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Protein

Coactosin-like protein

Gene

COTL1

Organism
Homo sapiens (Human)
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.2 Publications

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionActin-binding, Chaperone

Enzyme and pathway databases

ReactomeiR-HSA-6798695 Neutrophil degranulation

Names & Taxonomyi

Protein namesi
Recommended name:
Coactosin-like protein
Gene namesi
Name:COTL1
Synonyms:CLP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000103187.7
HGNCiHGNC:18304 COTL1
MIMi606748 gene
neXtProtiNX_Q14019

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi75K → A: Abolishes actin-binding activity. 1 Publication1
Mutagenesisi130K → A: No effect on 5LO-binding activity. 1 Publication1
Mutagenesisi131K → A: Abolishes 5LO-binding activity. 1 Publication1
Mutagenesisi131K → E: Abolishes 5LO-binding activity. 1 Publication1
Mutagenesisi131K → R: No effect on 5LO-binding activity. 1 Publication1

Organism-specific databases

DisGeNETi23406
OpenTargetsiENSG00000103187
PharmGKBiPA38522

Polymorphism and mutation databases

DMDMi21759076

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002149542 – 142Coactosin-like proteinAdd BLAST141

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei102N6-acetyllysineCombined sources1
Modified residuei126N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ14019
MaxQBiQ14019
PaxDbiQ14019
PeptideAtlasiQ14019
PRIDEiQ14019
ProteomicsDBi59796
TopDownProteomicsiQ14019

2D gel databases

OGPiQ14019
REPRODUCTION-2DPAGEiIPI00017704

PTM databases

iPTMnetiQ14019
PhosphoSitePlusiQ14019
SwissPalmiQ14019

Expressioni

Tissue specificityi

Widely expressed with highest levels in placenta, lung, kidney and peripheral blood leukocytes and lower levels in brain, liver and pancreas.1 Publication

Gene expression databases

BgeeiENSG00000103187
CleanExiHS_COTL1
ExpressionAtlasiQ14019 baseline and differential
GenevisibleiQ14019 HS

Organism-specific databases

HPAiCAB062328
HPA008918

Interactioni

Subunit structurei

Interacts with 5-lipoxygenase (ALOX5/5LO) in a calcium-independent manner. Binds to F-actin with a stoichiometry of 1:2.4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi116979, 24 interactors
DIPiDIP-30951N
IntActiQ14019, 7 interactors
STRINGi9606.ENSP00000262428

Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 18Combined sources12
Beta strandi20 – 23Combined sources4
Beta strandi26 – 32Combined sources7
Beta strandi35 – 44Combined sources10
Helixi45 – 51Combined sources7
Beta strandi54 – 56Combined sources3
Beta strandi57 – 66Combined sources10
Helixi69 – 71Combined sources3
Beta strandi73 – 82Combined sources10
Beta strandi84 – 86Combined sources3
Helixi88 – 101Combined sources14
Turni102 – 104Combined sources3
Beta strandi109 – 114Combined sources6
Helixi117 – 120Combined sources4
Helixi122 – 131Combined sources10

3D structure databases

ProteinModelPortaliQ14019
SMRiQ14019
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14019

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 binding10

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410INZZ Eukaryota
ENOG41120RS LUCA
GeneTreeiENSGT00390000012498
HOGENOMiHOG000007758
HOVERGENiHBG051082
InParanoidiQ14019
OMAiFILVVWI
OrthoDBiEOG091G0RGQ
PhylomeDBiQ14019
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.

Q14019-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKIDKEAC RAAYNLVRDD GSAVIWVTFK YDGSTIVPGE QGAEYQHFIQ
60 70 80 90 100
QCTDDVRLFA FVRFTTGDAM SKRSKFALIT WIGENVSGLQ RAKTGTDKTL
110 120 130 140
VKEVVQNFAK EFVISDRKEL EEDFIKSELK KAGGANYDAQ TE
Length:142
Mass (Da):15,945
Last modified:January 23, 2007 - v3
Checksum:iA4B881DD8E89A35D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38P → H in AAH42970 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L54057 mRNA Translation: AAA88022.1
BT006968 mRNA Translation: AAP35614.1
AK315675 mRNA Translation: BAG38040.1
CH471114 Genomic DNA Translation: EAW95476.1
CH471114 Genomic DNA Translation: EAW95477.1
BC010039 mRNA Translation: AAH10039.1
BC010884 mRNA Translation: AAH10884.1
BC016702 mRNA Translation: AAH16702.1
BC042970 mRNA Translation: AAH42970.1
BC053682 mRNA Translation: AAH53682.1
CCDSiCCDS10947.1
RefSeqiNP_066972.1, NM_021149.3
UniGeneiHs.289092

Genome annotation databases

EnsembliENST00000262428; ENSP00000262428; ENSG00000103187
GeneIDi23406
KEGGihsa:23406
UCSCiuc002fid.5 human

Similar proteinsi

Entry informationi

Entry nameiCOTL1_HUMAN
AccessioniPrimary (citable) accession number: Q14019
Secondary accession number(s): B2RDU3, D3DUL9, Q86XM5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 161 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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