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P31146 (COR1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coronin-1A
Alternative name(s):
Coronin-like protein A
Short name=Clipin-A
Coronin-like protein p57
Tryptophan aspartate-containing coat protein
Short name=TACO
Gene names
Name:CORO1A
Synonyms:CORO1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.10

Subunit structure

Binds actin.

Subcellular location

Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Cytoplasmic vesiclephagosome 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.

Post-translational modification

phosphorylation at Thr-412 by PKC strongly down-regulates the association with actin.

Polyubiquitinated by RNF128 with 'Lys-48'-linked chains, leading to proteasomal degradation.

Involvement in disease

Immunodeficiency 8 (IMD8) [MIM:615401]: A disease of the immune system leading to recurrent infections, and characterized by CD4+ T-cells lymphopenia. Patients can develop B-cell lymphoproliferation associated with Epstein-Barr virus infection.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.17

Sequence similarities

Belongs to the WD repeat coronin family.

Contains 7 WD repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainCoiled coil
Repeat
WD repeat
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell homeostasis

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton organization

Inferred from mutant phenotype PubMed 17442961. Source: UniProtKB

actin filament organization

Inferred from electronic annotation. Source: Ensembl

calcium ion transport

Inferred from electronic annotation. Source: Ensembl

cell-substrate adhesion

Inferred from mutant phenotype PubMed 17442961. Source: UniProtKB

cellular component movement

Non-traceable author statement PubMed 17341475. Source: UniProtKB

cellular response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

homeostasis of number of cells within a tissue

Inferred from electronic annotation. Source: Ensembl

innate immune response

Non-traceable author statement PubMed 17341475. Source: UniProtKB

leukocyte chemotaxis

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of actin nucleation

Inferred from direct assay PubMed 17442961. Source: UniProtKB

phagocytosis

Inferred from mutant phenotype PubMed 17442961. Source: UniProtKB

phagolysosome assembly

Inferred from mutant phenotype PubMed 12132654. Source: UniProtKB

positive chemotaxis

Inferred from direct assay PubMed 17442961. Source: UniProtKB

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from Biological aspect of Ancestor. Source: RefGenome

uropod organization

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentactin filament

Inferred from direct assay PubMed 15800061. Source: UniProtKB

cortical actin cytoskeleton

Inferred from direct assay PubMed 15800061. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 17341475. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

immunological synapse

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from direct assay PubMed 17442961. Source: UniProtKB

phagocytic cup

Inferred from direct assay PubMed 17442961. Source: UniProtKB

phagocytic vesicle

Inferred from direct assay PubMed 17442961. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 17341475PubMed 17442961. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 11094157. Source: UniProtKB

   Molecular_functionactin filament binding

Inferred from direct assay PubMed 15601263Ref.1. Source: UniProtKB

cytoskeletal protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol 3-kinase binding

Inferred from direct assay PubMed 11094157. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 9365277. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11094157. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 15601263. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STAT3P407632EBI-1046676,EBI-518675

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 461460Coronin-1A
PRO_0000050920

Regions

Repeat13 – 6351WD 1
Repeat73 – 11038WD 2
Repeat123 – 16038WD 3
Repeat164 – 20441WD 4
Repeat207 – 25145WD 5
Repeat258 – 29639WD 6
Repeat302 – 34948WD 7
Coiled coil424 – 46037 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.8
Modified residue21Phosphoserine; by PKC Ref.16
Modified residue4121Phosphothreonine; by PKC Ref.16
Modified residue4491N6-acetyllysine Ref.13

Natural variations

Natural variant1341V → M in IMD8; the mutation causes a decrease in protein stability; patient T-cell blasts show delayed activation of signaling molecules MAPK3 and MAPK1. Ref.17
VAR_070447
Natural variant4151R → K.
Corresponds to variant rs1804109 [ dbSNP | Ensembl ].
VAR_011956
Natural variant4431T → P.
Corresponds to variant rs1053574 [ dbSNP | Ensembl ].
VAR_011957

Experimental info

Sequence conflict81S → T in AAA77058. Ref.3
Sequence conflict2451R → W in AAA77058. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P31146 [UniParc].

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

FASTA46151,026
        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 

« Hide

References

« Hide '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] [Europe PMC] [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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[8]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[9]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 355-374.
Tissue: Keratinocyte.
[10]"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] [Europe PMC] [Abstract]
Cited for: ROLE IN PHAGOSOME TRAFFICKING.
[11]"Severe combined immunodeficiency (SCID) and attention deficit hyperactivity disorder (ADHD) associated with a Coronin-1A mutation and a chromosome 16p11.2 deletion."
Shiow L.R., Paris K., Akana M.C., Cyster J.G., Sorensen R.U., Puck J.M.
Clin. Immunol. 131:24-30(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IMD8.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"GRAIL (gene related to anergy in lymphocytes) regulates cytoskeletal reorganization through ubiquitination and degradation of Arp2/3 subunit 5 and coronin 1A."
Ichikawa D., Mizuno M., Yamamura T., Miyake S.
J. Biol. Chem. 286:43465-43474(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY RNF128.
[16]"Constitutive turnover of phosphorylation at Thr-412 of human p57/coronin-1 regulates the interaction with actin."
Oku T., Nakano M., Kaneko Y., Ando Y., Kenmotsu H., Itoh S., Tsuiji M., Seyama Y., Toyoshima S., Tsuji T.
J. Biol. Chem. 287:42910-42920(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-2 AND THR-412, INTERACTION WITH ACTIN.
[17]"Whole-exome sequencing identifies Coronin-1A deficiency in 3 siblings with immunodeficiency and EBV-associated B-cell lymphoproliferation."
Moshous D., Martin E., Carpentier W., Lim A., Callebaut I., Canioni D., Hauck F., Majewski J., Schwartzentruber J., Nitschke P., Sirvent N., Frange P., Picard C., Blanche S., Revy P., Fischer A., Latour S., Jabado N., de Villartay J.P.
J. Allergy Clin. Immunol. 131:1594-1603(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IMD8 MET-134, CHARACTERIZATION OF VARIANT IMD8 MET-134.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D44497 mRNA. Translation: BAA07940.1.
X89109 mRNA. Translation: CAA61482.1.
U34690 mRNA. Translation: AAA77058.1.
AF495470 mRNA. Translation: AAM18516.1.
AK314714 mRNA. Translation: BAG37258.1.
CH471238 Genomic DNA. Translation: EAW79906.1.
BC110374 mRNA. Translation: AAI10375.1.
BC126385 mRNA. Translation: AAI26386.1.
BC126387 mRNA. Translation: AAI26388.1.
CCDSCCDS10673.1.
PIRS65665.
RefSeqNP_001180262.1. NM_001193333.2.
NP_009005.1. NM_007074.3.
UniGeneHs.415067.

3D structure databases

ProteinModelPortalP31146.
SMRP31146. Positions 9-394, 430-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116322. 16 interactions.
IntActP31146. 18 interactions.
MINTMINT-263387.
STRING9606.ENSP00000219150.

PTM databases

PhosphoSiteP31146.

Polymorphism databases

DMDM1706004.

2D gel databases

OGPP31146.
UCD-2DPAGEP31146.

Proteomic databases

MaxQBP31146.
PaxDbP31146.
PeptideAtlasP31146.
PRIDEP31146.

Protocols and materials databases

DNASU11151.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219150; ENSP00000219150; ENSG00000102879.
ENST00000570045; ENSP00000455552; ENSG00000102879.
GeneID11151.
KEGGhsa:11151.
UCSCuc002dww.3. human.

Organism-specific databases

CTD11151.
GeneCardsGC16P030194.
HGNCHGNC:2252. CORO1A.
HPACAB046473.
HPA051132.
MIM605000. gene.
615401. phenotype.
neXtProtNX_P31146.
Orphanet228003. Severe combined immunodeficiency due to CORO1A deficiency.
PharmGKBPA26768.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000166356.
HOVERGENHBG059978.
InParanoidP31146.
KOK13882.
OMAFMALICE.
PhylomeDBP31146.
TreeFamTF314280.

Enzyme and pathway databases

SignaLinkP31146.

Gene expression databases

ArrayExpressP31146.
BgeeP31146.
CleanExHS_CORO1A.
GenevestigatorP31146.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR029508. CORO1A.
IPR015505. Coronin.
IPR015048. DUF1899.
IPR015049. DUF1900.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERPTHR10856. PTHR10856. 1 hit.
PTHR10856:SF18. PTHR10856:SF18. 1 hit.
PfamPF08953. DUF1899. 1 hit.
PF08954. DUF1900. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCORO1A.
GenomeRNAi11151.
NextBio42396.
PROP31146.
SOURCESearch...

Entry information

Entry nameCOR1A_HUMAN
AccessionPrimary (citable) accession number: P31146
Secondary accession number(s): B2RBL1, Q2YD73
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

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