Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Coactosin-like protein

Gene

Cotl1

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

Functioni

Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis (By similarity).By similarity1 Publication

GO - Molecular functioni

  • actin binding Source: MGI
  • enzyme binding Source: UniProtKB

GO - Biological processi

  • defense response to fungus Source: UniProtKB

Keywordsi

Molecular functionActin-binding, Chaperone

Enzyme and pathway databases

ReactomeiR-MMU-6798695 Neutrophil degranulation

Names & Taxonomyi

Protein namesi
Recommended name:
Coactosin-like protein
Gene namesi
Name:Cotl1
Synonyms:Clp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1919292 Cotl1

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, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002149552 – 142Coactosin-like proteinAdd BLAST141

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei102N6-acetyllysineBy similarity1
Modified residuei141PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CQI6
MaxQBiQ9CQI6
PaxDbiQ9CQI6
PRIDEiQ9CQI6
TopDownProteomicsiQ9CQI6

2D gel databases

UCD-2DPAGEQ9CQI6

PTM databases

iPTMnetiQ9CQI6
PhosphoSitePlusiQ9CQI6
SwissPalmiQ9CQI6

Expressioni

Gene expression databases

BgeeiENSMUSG00000031827
CleanExiMM_COTL1
ExpressionAtlasiQ9CQI6 baseline and differential
GenevisibleiQ9CQI6 MM

Interactioni

Subunit structurei

Interacts with 5-lipoxygenase (ALOX5/5LO) in a calcium-independent manner. Binds to F-actin with a stoichiometry of 1:2 (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: MGI
  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi215111, 4 interactors
IntActiQ9CQI6, 1 interactor
STRINGi10090.ENSMUSP00000034285

Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 18Combined sources12
Beta strandi19 – 22Combined sources4
Beta strandi25 – 43Combined sources19
Helixi45 – 49Combined sources5
Beta strandi57 – 62Combined sources6
Turni70 – 73Combined sources4
Beta strandi77 – 82Combined sources6
Beta strandi84 – 86Combined sources3
Helixi88 – 94Combined sources7
Turni95 – 97Combined sources3
Helixi98 – 104Combined sources7
Beta strandi111 – 114Combined sources4
Helixi117 – 120Combined sources4
Helixi122 – 131Combined sources10
Helixi136 – 139Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UDMNMR-A1-142[»]
1WM4NMR-A1-142[»]
ProteinModelPortaliQ9CQI6
SMRiQ9CQI6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CQI6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 130ADF-HPROSITE-ProRule annotationAdd BLAST129

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni66 – 75Flexible and important for F-actin bindingBy similarity10

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410INZZ Eukaryota
ENOG41120RS LUCA
GeneTreeiENSGT00390000012498
HOGENOMiHOG000007758
HOVERGENiHBG051082
InParanoidiQ9CQI6
OMAiFILVVWI
OrthoDBiEOG091G0RGQ
PhylomeDBiQ9CQI6
TreeFamiTF324318

Family and domain databases

Gene3Di3.40.20.10, 1 hit
InterProiView protein in InterPro
IPR002108 ADF-H
IPR029006 ADF-H/Gelsolin-like_dom_sf
IPR030502 CLP
PANTHERiPTHR10829:SF2 PTHR10829:SF2, 1 hit
PfamiView protein in Pfam
PF00241 Cofilin_ADF, 1 hit
SMARTiView protein in SMART
SM00102 ADF, 1 hit
PROSITEiView protein in PROSITE
PS51263 ADF_H, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q9CQI6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKIDKEAC RAAYNLVRDD GSAVIWVTFR YDGATIVPGD QGADYQHFIQ
60 70 80 90 100
QCTDDVRLFA FVRFTTGDAM SKRSKFALIT WIGEDVSGLQ RAKTGTDKTL
110 120 130 140
VKEVVQNFAK EFVISDRKEL EEDFIRSELK KAGGANYDAQ SE
Length:142
Mass (Da):15,944
Last modified:January 23, 2007 - v3
Checksum:i88CB1BF12447ABC8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010052 mRNA Translation: BAB26668.1
AK007994 mRNA Translation: BAB25396.1
AK008085 mRNA Translation: BAB25450.1
BC011068 mRNA Translation: AAH11068.1
BC010249 mRNA Translation: AAH10249.1
CCDSiCCDS22712.1
RefSeqiNP_082347.1, NM_028071.3
UniGeneiMm.393405

Genome annotation databases

EnsembliENSMUST00000034285; ENSMUSP00000034285; ENSMUSG00000031827
ENSMUST00000168698; ENSMUSP00000126329; ENSMUSG00000031827
GeneIDi72042
KEGGimmu:72042
UCSCiuc012glt.1 mouse

Similar proteinsi

Entry informationi

Entry nameiCOTL1_MOUSE
AccessioniPrimary (citable) accession number: Q9CQI6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 137 of the entry and version 3 of the sequence. See 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health