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Coronin-1A (Coronin-like protein A) (Clipin-A) (Coronin-like protein p57) (Tryptophan aspartate-containing coat protein) (TACO)

 COR1A_MOUSE             Reviewed;         461 AA.
O89053; Q7TMU0; Q9R1Y8; Q9R288;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
22-NOV-2017, entry version 160.
RecName: Full=Coronin-1A;
AltName: Full=Coronin-like protein A;
Short=Clipin-A;
AltName: Full=Coronin-like protein p57;
AltName: Full=Tryptophan aspartate-containing coat protein;
Short=TACO;
Name=Coro1a; Synonyms=Coro1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9778037; DOI=10.1089/dna.1998.17.779;
Okumura M., Kung C., Wong S., Rodgers M., Thomas M.L.;
"Definition of family of coronin-related proteins conserved between
humans and mice: close genetic linkage between coronin-2 and CD45-
associated protein.";
DNA Cell Biol. 17:779-787(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-14, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND ROLE IN PHAGOSOME TRAFFICKING.
STRAIN=C57BL/6J; TISSUE=Macrophage;
PubMed=10338208; DOI=10.1016/S0092-8674(00)80754-0;
Ferrari G., Langen H., Naito M., Pieters J.;
"A coat protein on phagosomes involved in the intracellular survival
of mycobacteria.";
Cell 97:435-447(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Kohchi C., Inagawa H., Makino K., Terada H., Soma G.;
"A new therapeutic strategy of mycobacterium infection by use of anti-
TACO sequence.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hematopoietic, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 156-276.
STRAIN=BALB/cJ; TISSUE=Spleen;
PubMed=9798653; DOI=10.1016/S0161-5890(98)00031-5;
Chu C.C., Paul W.E.;
"Expressed genes in interleukin-4 treated B cells identified by cDNA
representational difference analysis.";
Mol. Immunol. 35:487-502(1998).
[6]
PROTEIN SEQUENCE OF 215-233, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418 AND SER-422, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
PHOSPHORYLATION AT SER-412.
PubMed=23100250; DOI=10.1074/jbc.M112.349829;
Oku T., Nakano M., Kaneko Y., Ando Y., Kenmotsu H., Itoh S.,
Tsuiji M., Seyama Y., Toyoshima S., Tsuji T.;
"Constitutive turnover of phosphorylation at Thr-412 of human
p57/coronin-1 regulates the interaction with actin.";
J. Biol. Chem. 287:42910-42920(2012).
[10]
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 430-461, AND COILED-COIL
DOMAIN.
PubMed=16172398; DOI=10.1073/pnas.0502390102;
Kammerer R.A., Kostrewa D., Progias P., Honnappa S., Avila D.,
Lustig A., Winkler F.K., Pieters J., Steinmetz M.O.;
"A conserved trimerization motif controls the topology of short coiled
coils.";
Proc. Natl. Acad. Sci. U.S.A. 102:13891-13896(2005).
[11]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-402, WD REPEATS, AND
COILED-COIL DOMAIN.
PubMed=16407068; DOI=10.1016/j.str.2005.09.013;
Appleton B.A., Wu P., Wiesmann C.;
"The crystal structure of murine coronin-1: a regulator of actin
cytoskeletal dynamics in lymphocytes.";
Structure 14:87-96(2006).
-!- FUNCTION: May be a crucial component of the cytoskeleton of highly
motile cells, functioning both in the invagination of large pieces
of plasma membrane, as well as in forming protrusions of the
plasma membrane involved in cell locomotion. In mycobacteria-
infected cells, its retention on the phagosomal membrane prevents
fusion between phagosomes and lysosomes.
{ECO:0000269|PubMed:10338208}.
-!- SUBUNIT: Binds actin. {ECO:0000250}.
-!- INTERACTION:
P63092:GNAS (xeno); NbExp=2; IntAct=EBI-6665847, EBI-1047114;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10338208}. Cytoplasm, cell cortex
{ECO:0000269|PubMed:10338208}. Cytoplasmic vesicle, phagosome
membrane {ECO:0000269|PubMed:10338208}. Note=In non-infected
macrophages, associated with the cortical microtubule network. In
mycobacteria-infected macrophages, becomes progressively
relocalized and retained around the mycobacterial phagosomes.
Retention on the phagosomal membrane is strictly dependent on
mycobacterial viability and not due to impaired acidification.
-!- TISSUE SPECIFICITY: Expressed in spleen, lymph nodes, thymus,
brain and at very lower levels in lung. Also expressed in cells of
the lymphoid/myeloid lineage. Not expressed in Kuffper cells.
{ECO:0000269|PubMed:10338208}.
-!- PTM: phosphorylation at Ser-412 by PKC strongly down-regulates the
association with actin. {ECO:0000250}.
-!- PTM: Polyubiquitinated by RNF128 with 'Lys-48'-linked chains,
leading to proteasomal degradation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the WD repeat coronin family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF143955; AAD32703.1; -; mRNA.
EMBL; AF047388; AAD31082.1; -; mRNA.
EMBL; AF495468; AAM18514.1; -; mRNA.
EMBL; BC002136; AAH02136.1; -; mRNA.
EMBL; BC053398; AAH53398.1; -; mRNA.
EMBL; U89399; AAC36506.1; -; mRNA.
CCDS; CCDS21840.1; -.
RefSeq; NP_001288303.1; NM_001301374.1.
RefSeq; NP_034028.1; NM_009898.3.
RefSeq; XP_006507347.1; XM_006507284.3.
RefSeq; XP_006507348.1; XM_006507285.3.
UniGene; Mm.290482; -.
PDB; 2AKF; X-ray; 1.20 A; A/B/C=430-461.
PDB; 2AQ5; X-ray; 1.75 A; A=1-402.
PDB; 2B4E; X-ray; 2.30 A; A=1-402.
PDBsum; 2AKF; -.
PDBsum; 2AQ5; -.
PDBsum; 2B4E; -.
ProteinModelPortal; O89053; -.
SMR; O89053; -.
BioGrid; 198732; 2.
IntAct; O89053; 3.
MINT; MINT-4091570; -.
STRING; 10090.ENSMUSP00000032949; -.
iPTMnet; O89053; -.
PhosphoSitePlus; O89053; -.
SwissPalm; O89053; -.
EPD; O89053; -.
PaxDb; O89053; -.
PeptideAtlas; O89053; -.
PRIDE; O89053; -.
Ensembl; ENSMUST00000032949; ENSMUSP00000032949; ENSMUSG00000030707.
Ensembl; ENSMUST00000106364; ENSMUSP00000101972; ENSMUSG00000030707.
GeneID; 12721; -.
KEGG; mmu:12721; -.
UCSC; uc009jsk.2; mouse.
CTD; 11151; -.
MGI; MGI:1345961; Coro1a.
eggNOG; KOG0303; Eukaryota.
eggNOG; ENOG410XQAD; LUCA.
GeneTree; ENSGT00760000119195; -.
HOGENOM; HOG000166356; -.
HOVERGEN; HBG059978; -.
InParanoid; O89053; -.
KO; K13882; -.
OMA; CYDDIRI; -.
OrthoDB; EOG091G03H5; -.
PhylomeDB; O89053; -.
TreeFam; TF314280; -.
ChiTaRS; Coro1a; mouse.
EvolutionaryTrace; O89053; -.
PRO; PR:O89053; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030707; -.
CleanEx; MM_CORO1A; -.
ExpressionAtlas; O89053; baseline and differential.
Genevisible; O89053; MM.
GO; GO:0005884; C:actin filament; ISO:MGI.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0031252; C:cell leading edge; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0001772; C:immunological synapse; IDA:MGI.
GO; GO:0030027; C:lamellipodium; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0001891; C:phagocytic cup; ISO:MGI.
GO; GO:0045335; C:phagocytic vesicle; ISO:MGI.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0051015; F:actin filament binding; IDA:MGI.
GO; GO:0003785; F:actin monomer binding; ISO:MGI.
GO; GO:0008092; F:cytoskeletal protein binding; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; IGI:MGI.
GO; GO:0032036; F:myosin heavy chain binding; ISO:MGI.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
GO; GO:0007015; P:actin filament organization; IMP:MGI.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0016477; P:cell migration; IMP:MGI.
GO; GO:0031589; P:cell-substrate adhesion; ISO:MGI.
GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
GO; GO:0061502; P:early endosome to recycling endosome transport; IMP:MGI.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
GO; GO:0030595; P:leukocyte chemotaxis; IMP:MGI.
GO; GO:0043320; P:natural killer cell degranulation; ISO:MGI.
GO; GO:0051126; P:negative regulation of actin nucleation; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
GO; GO:0031339; P:negative regulation of vesicle fusion; IMP:MGI.
GO; GO:0038180; P:nerve growth factor signaling pathway; IGI:MGI.
GO; GO:0006909; P:phagocytosis; ISO:MGI.
GO; GO:0001845; P:phagolysosome assembly; ISO:MGI.
GO; GO:0050918; P:positive chemotaxis; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI.
GO; GO:0050870; P:positive regulation of T cell activation; IMP:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
GO; GO:0030833; P:regulation of actin filament polymerization; IMP:MGI.
GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IMP:MGI.
GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IGI:MGI.
GO; GO:0034097; P:response to cytokine; IMP:MGI.
GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
GO; GO:0032796; P:uropod organization; IMP:MGI.
Gene3D; 2.120.10.30; -; 1.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR029508; CORO1A.
InterPro; IPR015505; Coronin.
InterPro; IPR015048; DUF1899.
InterPro; IPR015049; Trimer_CC.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR10856; PTHR10856; 1.
PANTHER; PTHR10856:SF18; PTHR10856:SF18; 1.
Pfam; PF08953; DUF1899; 1.
Pfam; PF08954; Trimer_CC; 1.
Pfam; PF00400; WD40; 3.
SMART; SM01166; DUF1899; 1.
SMART; SM00320; WD40; 3.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 2.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Direct protein sequencing; Membrane; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P31146}.
CHAIN 2 461 Coronin-1A.
/FTId=PRO_0000050921.
REPEAT 13 63 WD 1. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:16407068}.
REPEAT 73 110 WD 2. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:16407068}.
REPEAT 123 160 WD 3. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:16407068}.
REPEAT 164 204 WD 4. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:16407068}.
REPEAT 207 251 WD 5. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:16407068}.
REPEAT 258 296 WD 6. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:16407068}.
REPEAT 302 349 WD 7. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:16407068}.
COILED 424 461 {ECO:0000269|PubMed:16172398,
ECO:0000269|PubMed:16407068}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P31146}.
MOD_RES 2 2 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P31146}.
MOD_RES 412 412 Phosphoserine; by PKC.
{ECO:0000269|PubMed:23100250}.
MOD_RES 418 418 Phosphothreonine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 125 125 I -> V (in Ref. 1; AAD32703 and 4;
AAH02136). {ECO:0000305}.
CONFLICT 299 299 S -> F (in Ref. 4; AAH53398).
{ECO:0000305}.
TURN 10 13 {ECO:0000244|PDB:2AQ5}.
STRAND 15 18 {ECO:0000244|PDB:2AQ5}.
HELIX 21 23 {ECO:0000244|PDB:2AQ5}.
STRAND 24 27 {ECO:0000244|PDB:2AQ5}.
STRAND 39 42 {ECO:0000244|PDB:2AQ5}.
STRAND 44 51 {ECO:0000244|PDB:2AQ5}.
STRAND 54 56 {ECO:0000244|PDB:2AQ5}.
STRAND 59 63 {ECO:0000244|PDB:2AQ5}.
STRAND 84 89 {ECO:0000244|PDB:2AQ5}.
STRAND 96 101 {ECO:0000244|PDB:2AQ5}.
STRAND 104 110 {ECO:0000244|PDB:2AQ5}.
STRAND 124 128 {ECO:0000244|PDB:2AQ5}.
STRAND 134 139 {ECO:0000244|PDB:2AQ5}.
STRAND 141 143 {ECO:0000244|PDB:2AQ5}.
STRAND 146 151 {ECO:0000244|PDB:2AQ5}.
STRAND 156 160 {ECO:0000244|PDB:2AQ5}.
TURN 161 163 {ECO:0000244|PDB:2AQ5}.
STRAND 166 170 {ECO:0000244|PDB:2AQ5}.
TURN 172 174 {ECO:0000244|PDB:2AQ5}.
STRAND 179 184 {ECO:0000244|PDB:2AQ5}.
STRAND 191 195 {ECO:0000244|PDB:2AQ5}.
STRAND 198 204 {ECO:0000244|PDB:2AQ5}.
TURN 205 208 {ECO:0000244|PDB:2AQ5}.
STRAND 209 215 {ECO:0000244|PDB:2AQ5}.
STRAND 220 222 {ECO:0000244|PDB:2AQ5}.
STRAND 225 228 {ECO:0000244|PDB:2AQ5}.
STRAND 233 239 {ECO:0000244|PDB:2AQ5}.
STRAND 245 251 {ECO:0000244|PDB:2AQ5}.
STRAND 259 263 {ECO:0000244|PDB:2AQ5}.
STRAND 271 275 {ECO:0000244|PDB:2AQ5}.
TURN 277 279 {ECO:0000244|PDB:2AQ5}.
STRAND 281 286 {ECO:0000244|PDB:2AQ5}.
STRAND 292 297 {ECO:0000244|PDB:2AQ5}.
STRAND 304 310 {ECO:0000244|PDB:2AQ5}.
STRAND 317 321 {ECO:0000244|PDB:2AQ5}.
HELIX 324 326 {ECO:0000244|PDB:2AQ5}.
HELIX 329 331 {ECO:0000244|PDB:2AQ5}.
STRAND 333 341 {ECO:0000244|PDB:2AQ5}.
STRAND 344 351 {ECO:0000244|PDB:2AQ5}.
TURN 361 363 {ECO:0000244|PDB:2AQ5}.
HELIX 376 380 {ECO:0000244|PDB:2AQ5}.
HELIX 432 460 {ECO:0000244|PDB:2AKF}.
SEQUENCE 461 AA; 50989 MW; 9098F53757C5318D CRC64;
MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQTTWDSGFC AVNPKFMALI CEASGGGAFL
VLPLGKTGRV DKNVPLVCGH TAPVLDIAWC PHNDNVIASG SEDCTVMVWE IPDGGLVLPL
REPVITLEGH TKRVGIVAWH PTAQNVLLSA GCDNVILVWD VGTGAAVLTL GPDVHPDTIY
SVDWSRDGAL ICTSCRDKRV RVIEPRKGTV VAEKDRPHEG TRPVHAVFVS EGKILTTGFS
RMSERQVALW DTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE
APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERKCEPIAM TVPRKSDLFQ
EDLYPPTAGP DPALTAEEWL GGRDAGPLLI SLKDGYVPPK SRELRVNRGL DSARRRATPE
PSGTPSSDTV SRLEEDVRNL NAIVQKLQER LDRLEETVQA K


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