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Protein

Coronin-1A

Gene

Coro1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI
  • actin monomer binding Source: MGI
  • cytoskeletal protein binding Source: UniProtKB
  • identical protein binding Source: MGI
  • myosin heavy chain binding Source: MGI
  • phosphatidylinositol 3-kinase binding Source: MGI
  • poly(A) RNA binding Source: MGI
  • protein C-terminus binding Source: MGI
  • protein homodimerization activity Source: MGI

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • actin filament organization Source: MGI
  • calcium ion transport Source: MGI
  • cell migration Source: MGI
  • cell-substrate adhesion Source: MGI
  • cellular response to interleukin-4 Source: MGI
  • early endosome to recycling endosome transport Source: MGI
  • homeostasis of number of cells within a tissue Source: MGI
  • leukocyte chemotaxis Source: MGI
  • natural killer cell degranulation Source: MGI
  • negative regulation of actin nucleation Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of vesicle fusion Source: MGI
  • nerve growth factor signaling pathway Source: MGI
  • phagocytosis Source: MGI
  • phagolysosome assembly Source: MGI
  • positive chemotaxis Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of T cell activation Source: MGI
  • positive regulation of T cell proliferation Source: MGI
  • regulation of actin cytoskeleton organization Source: MGI
  • regulation of actin filament polymerization Source: MGI
  • regulation of actin polymerization or depolymerization Source: MGI
  • regulation of cell shape Source: MGI
  • regulation of release of sequestered calcium ion into cytosol Source: MGI
  • response to cytokine Source: MGI
  • T cell homeostasis Source: MGI
  • uropod organization Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:Coro1a
Synonyms:Coro1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1345961. Coro1a.

Subcellular locationi

  • Cytoplasmcytoskeleton 1 Publication
  • Cytoplasmcell cortex 1 Publication
  • Cytoplasmic vesiclephagosome membrane 1 Publication

  • 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.

GO - Cellular componenti

  • actin filament Source: MGI
  • axon Source: MGI
  • cell-cell junction Source: MGI
  • cell leading edge Source: MGI
  • cortical actin cytoskeleton Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: GOC
  • early endosome Source: MGI
  • extracellular exosome Source: MGI
  • immunological synapse Source: MGI
  • lamellipodium Source: MGI
  • membrane Source: MGI
  • phagocytic cup Source: MGI
  • phagocytic vesicle Source: MGI
  • phagocytic vesicle membrane Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 461460Coronin-1APRO_0000050921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21Phosphoserine; by PKCBy similarity
Modified residuei412 – 4121Phosphoserine; by PKC1 Publication
Modified residuei418 – 4181PhosphothreonineCombined sources
Modified residuei422 – 4221PhosphoserineCombined sources

Post-translational modificationi

phosphorylation at Ser-412 by PKC strongly down-regulates the association with actin.By similarity
Polyubiquitinated by RNF128 with 'Lys-48'-linked chains, leading to proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO89053.
PaxDbiO89053.
PRIDEiO89053.

PTM databases

iPTMnetiO89053.
PhosphoSiteiO89053.
SwissPalmiO89053.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiO89053.
CleanExiMM_CORO1A.
ExpressionAtlasiO89053. baseline and differential.
GenevisibleiO89053. MM.

Interactioni

Subunit structurei

Binds actin.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
GNASP630922EBI-6665847,EBI-1047114From a different organism.

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI
  • actin monomer binding Source: MGI
  • cytoskeletal protein binding Source: UniProtKB
  • identical protein binding Source: MGI
  • myosin heavy chain binding Source: MGI
  • phosphatidylinositol 3-kinase binding Source: MGI
  • protein C-terminus binding Source: MGI
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi198732. 2 interactions.
IntActiO89053. 3 interactions.
MINTiMINT-4091570.
STRINGi10090.ENSMUSP00000032949.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 134Combined sources
Beta strandi15 – 184Combined sources
Helixi21 – 233Combined sources
Beta strandi24 – 274Combined sources
Beta strandi39 – 424Combined sources
Beta strandi44 – 518Combined sources
Beta strandi54 – 563Combined sources
Beta strandi59 – 635Combined sources
Beta strandi84 – 896Combined sources
Beta strandi96 – 1016Combined sources
Beta strandi104 – 1107Combined sources
Beta strandi124 – 1285Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi156 – 1605Combined sources
Turni161 – 1633Combined sources
Beta strandi166 – 1705Combined sources
Turni172 – 1743Combined sources
Beta strandi179 – 1846Combined sources
Beta strandi191 – 1955Combined sources
Beta strandi198 – 2047Combined sources
Turni205 – 2084Combined sources
Beta strandi209 – 2157Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi225 – 2284Combined sources
Beta strandi233 – 2397Combined sources
Beta strandi245 – 2517Combined sources
Beta strandi259 – 2635Combined sources
Beta strandi271 – 2755Combined sources
Turni277 – 2793Combined sources
Beta strandi281 – 2866Combined sources
Beta strandi292 – 2976Combined sources
Beta strandi304 – 3107Combined sources
Beta strandi317 – 3215Combined sources
Helixi324 – 3263Combined sources
Helixi329 – 3313Combined sources
Beta strandi333 – 3419Combined sources
Beta strandi344 – 3518Combined sources
Turni361 – 3633Combined sources
Helixi376 – 3805Combined sources
Helixi432 – 46029Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AKFX-ray1.20A/B/C430-461[»]
2AQ5X-ray1.75A1-402[»]
2B4EX-ray2.30A1-402[»]
ProteinModelPortaliO89053.
SMRiO89053. Positions 9-394, 430-461.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO89053.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati13 – 6351WD 1PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati73 – 11038WD 2PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati123 – 16038WD 3PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati164 – 20441WD 4PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati207 – 25145WD 5PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati258 – 29639WD 6PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati302 – 34948WD 7PROSITE-ProRule annotation1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili424 – 461382 PublicationsAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat coronin family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0303. Eukaryota.
ENOG410XQAD. LUCA.
HOGENOMiHOG000166356.
HOVERGENiHBG059978.
InParanoidiO89053.
KOiK13882.
OMAiFMALICE.
OrthoDBiEOG7J70FB.
PhylomeDBiO89053.
TreeFamiTF314280.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR029508. CORO1A.
IPR015505. Coronin.
IPR015048. DUF1899.
IPR015049. Trimer_CC.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR10856. PTHR10856. 1 hit.
PTHR10856:SF18. PTHR10856:SF18. 1 hit.
PfamiPF08953. DUF1899. 1 hit.
PF08954. Trimer_CC. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM01166. DUF1899. 1 hit.
SM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O89053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQTTWDSGFC AVNPKFMALI
60 70 80 90 100
CEASGGGAFL VLPLGKTGRV DKNVPLVCGH TAPVLDIAWC PHNDNVIASG
110 120 130 140 150
SEDCTVMVWE IPDGGLVLPL REPVITLEGH TKRVGIVAWH PTAQNVLLSA
160 170 180 190 200
GCDNVILVWD VGTGAAVLTL GPDVHPDTIY SVDWSRDGAL ICTSCRDKRV
210 220 230 240 250
RVIEPRKGTV VAEKDRPHEG TRPVHAVFVS EGKILTTGFS RMSERQVALW
260 270 280 290 300
DTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE
310 320 330 340 350
APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERKCEPIAM
360 370 380 390 400
TVPRKSDLFQ EDLYPPTAGP DPALTAEEWL GGRDAGPLLI SLKDGYVPPK
410 420 430 440 450
SRELRVNRGL DSARRRATPE PSGTPSSDTV SRLEEDVRNL NAIVQKLQER
460
LDRLEETVQA K
Length:461
Mass (Da):50,989
Last modified:January 23, 2007 - v5
Checksum:i9098F53757C5318D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251I → V in AAD32703 (PubMed:9778037).Curated
Sequence conflicti125 – 1251I → V in AAH02136 (PubMed:15489334).Curated
Sequence conflicti299 – 2991S → F in AAH53398 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF143955 mRNA. Translation: AAD32703.1.
AF047388 mRNA. Translation: AAD31082.1.
AF495468 mRNA. Translation: AAM18514.1.
BC002136 mRNA. Translation: AAH02136.1.
BC053398 mRNA. Translation: AAH53398.1.
U89399 mRNA. Translation: AAC36506.1.
CCDSiCCDS21840.1.
RefSeqiNP_001288303.1. NM_001301374.1.
NP_034028.1. NM_009898.3.
XP_006507347.1. XM_006507284.2.
XP_006507348.1. XM_006507285.2.
UniGeneiMm.290482.

Genome annotation databases

EnsembliENSMUST00000032949; ENSMUSP00000032949; ENSMUSG00000030707.
ENSMUST00000106364; ENSMUSP00000101972; ENSMUSG00000030707.
GeneIDi12721.
KEGGimmu:12721.
UCSCiuc009jsk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF143955 mRNA. Translation: AAD32703.1.
AF047388 mRNA. Translation: AAD31082.1.
AF495468 mRNA. Translation: AAM18514.1.
BC002136 mRNA. Translation: AAH02136.1.
BC053398 mRNA. Translation: AAH53398.1.
U89399 mRNA. Translation: AAC36506.1.
CCDSiCCDS21840.1.
RefSeqiNP_001288303.1. NM_001301374.1.
NP_034028.1. NM_009898.3.
XP_006507347.1. XM_006507284.2.
XP_006507348.1. XM_006507285.2.
UniGeneiMm.290482.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AKFX-ray1.20A/B/C430-461[»]
2AQ5X-ray1.75A1-402[»]
2B4EX-ray2.30A1-402[»]
ProteinModelPortaliO89053.
SMRiO89053. Positions 9-394, 430-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198732. 2 interactions.
IntActiO89053. 3 interactions.
MINTiMINT-4091570.
STRINGi10090.ENSMUSP00000032949.

PTM databases

iPTMnetiO89053.
PhosphoSiteiO89053.
SwissPalmiO89053.

Proteomic databases

EPDiO89053.
PaxDbiO89053.
PRIDEiO89053.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032949; ENSMUSP00000032949; ENSMUSG00000030707.
ENSMUST00000106364; ENSMUSP00000101972; ENSMUSG00000030707.
GeneIDi12721.
KEGGimmu:12721.
UCSCiuc009jsk.2. mouse.

Organism-specific databases

CTDi11151.
MGIiMGI:1345961. Coro1a.

Phylogenomic databases

eggNOGiKOG0303. Eukaryota.
ENOG410XQAD. LUCA.
HOGENOMiHOG000166356.
HOVERGENiHBG059978.
InParanoidiO89053.
KOiK13882.
OMAiFMALICE.
OrthoDBiEOG7J70FB.
PhylomeDBiO89053.
TreeFamiTF314280.

Miscellaneous databases

ChiTaRSiCoro1a. mouse.
EvolutionaryTraceiO89053.
PROiO89053.
SOURCEiSearch...

Gene expression databases

BgeeiO89053.
CleanExiMM_CORO1A.
ExpressionAtlasiO89053. baseline and differential.
GenevisibleiO89053. MM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR029508. CORO1A.
IPR015505. Coronin.
IPR015048. DUF1899.
IPR015049. Trimer_CC.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR10856. PTHR10856. 1 hit.
PTHR10856:SF18. PTHR10856:SF18. 1 hit.
PfamiPF08953. DUF1899. 1 hit.
PF08954. Trimer_CC. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM01166. DUF1899. 1 hit.
SM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Definition of family of coronin-related proteins conserved between humans and mice: close genetic linkage between coronin-2 and CD45-associated protein."
    Okumura M., Kung C., Wong S., Rodgers M., Thomas M.L.
    DNA Cell Biol. 17:779-787(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-14, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ROLE IN PHAGOSOME TRAFFICKING.
    Strain: C57BL/6J.
    Tissue: Macrophage.
  3. "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].
  4. "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: Hematopoietic and Mammary tumor.
  5. "Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
    Chu C.C., Paul W.E.
    Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 156-276.
    Strain: BALB/cJ.
    Tissue: Spleen.
  6. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 215-233, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418 AND SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Liver, Lung, Spleen and Testis.
  9. "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-412.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 430-461, COILED-COIL DOMAIN.
  11. "The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes."
    Appleton B.A., Wu P., Wiesmann C.
    Structure 14:87-96(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-402, WD REPEATS, COILED-COIL DOMAIN.

Entry informationi

Entry nameiCOR1A_MOUSE
AccessioniPrimary (citable) accession number: O89053
Secondary accession number(s): Q7TMU0, Q9R1Y8, Q9R288
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 148 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.