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: Annotation score: 4 out of 5-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
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Actin-binding

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1919292. Cotl1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcytoskeleton By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

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.

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.
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

Contains 1 ADF-H domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410INZZ. Eukaryota.
ENOG41120RS. LUCA.
GeneTreeiENSGT00390000012498.
HOGENOMiHOG000007758.
HOVERGENiHBG051082.
InParanoidiQ9CQI6.
OMAiFTLITWI.
OrthoDBiEOG091G0RGQ.
PhylomeDBiQ9CQI6.
TreeFamiTF324318.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
[Graphical view]
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi215111. 4 interactors.
STRINGi10090.ENSMUSP00000034285.

PTM databases

iPTMnetiQ9CQI6.
PhosphoSitePlusiQ9CQI6.

2D gel databases

UCD-2DPAGEQ9CQI6.

Proteomic databases

EPDiQ9CQI6.
MaxQBiQ9CQI6.
PaxDbiQ9CQI6.
PRIDEiQ9CQI6.
TopDownProteomicsiQ9CQI6.

Protocols and materials databases

DNASUi72042.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23406.
MGIiMGI:1919292. Cotl1.

Phylogenomic databases

eggNOGiENOG410INZZ. Eukaryota.
ENOG41120RS. LUCA.
GeneTreeiENSGT00390000012498.
HOGENOMiHOG000007758.
HOVERGENiHBG051082.
InParanoidiQ9CQI6.
OMAiFTLITWI.
OrthoDBiEOG091G0RGQ.
PhylomeDBiQ9CQI6.
TreeFamiTF324318.

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiQ9CQI6.
PROiQ9CQI6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031827.
CleanExiMM_COTL1.
ExpressionAtlasiQ9CQI6. baseline and differential.
GenevisibleiQ9CQI6. MM.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
[Graphical view]
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOTL1_MOUSE
AccessioniPrimary (citable) accession number: Q9CQI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 128 of the entry and version 3 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.