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Q14019 (COTL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coactosin-like protein
Gene names
Name:COTL1
Synonyms:CLP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.11

Subunit structure

Interacts with 5-lipoxygenase (ALOX5/5LO) in a calcium-independent manner. Binds to F-actin with a stoichiometry of 1:2. Ref.9 Ref.11 Ref.15 Ref.16

Subcellular location

Cytoplasmcytoskeleton By similarity. Nucleus membrane; Peripheral membrane protein Ref.8 Ref.11.

Tissue specificity

Widely expressed with highest levels in placenta, lung, kidney and peripheral blood leukocytes and lower levels in brain, liver and pancreas. Ref.8

Sequence similarities

Belongs to the actin-binding proteins ADF family. Coactosin subfamily.

Contains 1 ADF-H domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ALOX5P099174EBI-79926,EBI-79934

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.13
Chain2 – 142141Coactosin-like protein
PRO_0000214954

Regions

Domain2 – 130129ADF-H
Region66 – 7510Flexible and important for F-actin binding

Amino acid modifications

Modified residue21N-acetylalanine Ref.13
Modified residue1021N6-acetyllysine Ref.10
Modified residue1261N6-acetyllysine Ref.10

Experimental info

Mutagenesis751K → A: Abolishes actin-binding activity. Ref.8
Mutagenesis1301K → A: No effect on 5LO-binding activity. Ref.9
Mutagenesis1311K → A: Abolishes 5LO-binding activity. Ref.9
Mutagenesis1311K → E: Abolishes 5LO-binding activity. Ref.9
Mutagenesis1311K → R: No effect on 5LO-binding activity. Ref.9
Sequence conflict381P → H in AAH42970. Ref.5

Secondary structure

............................ 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14019 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A4B881DD8E89A35D

FASTA14215,945
        10         20         30         40         50         60 
MATKIDKEAC RAAYNLVRDD GSAVIWVTFK YDGSTIVPGE QGAEYQHFIQ QCTDDVRLFA 

        70         80         90        100        110        120 
FVRFTTGDAM SKRSKFALIT WIGENVSGLQ RAKTGTDKTL VKEVVQNFAK EFVISDRKEL 

       130        140 
EEDFIKSELK KAGGANYDAQ TE 

« Hide

References

« Hide 'large scale' references
[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(1997) [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 (MAY-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. expand/collapse author list , 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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Tissue: Platelet.
[7]Lubec G., Afjehi-Sadat L.
Submitted (MAR-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(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-75.
[9]"5-lipoxygenase interacts with coactosin-like protein."
Provost P., Doucet J., Hammarberg T., Gerisch G., Samuelsson B., Radmark O.
J. Biol. Chem. 276:16520-16527(2001) [PubMed] [Europe PMC] [Abstract]
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(2009) [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(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"NMR structure of human coactosin-like protein."
Liepinsh E., Rakonjac M., Boissonneault V., Provost P., Samuelsson B., Radmark O., Otting G.
J. Biomol. NMR 30:353-356(2004) [PubMed] [Europe PMC] [Abstract]
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(2004) [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(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, SUBUNIT, F-ACTIN BINDING REGION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10947.1.
RefSeqNP_066972.1. NM_021149.3.
UniGeneHs.289092.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ14019.
SMRQ14019. Positions 1-131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116979. 8 interactions.
IntActQ14019. 1 interaction.
STRING9606.ENSP00000262428.

PTM databases

PhosphoSiteQ14019.

Polymorphism databases

DMDM21759076.

2D gel databases

OGPQ14019.
REPRODUCTION-2DPAGEIPI00017704.

Proteomic databases

MaxQBQ14019.
PaxDbQ14019.
PeptideAtlasQ14019.
PRIDEQ14019.

Protocols and materials databases

DNASU23406.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262428; ENSP00000262428; ENSG00000103187.
GeneID23406.
KEGGhsa:23406.
UCSCuc002fid.3. human.

Organism-specific databases

CTD23406.
GeneCardsGC16M084599.
H-InvDBHIX0134273.
HGNCHGNC:18304. COTL1.
HPAHPA008918.
MIM606748. gene.
neXtProtNX_Q14019.
PharmGKBPA38522.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253317.
HOGENOMHOG000007758.
HOVERGENHBG051082.
InParanoidQ14019.
OMAEYANDKE.
OrthoDBEOG7R56V4.
PhylomeDBQ14019.
TreeFamTF324318.

Gene expression databases

ArrayExpressQ14019.
BgeeQ14019.
CleanExHS_COTL1.
GenevestigatorQ14019.

Family and domain databases

Gene3D3.40.20.10. 1 hit.
InterProIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
[Graphical view]
PfamPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
SMARTSM00102. ADF. 1 hit.
[Graphical view]
PROSITEPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOTL1. human.
EvolutionaryTraceQ14019.
GeneWikiCOTL1.
GenomeRNAi23406.
NextBio45583.
PROQ14019.
SOURCESearch...

Entry information

Entry nameCOTL1_HUMAN
AccessionPrimary (citable) accession number: Q14019
Secondary accession number(s): B2RDU3, D3DUL9, Q86XM5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM