Coronin-1A - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P31146 (COR1A_HUMAN)

Last modified June 16, 2009. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Coronin-1A
Alternative name(s):
    Coronin-like protein p57
    Coronin-like protein A
      Short name=Clipin-A
    Tryptophan aspartate-containing coat protein
      Short name=TACO

Gene names

Name:	CORO1A
Synonyms:	CORO1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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. Ref.8
Subunit structure	Binds actin By similarity.
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cytoplasm › cell cortex By similarity. Cytoplasmic vesicle › phagosome membrane By similarity. 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 By similarity.
Tissue specificity	Expressed in brain, thymus, spleen, bone marrow and lymph node. Low in lung and gut.
Sequence similarities	Belongs to the WD repeat coronin family. Contains 5 WD repeats.

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Ontologies

Keywords
Cellular component	Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat WD repeat
Ligand	Actin-binding
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell-substrate adhesion Inferred from mutant phenotype. Source: UniProtKB innate immune response Non-traceable author statement. Source: UniProtKB negative regulation of actin nucleation Inferred from direct assay. Source: UniProtKB phagolysosome formation Inferred from mutant phenotype. Source: UniProtKB positive chemotaxis Inferred from direct assay. Source: UniProtKB
Cellular component	cortical actin cytoskeleton Inferred from direct assay. Source: UniProtKB filamentous actin Inferred from direct assay. Source: UniProtKB lamellipodium Inferred from direct assay. Source: UniProtKB phagocytic cup Inferred from direct assay. Source: UniProtKB phagocytic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin filament binding Ref.1 Inferred from direct assay. Source: UniProtKB phosphoinositide 3-kinase binding Inferred from direct assay. Source: UniProtKB protein C-terminus binding Inferred from physical interaction. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
DKK1	O94907	1	EBI-1046676,EBI-742864
UBE2G2	P60604	1	EBI-1046676,EBI-1051028

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 461

460

Coronin-1A

PRO_0000050920

Regions

Repeat

79 – 119

WD 1

Repeat

129 – 169

WD 2

Repeat

174 – 213

WD 3

Repeat

218 – 260

WD 4

Repeat

265 – 305

WD 5

Coiled coil

424 – 460

Potential

Amino acid modifications

Modified residue

N-acetylserine Ref.6

Natural variations

Natural variant

415

R → K: dbSNP rs1804109.

VAR_011956

Natural variant

443

T → P: dbSNP rs1053574.

VAR_011957

Experimental info

Sequence conflict

S → T in AAA77058. Ref.3

Sequence conflict

245

R → W in AAA77058. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P31146-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: DE3FEDA57041515E
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FASTA

461

51,026

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a novel actin-binding protein, p57, with a WD repeat and a leucine zipper motif." Suzuki K., Nishihata J., Arai Y., Honma N., Yamamoto K., Irimura T., Toyoshima S. FEBS Lett. 364:283-288(1995) [PubMed: 7758584] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Peripheral blood leukocyte.
[2]	Grogan A., Keep N.H., Reeves E., Segal A.W. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	Liau G., Popa I., Argraves K., Argraves W.S. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[4]	"A new therapeutic strategy of mycobacterium infection by use of anti-TACO sequence." Kohchi C., Inagawa H., Makino K., Terada H., Soma G. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-9; 50-65; 242-252; 433-448 AND 453-460, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: T-cell.
[7]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 355-374. Tissue: Keratinocyte.
[8]	"A coat protein on phagosomes involved in the intracellular survival of mycobacteria." Ferrari G., Langen H., Naito M., Pieters J. Cell 97:435-447(1999) [PubMed: 10338208] [Abstract] Cited for: ROLE IN PHAGOSOME TRAFFICKING.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	D44497 mRNA. Translation: BAA07940.1. X89109 mRNA. Translation: CAA61482.1. U34690 mRNA. Translation: AAA77058.1. AF495470 mRNA. Translation: AAM18516.1. BC110374 mRNA. Translation: AAI10375.1. BC126385 mRNA. Translation: AAI26386.1. BC126387 mRNA. Translation: AAI26388.1.
IPI	IPI00010133.
PIR	S65665.
RefSeq	NP_009005.1.
UniGene	Hs.415067
3D structure databases
HSSP	HSSP built from PDB template 1ERJ based on UniProtKB P16649.
SMR	P31146. Positions 7-401, 8-402.
ModBase	Search...
Protein-protein interaction databases
IntAct	P31146. 2 interactions.
PTM databases
PhosphoSite	P31146.
2-D gel databases
Aarhus/Ghent-2DPAGE	2416. IEF.
OGP	P31146.
Proteomic databases
PeptideAtlas	P31146.
PRIDE	P31146.
Genome annotation databases
Ensembl	ENSG00000102879. Homo sapiens. [Contig view]
GeneID	11151.
KEGG	hsa:11151.
Organism-specific databases
GeneCards	GC16P030103.
H-InvDB	HIX0012929.
HGNC	HGNC:2252. CORO1A.
MIM	605000. gene.
PharmGKB	PA26768.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P31146.
HOVERGEN	P31146.
OMA	P31146. HAVFVSE.
Gene expression databases
ArrayExpress	P31146.
Bgee	P31146.
CleanEx	HS_CORO1A.
GermOnline	ENSG00000102879. Homo sapiens.
Family and domain databases
InterPro	IPR015505. Coronin. IPR015048. DUF1899. IPR015049. DUF1900. IPR015943. WD40/YVTN_repeat-like. IPR001680. WD40_repeat. IPR019782. WD40_repeat_2. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_region. IPR019781. WD40_repeat_sg. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PANTHER	PTHR10856. Coronin. 1 hit.
Pfam	PF08953. DUF1899. 1 hit. PF08954. DUF1900. 1 hit. PF00400. WD40. 3 hits. [Graphical view]
ProDom	PD000018. WD40. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00320. WD40. 3 hits. [Graphical view]
PROSITE	PS00678. WD_REPEATS_1. 2 hits. PS50082. WD_REPEATS_2. 2 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	42396.
SOURCE	Search...

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Entry information

Entry name

COR1A_HUMAN

Accession

Primary (citable) accession number: P31146
Secondary accession number(s): Q2YD73

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 87 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents