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UniProtKB/Swiss-Prot entry P31146


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COR1A_HUMAN
Primary accession number P31146
Secondary accession number Q2YD73
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 4, 2008 (Entry version 81)
Name and origin of the protein
Protein name Coronin-1A
Synonyms Coronin-like protein p57
Coronin-like protein A
Clipin-A
Tryptophan aspartate-containing coat protein
TACO
Gene name
Name: CORO1A
Synonyms: CORO1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Peripheral blood leukocyte;
DOI=10.1016/0014-5793(95)00393-N; PubMed=7758584 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki K., Nishihata J., Arai Y., Honma N., Yamamoto K., Irimura T., Toyoshima S.;
"Molecular cloning of a novel actin-binding protein, p57, with a WD repeat and a leucine zipper motif.";
FEBS Lett. 364:283-288(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Grogan A., Keep N.H., Reeves E., Segal A.W.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
Liau G., Popa I., Argraves K., Argraves W.S.;
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
PROTEIN SEQUENCE OF 2-9; 50-65; 242-252; 433-448 AND 453-460, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 355-374.
TISSUE=Keratinocyte;
DOI=10.1002/elps.11501301199; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[8]
ROLE IN PHAGOSOME TRAFFICKING.
DOI=10.1016/S0092-8674(00)80754-0; PubMed=10338208 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D44497; BAA07940.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X89109; CAA61482.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U34690; AAA77058.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF495470; AAM18516.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC110374; AAI10375.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126385; AAI26386.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126387; AAI26388.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S65665; S65665.
RefSeq NP_009005.1; -.
UniGene Hs.415067
3D structure databases
HSSP P16649; 1ERJ. [HSSP ENTRY / PDB]
SMR P31146; 7-401, 8-402.
ModBase P31146.
Protein-protein interaction databases
IntAct P31146; -.
PTM databases
PhosphoSite P31146; -.
2D gel databases
Aarhus/Ghent-2DPAGE 2416; IEF.
OGP P31146; -.
Organism-specific databases
H-InvDB HIX0012929; -.
HGNC HGNC:2252; CORO1A.
GenAtlas CORO1A.
MIM 605000; gene. [NCBI / EBI]
PharmGKB PA26768; -.
GeneCards P31146.
Gene expression databases
ArrayExpress P31146; -.
CleanEx HS_CORO1A; -.
GermOnline ENSG00000102879; Homo sapiens.
Ontologies
GO
GO:0030864; Cellular component: cortical actin cytoskeleton (inferred from direct assay from UniProtKB).
GO:0031941; Cellular component: filamentous actin (inferred from direct assay from UniProtKB).
GO:0030027; Cellular component: lamellipodium (inferred from direct assay from UniProtKB).
GO:0001891; Cellular component: phagocytic cup (inferred from direct assay from UniProtKB).
GO:0045335; Cellular component: phagocytic vesicle (inferred from direct assay from UniProtKB).
GO:0051015; Molecular function: actin filament binding (inferred from direct assay from UniProtKB).
GO:0043548; Molecular function: phosphoinositide 3-kinase binding (inferred from direct assay from UniProtKB).
GO:0008022; Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (inferred from direct assay from UniProtKB).
GO:0006928; Biological process: cell motion (non-traceable author statement from UniProtKB).
GO:0031589; Biological process: cell-substrate adhesion (inferred from mutant phenotype from UniProtKB).
GO:0045087; Biological process: innate immune response (non-traceable author statement from UniProtKB).
GO:0051126; Biological process: negative regulation of actin nucleation (inferred from direct assay from UniProtKB).
GO:0001845; Biological process: phagolysosome formation (inferred from mutant phenotype from UniProtKB).
GO:0050918; Biological process: positive chemotaxis (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR015505; Coronin.
IPR015048; DUF1899.
IPR015049; DUF1900.
IPR015943; WD40/YVTN_repeat-like.
IPR001680; WD40_repeat.
Graphical view of domain structure.
Gene3D G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
PANTHER PTHR10856; Coronin; 1.
Pfam PF08953; DUF1899; 1.
PF08954; DUF1900; 1.
PF00400; WD40; 3.
Pfam graphical view of domain structure.
PRINTS PR00320; GPROTEINBRPT.
ProDom PD000018; WD40; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00320; WD40; 3.
SMART graphical view of domain structure.
PROSITE PS00678; WD_REPEATS_1; 2.
PS50082; WD_REPEATS_2; 2.
PS50294; WD_REPEATS_REGION; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P31146.
ProtoNet P31146.
Proteomic databases
PeptideAtlas P31146; -.
Genome annotation databases
Ensembl ENSG00000102879; Homo sapiens. [Contig view]
GeneID 11151; -.
KEGG hsa:11151; -.
Phylogenomic databases
HOGENOM P31146; -.
HOVERGEN P31146; -.
Other
LinkHub P31146; -.
NextBio 42396; -.
SOURCE CORO1A; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Actin-binding; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing; Membrane; Polymorphism; Repeat; WD repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   461  460     Coronin-1A. PRO_0000050920
REPEAT   79   119  41     WD 1. 
REPEAT   129   169  41     WD 2. 
REPEAT   174   213  40     WD 3. 
REPEAT   218   260  43     WD 4. 
REPEAT   265   305  41     WD 5. 
COILED   424   460  37     Potential. 
MOD_RES   2     2        N-acetylserine. 
VARIANT   415   415  1     R -> K (in dbSNP:rs1804109 [NCBI]). VAR_011956 
VARIANT   443   443  1     T -> P (in dbSNP:rs1053574 [NCBI]). VAR_011957 
CONFLICT   8     8        S -> T (in Ref. 3; AAA77058). 
CONFLICT   245   245        R -> W (in Ref. 3; AAA77058). 
Sequence information
Length: 461 AA [This is the length of the unprocessed precursor] Molecular weight: 51026 Da [This is the MW of the unprocessed precursor] CRC64: DE3FEDA57041515E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQTTWDSGFC AVNPKFVALI CEASGGGAFL 

        70         80         90        100        110        120 
VLPLGKTGRV DKNAPTVCGH TAPVLDIAWC PHNDNVIASG SEDCTVMVWE IPDGGLMLPL 

       130        140        150        160        170        180 
REPVVTLEGH TKRVGIVAWH TTAQNVLLSA GCDNVIMVWD VGTGAAMLTL GPEVHPDTIY 

       190        200        210        220        230        240 
SVDWSRDGGL ICTSCRDKRV RIIEPRKGTV VAEKDRPHEG TRPVRAVFVS EGKILTTGFS 

       250        260        270        280        290        300 
RMSERQVALW DTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE 

       310        320        330        340        350        360 
APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERRCEPIAM TVPRKSDLFQ 

       370        380        390        400        410        420 
EDLYPPTAGP DPALTAEEWL GGRDAGPLLI SLKDGYVPPK SRELRVNRGL DTGRRRAAPE 

       430        440        450        460 
ASGTPSSDAV SRLEEEMRKL QATVQELQKR LDRLEETVQA K 

P31146 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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