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Protein

Coronin-1B

Gene

Coro1b

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

Functioni

Regulates leading edge dynamics and cell motility in fibroblasts. May be involved in cytokinesis and signal transduction (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Coronin-1B
Alternative name(s):
Coronin-2
Gene namesi
Name:Coro1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1345963 Coro1b

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000509231 – 484Coronin-1BAdd BLAST484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation on Ser-2 regulates the interaction with the Arp2/3 complex and cell motility in fibroblasts. Phosphorylation does not seem to affect subcellular location (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9WUM3
MaxQBiQ9WUM3
PaxDbiQ9WUM3
PRIDEiQ9WUM3

PTM databases

iPTMnetiQ9WUM3
PhosphoSitePlusiQ9WUM3

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSMUSG00000024835
CleanExiMM_CORO1B
ExpressionAtlasiQ9WUM3 baseline and differential
GenevisibleiQ9WUM3 MM

Interactioni

Subunit structurei

Forms homooligomers, but does not form complexes with the other coronins. Interacts with Arp2/3 complex components, including ACTR2, ARPC1B and ARPC2. Binds actin (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204713, 2 interactors
IntActiQ9WUM3, 3 interactors
MINTiQ9WUM3
STRINGi10090.ENSMUSP00000008893

Structurei

3D structure databases

ProteinModelPortaliQ9WUM3
SMRiQ9WUM3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati80 – 120WD 1Add BLAST41
Repeati130 – 170WD 2Add BLAST41
Repeati174 – 213WD 3Add BLAST40
Repeati217 – 260WD 4Add BLAST44
Repeati265 – 305WD 5Add BLAST41

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili444 – 482Sequence analysisAdd BLAST39

Sequence similaritiesi

Belongs to the WD repeat coronin family.Curated

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0303 Eukaryota
ENOG410XQAD LUCA
GeneTreeiENSGT00760000119195
HOGENOMiHOG000166356
HOVERGENiHBG059978
InParanoidiQ9WUM3
KOiK13886
OMAiLKNGYVP
OrthoDBiEOG091G03H5
PhylomeDBiQ9WUM3
TreeFamiTF314280

Family and domain databases

Gene3Di2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR027340 Coro1b
IPR015505 Coronin
IPR015048 DUF1899
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
PANTHERiPTHR10856 PTHR10856, 1 hit
PTHR10856:SF24 PTHR10856:SF24, 1 hit
PfamiView protein in Pfam
PF08953 DUF1899, 1 hit
PF00400 WD40, 3 hits
SMARTiView protein in SMART
SM01166 DUF1899, 1 hit
SM00320 WD40, 3 hits
SUPFAMiSSF50978 SSF50978, 1 hit
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 1 hit
PS50082 WD_REPEATS_2, 2 hits
PS50294 WD_REPEATS_REGION, 1 hit

Sequencei

Sequence statusi: Complete.

Q9WUM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV
60 70 80 90 100
IVEASGGGAF MVLPLNKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS
110 120 130 140 150
GSEDCTVMVW QIPENGLTSP LTEPVVVLEG HTKRVGIITW HPTARNVLLS
160 170 180 190 200
AGCDNVVLIW NVGTAEELYR LDSLHPDLIY NVSWNHNGSL FCSACKDKSV
210 220 230 240 250
RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS RMSERQLALW
260 270 280 290 300
DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITDE
310 320 330 340 350
PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM
360 370 380 390 400
TVPRKSDLFQ DDLYPDTAGP EAALEAEDWV SGQDANPILI SLREAYVPSK
410 420 430 440 450
QRDLKVSRRN VLSDSRPASY SRSGASTATA VTDVPSGNLA GAGEAGKLEE
460 470 480
VMQELRALRM LVKEQGERIS RLEEQLGRME NGDT
Length:484
Mass (Da):53,912
Last modified:November 1, 1999 - v1
Checksum:i9631CC02E7EAC72F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti393R → G in BAB25985 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF143956 mRNA Translation: AAD32704.1
AK008947 mRNA Translation: BAB25985.1
AK149639 mRNA Translation: BAE29000.1
CCDSiCCDS29418.1
RefSeqiNP_035908.1, NM_011778.2
XP_006531804.1, XM_006531741.2
XP_006531805.1, XM_006531742.1
UniGeneiMm.276859

Genome annotation databases

EnsembliENSMUST00000008893; ENSMUSP00000008893; ENSMUSG00000024835
ENSMUST00000181494; ENSMUSP00000137780; ENSMUSG00000097771
GeneIDi23789
KEGGimmu:23789
UCSCiuc008fyy.1 mouse

Similar proteinsi

Entry informationi

Entry nameiCOR1B_MOUSE
AccessioniPrimary (citable) accession number: Q9WUM3
Secondary accession number(s): Q3UEB1, Q9CVA2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: March 28, 2018
This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health