=Brain;
RA Grogan A., Keep N.H., Reeves E., Segal A.W.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Liau G., Popa I., Argraves K., Argraves W.S.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [8]
RP PROTEIN SEQUENCE OF 2-9; 50-65; 242-252; 433-448 AND 453-460, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 355-374.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [10]
RP ROLE IN PHAGOSOME TRAFFICKING.
RX PubMed=10338208; DOI=10.1016/s0092-8674(00)80754-0;
RA Ferrari G., Langen H., Naito M., Pieters J.;
RT "A coat protein on phagosomes involved in the intracellular survival of
RT mycobacteria.";
RL Cell 97:435-447(1999).
RN [11]
RP INVOLVEMENT IN IMD8.
RX PubMed=19097825; DOI=10.1016/j.clim.2008.11.002;
RA Shiow L.R., Paris K., Akana M.C., Cyster J.G., Sorensen R.U., Puck J.M.;
RT "Severe combined immunodeficiency (SCID) and attention deficit
RT hyperactivity disorder (ADHD) associated with a Coronin-1A mutation and a
RT chromosome 16p11.2 deletion.";
RL Clin. Immunol. 131:24-30(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
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 [15]
RP UBIQUITINATION BY RNF128.
RX PubMed=22016387; DOI=10.1074/jbc.m111.222711;
RA Ichikawa D., Mizuno M., Yamamura T., Miyake S.;
RT "GRAIL (gene related to anergy in lymphocytes) regulates cytoskeletal
RT reorganization through ubiquitination and degradation of Arp2/3 subunit 5
RT and coronin 1A.";
RL J. Biol. Chem. 286:43465-43474(2011).
RN [16]
RP PHOSPHORYLATION AT SER-2 AND THR-412, AND INTERACTION WITH ACTIN.
RX PubMed=23100250; DOI=10.1074/jbc.m112.349829;
RA Oku T., Nakano M., Kaneko Y., Ando Y., Kenmotsu H., Itoh S., Tsuiji M.,
RA Seyama Y., Toyoshima S., Tsuji T.;
RT "Constitutive turnover of phosphorylation at Thr-412 of human p57/coronin-1
RT regulates the interaction with actin.";
RL J. Biol. Chem. 287:42910-42920(2012).
RN [17]
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP VARIANT IMD8 MET-134, AND CHARACTERIZATION OF VARIANT IMD8 MET-134.
RX PubMed=23522482; DOI=10.1016/j.jaci.2013.01.042;
RA Moshous D., Martin E., Carpentier W., Lim A., Callebaut I., Canioni D.,
RA Hauck F., Majewski J., Schwartzentruber J., Nitschke P., Sirvent N.,
RA Frange P., Picard C., Blanche S., Revy P., Fischer A., Latour S.,
RA Jabado N., de Villartay J.P.;
RT "Whole-exome sequencing identifies Coronin-1A deficiency in 3 siblings with
RT immunodeficiency and EBV-associated B-cell lymphoproliferation.";
RL J. Allergy Clin. Immunol. 131:1594-1603(2013).
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 cells,
CC its retention on the phagosomal membrane prevents fusion between
CC phagosomes and lysosomes. {ECO:0000269|PubMed:10338208}.
CC -!- SUBUNIT: Binds actin.
CC -!- INTERACTION:
CC P31146; P05067: APP; NbExp=3; IntAct=EBI-1046676, EBI-77613;
CC P31146; A1L4K1: FSD2; NbExp=7; IntAct=EBI-1046676, EBI-5661036;
CC P31146; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1046676, EBI-618309;
CC P31146; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-1046676, EBI-9091197;
CC P31146; P43364: MAGEA11; NbExp=3; IntAct=EBI-1046676, EBI-739552;
CC P31146; P40763: STAT3; NbExp=2; IntAct=EBI-1046676, EBI-518675;
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:0000269|PubMed:23100250}.
CC -!- PTM: Polyubiquitinated by RNF128 with 'Lys-48'-linked chains, leading
CC to proteasomal degradation. {ECO:0000269|PubMed:22016387}.
CC -!- DISEASE: Immunodeficiency 8 (IMD8) [MIM:615401]: A disease of the
CC immune system leading to recurrent infections, and characterized by
CC CD4+ T-cells lymphopenia. Patients can develop B-cell
CC lymphoproliferation associated with Epstein-Barr virus infection.
CC {ECO:0000269|PubMed:19097825, ECO:0000269|PubMed:23522482}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
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DR EMBL; D44497; BAA07940.1; -; mRNA.
DR EMBL; X89109; CAA61482.1; -; mRNA.
DR EMBL; U34690; AAA77058.1; -; mRNA.
DR EMBL; AF495470; AAM18516.1; -; mRNA.
DR EMBL; AK314714; BAG37258.1; -; mRNA.
DR EMBL; CH471238; EAW79906.1; -; Genomic_DNA.
DR EMBL; BC110374; AAI10375.1; -; mRNA.
DR EMBL; BC126385; AAI26386.1; -; mRNA.
DR EMBL; BC126387; AAI26388.1; -; mRNA.
DR CCDS; CCDS10673.1; -.
DR PIR; S65665; S65665.
DR RefSeq; NP_001180262.1; NM_001193333.2.
DR RefSeq; NP_009005.1; NM_007074.3.
DR RefSeq; XP_011544016.1; XM_011545714.2.
DR AlphaFoldDB; P31146; -.
DR SMR; P31146; -.
DR BioGRID; 116322; 121.
DR IntAct; P31146; 51.
DR MINT; P31146; -.
DR STRING; 9606.ENSP00000219150; -.
DR GlyGen; P31146; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P31146; -.
DR MetOSite; P31146; -.
DR PhosphoSitePlus; P31146; -.
DR SwissPalm; P31146; -.
DR BioMuta; CORO1A; -.
DR DMDM; 1706004; -.
DR OGP; P31146; -.
DR UCD-2DPAGE; P31146; -.
DR EPD; P31146; -.
DR jPOST; P31146; -.
DR MassIVE; P31146; -.
DR MaxQB; P31146; -.
DR PaxDb; P31146; -.
DR PeptideAtlas; P31146; -.
DR PRIDE; P31146; -.
DR ProteomicsDB; 54759; -.
DR TopDownProteomics; P31146; -.
DR Antibodypedia; 27060; 483 antibodies from 40 providers.
DR DNASU; 11151; -.
DR Ensembl; ENST00000219150.10; ENSP00000219150.6; ENSG00000102879.16.
DR Ensembl; ENST00000570045.5; ENSP00000455552.1; ENSG00000102879.16.
DR GeneID; 11151; -.
DR KEGG; hsa:11151; -.
DR MANE-Select; ENST00000219150.10; ENSP00000219150.6; NM_007074.4; NP_009005.1.
DR UCSC; uc002dww.4; human.
DR CTD; 11151; -.
DR DisGeNET; 11151; -.
DR GeneCards; CORO1A; -.
DR HGNC; HGNC:2252; CORO1A.
DR HPA; ENSG00000102879; Group enriched (bone marrow, lymphoid tissue).
DR MalaCards; CORO1A; -.
DR MIM; 605000; gene.
DR MIM; 615401; phenotype.
DR neXtProt; NX_P31146; -.
DR OpenTargets; ENSG00000102879; -.
DR Orphanet; 228003; Severe combined immunodeficiency due to CORO1A deficiency.
DR PharmGKB; PA26768; -.
DR VEuPathDB; HostDB:ENSG00000102879; -.
DR eggNOG; KOG0303; Eukaryota.
DR GeneTree; ENSGT00940000160628; -.
DR HOGENOM; CLU_026859_0_1_1; -.
DR InParanoid; P31146; -.
DR OMA; MVMVWEI; -.
DR OrthoDB; 552726at2759; -.
DR PhylomeDB; P31146; -.
DR TreeFam; TF314280; -.
DR PathwayCommons; P31146; -.
DR Reactome; R-HSA-9636383; Prevention of phagosomal-lysosomal fusion.
DR SignaLink; P31146; -.
DR SIGNOR; P31146; -.
DR BioGRID-ORCS; 11151; 23 hits in 1087 CRISPR screens.
DR ChiTaRS; CORO1A; human.
DR GeneWiki; CORO1A; -.
DR GenomeRNAi; 11151; -.
DR Pharos; P31146; Tbio.
DR PRO; PR:P31146; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P31146; protein.
DR Bgee; ENSG00000102879; Expressed in granulocyte and 168 other tissues.
DR ExpressionAtlas; P31146; baseline and differential.
DR Genevisible; P31146; HS.
DR GO; GO:0005884; C:actin filament; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IPI:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; IMP:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISS:UniProtKB.
DR GO; GO:0032036; F:myosin heavy chain binding; IPI:UniProtKB.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
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; IMP:UniProtKB.
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:0045087; P:innate immune response; NAS:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; IEA:Ensembl.
DR GO; GO:0043320; P:natural killer cell degranulation; IMP:UniProtKB.
DR GO; GO:0051126; P:negative regulation of actin nucleation; IDA:UniProtKB.
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:0006909; P:phagocytosis; IMP:UniProtKB.
DR GO; GO:0001845; P:phagolysosome assembly; IMP:UniProtKB.
DR GO; GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
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:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
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; Disease variant; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8"
FT CHAIN 2..461
FT /note="Coronin-1A"
FT /id="PRO_0000050920"
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 403..432
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:0000269|Ref.8"
FT MOD_RES 2
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:23100250"
FT MOD_RES 412
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000269|PubMed:23100250"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O89053"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 134
FT /note="V -> M (in IMD8; the mutation causes a decrease in
FT protein stability; patient T-cell blasts show delayed
FT activation of signaling molecules MAPK3 and MAPK1;
FT dbSNP:rs397514755)"
FT /evidence="ECO:0000269|PubMed:23522482"
FT /id="VAR_070447"
FT VARIANT 415
FT /note="R -> K (in dbSNP:rs1804109)"
FT /id="VAR_011956"
FT CONFLICT 8
FT /note="S -> T (in Ref. 3; AAA77058)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="R -> W (in Ref. 3; AAA77058)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 51026 MW; DE3FEDA57041515E CRC64;
MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQTTWDSGFC AVNPKFVALI CEASGGGAFL
VLPLGKTGRV DKNAPTVCGH TAPVLDIAWC PHNDNVIASG SEDCTVMVWE IPDGGLMLPL
REPVVTLEGH TKRVGIVAWH TTAQNVLLSA GCDNVIMVWD VGTGAAMLTL GPEVHPDTIY
SVDWSRDGGL ICTSCRDKRV RIIEPRKGTV VAEKDRPHEG TRPVRAVFVS EGKILTTGFS
RMSERQVALW DTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE
APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERRCEPIAM TVPRKSDLFQ
EDLYPPTAGP DPALTAEEWL GGRDAGPLLI SLKDGYVPPK SRELRVNRGL DTGRRRAAPE
ASGTPSSDAV SRLEEEMRKL QATVQELQKR LDRLEETVQA K
