P31146 (COR1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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

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 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 7 WD repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat WD repeat
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell-substrate adhesion Inferred from mutant phenotype. Source: UniProtKB innate immune response Non-traceable author statement. Source: UniProtKB leukocyte chemotaxis Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of actin nucleation Inferred from direct assay. Source: UniProtKB phagolysosome assembly Inferred from mutant phenotype. Source: UniProtKB positive chemotaxis Inferred from direct assay. Source: UniProtKB regulation of cell shape Inferred from Biological aspect of Ancestor. Source: RefGenome uropod organization Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	actin filament Inferred from direct assay. Source: UniProtKB cortical actin cytoskeleton 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 Inferred from direct assay Ref.1. Source: UniProtKB phosphatidylinositol 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STAT3	P40763	2	EBI-1046676,EBI-518675

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 461	460	Coronin-1A		PRO_0000050920
Regions
	Repeat	13 – 63	51	WD 1
	Repeat	73 – 110	38	WD 2
	Repeat	123 – 160	38	WD 3
	Repeat	164 – 204	41	WD 4
	Repeat	207 – 251	45	WD 5
	Repeat	258 – 296	39	WD 6
	Repeat	302 – 349	48	WD 7
	Coiled coil	424 – 460	37	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.8
	Modified residue	356	1	Phosphoserine Ref.11
	Modified residue	449	1	N6-acetyllysine Ref.12
Natural variations
	Natural variant	415	1	R → K. Corresponds to variant rs1804109 [ dbSNP | Ensembl ].		VAR_011956
	Natural variant	443	1	T → P. Corresponds to variant rs1053574 [ dbSNP | Ensembl ].		VAR_011957
Experimental info
	Sequence conflict	8	1	S → T in AAA77058. Ref.3
	Sequence conflict	245	1	R → W in AAA77058. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P31146 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: DE3FEDA57041515E	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

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]	"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. , 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: 14702039] [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. , 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: 15489334] [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, 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: 1286667] [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: 10338208] [Abstract] Cited for: ROLE IN PHAGOSOME TRAFFICKING.
[11]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, MASS SPECTROMETRY.
[13]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	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.
IPI	IPI00010133.
PIR	S65665.
RefSeq	NP_001180262.1. NM_001193333.2. NP_009005.1. NM_007074.3.
UniGene	Hs.415067.
3D structure databases
ProteinModelPortal	P31146.
SMR	P31146. Positions 9-394, 430-461.
ModBase	Search...
Protein-protein interaction databases
IntAct	P31146. 18 interactions.
STRING	P31146.
PTM databases
PhosphoSite	P31146.
Polymorphism databases
DMDM	1706004.
2D gel databases
Aarhus/Ghent-2DPAGE	2416. IEF.
OGP	P31146.
UCD-2DPAGE	P31146.
Proteomic databases
PeptideAtlas	P31146.
PRIDE	P31146.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000219150; ENSP00000219150; ENSG00000102879.
GeneID	11151.
KEGG	hsa:11151.
UCSC	uc002dww.1. human.
Organism-specific databases
CTD	11151.
GeneCards	GC16P030194.
H-InvDB	HIX0012929.
HGNC	HGNC:2252. CORO1A.
MIM	605000. gene.
neXtProt	NX_P31146.
Orphanet	228003. Severe combined immunodeficiency due to CORO1A deficiency.
PharmGKB	PA26768.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11534.
GeneTree	ENSGT00550000074317.
HOGENOM	HBG735393.
HOVERGEN	HBG059978.
InParanoid	P31146.
OMA	VPTVCGH.
OrthoDB	EOG4RNB8C.
PhylomeDB	P31146.
Gene expression databases
ArrayExpress	P31146.
Bgee	P31146.
CleanEx	HS_CORO1A.
Genevestigator	P31146.
GermOnline	ENSG00000102879. Homo sapiens.
Family and domain databases
InterPro	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]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KO	K13882.
PANTHER	PTHR10856. Coronin. 1 hit.
Pfam	PF08953. DUF1899. 1 hit. PF08954. DUF1900. 1 hit. PF00400. WD40. 3 hits. [Graphical view]
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
NextBio	42396.
SOURCE	Search...

Entry information

Entry name

COR1A_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 115 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.