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Protein

Coactosin-like protein

Gene

COTL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.2 Publications

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. enzyme binding Source: UniProtKB

GO - Biological processi

  1. defense response to fungus Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Coactosin-like protein
Gene namesi
Name:COTL1
Synonyms:CLP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:18304. COTL1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProtKB
  4. nuclear membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi75 – 751K → A: Abolishes actin-binding activity. 1 Publication
Mutagenesisi130 – 1301K → A: No effect on 5LO-binding activity. 1 Publication
Mutagenesisi131 – 1311K → A: Abolishes 5LO-binding activity. 1 Publication
Mutagenesisi131 – 1311K → E: Abolishes 5LO-binding activity. 1 Publication
Mutagenesisi131 – 1311K → R: No effect on 5LO-binding activity. 1 Publication

Organism-specific databases

PharmGKBiPA38522.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 142141Coactosin-like proteinPRO_0000214954Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei102 – 1021N6-acetyllysine1 Publication
Modified residuei126 – 1261N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ14019.
PaxDbiQ14019.
PeptideAtlasiQ14019.
PRIDEiQ14019.

2D gel databases

OGPiQ14019.
REPRODUCTION-2DPAGEIPI00017704.

PTM databases

PhosphoSiteiQ14019.

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

BgeeiQ14019.
CleanExiHS_COTL1.
ExpressionAtlasiQ14019. baseline and differential.
GenevestigatoriQ14019.

Organism-specific databases

HPAiHPA008918.

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

WithEntry#Exp.IntActNotes
ALOX5P099174EBI-79926,EBI-79934

Protein-protein interaction databases

BioGridi116979. 9 interactions.
IntActiQ14019. 1 interaction.
STRINGi9606.ENSP00000262428.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1812Combined sources
Beta strandi20 – 234Combined sources
Beta strandi26 – 327Combined sources
Beta strandi35 – 4410Combined sources
Helixi45 – 517Combined sources
Beta strandi54 – 563Combined sources
Beta strandi57 – 6610Combined sources
Helixi69 – 713Combined sources
Beta strandi73 – 8210Combined sources
Beta strandi84 – 863Combined sources
Helixi88 – 10114Combined sources
Turni102 – 1043Combined sources
Beta strandi109 – 1146Combined sources
Helixi117 – 1204Combined sources
Helixi122 – 13110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T2LX-ray2.80A/B2-142[»]
1T3XX-ray2.00A2-142[»]
1T3YX-ray1.15A2-142[»]
1TMWNMR-A2-142[»]
1VFQX-ray1.90A1-142[»]
1WNJNMR-A1-142[»]
ProteinModelPortaliQ14019.
SMRiQ14019. Positions 1-131.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14019.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 130129ADF-HPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 7510Flexible and important for F-actin binding

Sequence similaritiesi

Contains 1 ADF-H domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG253317.
GeneTreeiENSGT00390000012498.
HOGENOMiHOG000007758.
HOVERGENiHBG051082.
InParanoidiQ14019.
OMAiFTLITWI.
OrthoDBiEOG7R56V4.
PhylomeDBiQ14019.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381P → H in AAH42970 (PubMed:15489334).Curated

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.3. human.

Polymorphism databases

DMDMi21759076.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T2LX-ray2.80A/B2-142[»]
1T3XX-ray2.00A2-142[»]
1T3YX-ray1.15A2-142[»]
1TMWNMR-A2-142[»]
1VFQX-ray1.90A1-142[»]
1WNJNMR-A1-142[»]
ProteinModelPortaliQ14019.
SMRiQ14019. Positions 1-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116979. 9 interactions.
IntActiQ14019. 1 interaction.
STRINGi9606.ENSP00000262428.

PTM databases

PhosphoSiteiQ14019.

Polymorphism databases

DMDMi21759076.

2D gel databases

OGPiQ14019.
REPRODUCTION-2DPAGEIPI00017704.

Proteomic databases

MaxQBiQ14019.
PaxDbiQ14019.
PeptideAtlasiQ14019.
PRIDEiQ14019.

Protocols and materials databases

DNASUi23406.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262428; ENSP00000262428; ENSG00000103187.
GeneIDi23406.
KEGGihsa:23406.
UCSCiuc002fid.3. human.

Organism-specific databases

CTDi23406.
GeneCardsiGC16M084599.
H-InvDBHIX0134273.
HGNCiHGNC:18304. COTL1.
HPAiHPA008918.
MIMi606748. gene.
neXtProtiNX_Q14019.
PharmGKBiPA38522.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG253317.
GeneTreeiENSGT00390000012498.
HOGENOMiHOG000007758.
HOVERGENiHBG051082.
InParanoidiQ14019.
OMAiFTLITWI.
OrthoDBiEOG7R56V4.
PhylomeDBiQ14019.
TreeFamiTF324318.

Miscellaneous databases

ChiTaRSiCOTL1. human.
EvolutionaryTraceiQ14019.
GeneWikiiCOTL1.
GenomeRNAii23406.
NextBioi45583.
PROiQ14019.
SOURCEiSearch...

Gene expression databases

BgeeiQ14019.
CleanExiHS_COTL1.
ExpressionAtlasiQ14019. baseline and differential.
GenevestigatoriQ14019.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Homologous recombination of a flanking repeat gene cluster is a mechanism for a common contiguous gene deletion syndrome."
    Chen K.-S., Manian P., Koeuth T., Potocki L., Zhao Q., Chinault A.C., Lee C.-C., Lupski J.R.
    Nat. Genet. 17:154-163(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain, Cervix, Kidney, Lung and Uterus.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Tissue: Platelet.
  7. Lubec G., Afjehi-Sadat L.
    Submitted (FEB-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 76-91, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  8. "Coactosin-like protein, a human F-actin-binding protein: critical role of lysine-75."
    Provost P., Doucet J., Stock A., Gerisch G., Samuelsson B., Radmark O.
    Biochem. J. 359:255-263(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-75.
  9. Cited for: INTERACTION WITH 5-LIPOXYGENASE, MUTAGENESIS OF LYS-130 AND LYS-131.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Coactosin-like protein functions as a stabilizing chaperone for 5-lipoxygenase: role of tryptophan 102."
    Esser J., Rakonjac M., Hofmann B., Fischer L., Provost P., Schneider G., Steinhilber D., Samuelsson B., Radmark O.
    Biochem. J. 425:265-274(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. Cited for: STRUCTURE BY NMR.
  15. "Crystal structure of human coactosin-like protein at 1.9 A resolution."
    Li X., Liu X., Lou Z., Duan X., Wu H., Liu Y., Rao Z.
    Protein Sci. 13:2845-2851(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.
  16. "Binding model of human coactosin-like protein with filament actin revealed by mutagenesis."
    Dai H., Huang W., Xu J., Yao B., Xiong S., Ding H., Tang Y., Liu H., Wu J., Shi Y.
    Biochim. Biophys. Acta 1764:1688-1700(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBUNIT, F-ACTIN BINDING REGION.

Entry informationi

Entry nameiCOTL1_HUMAN
AccessioniPrimary (citable) accession number: Q14019
Secondary accession number(s): B2RDU3, D3DUL9, Q86XM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 132 of the entry and version 3 of the sequence. [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

External Data

Dasty 3

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 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.