Coactosin-like protein - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q14019 (COTL1_HUMAN)

Last modified July 7, 2009. Version 84. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Coactosin-like protein

Gene names

Name:	COTL1
Synonyms:	CLP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Ref.6
Subunit structure	Interacts with 5-lipoxygenase (5LO) in a calcium-independent manner. Ref.7
Subcellular location	Cytoplasm › cytoskeleton By similarity.
Tissue specificity	Widely expressed with highest levels in placenta, lung, kidney and peripheral blood leukocytes and lower levels in brain, liver and pancreas. Ref.6
Sequence similarities	Belongs to the actin-binding proteins ADF family. Coactosin subfamily. Contains 1 ADF-H domain.

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Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Ref.6 Inferred from direct assay. Source: UniProtKB enzyme binding Ref.7 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALOX5	P09917	3	EBI-79926,EBI-79934

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 142

141

Coactosin-like protein

PRO_0000214954

Regions

Domain

2 – 130

129

ADF-H

Amino acid modifications

Modified residue

115

Phosphoserine Ref.8

Experimental info

Mutagenesis

K → A: Abolishes actin-binding activity. Ref.6

Mutagenesis

130

K → A: No effect on 5LO-binding activity. Ref.7

Mutagenesis

131

K → A: Abolishes 5LO-binding activity. Ref.7

Mutagenesis

131

K → E: Abolishes 5LO-binding activity. Ref.7

Mutagenesis

131

K → R: No effect on 5LO-binding activity. Ref.7

Sequence conflict

P → H in AAH42970. Ref.3

Secondary structure

142

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q14019-1 [UniParc].

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

142

15,945

        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

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References

	« Hide 'large scale' referencesShow '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: 9326934] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Cervix, Kidney, Lung and Uterus.
[4]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11. Tissue: Platelet.
[5]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 76-91, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[6]	"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: 11583571] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-75.
[7]	"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: 11297527] [Abstract] Cited for: INTERACTION WITH 5-LIPOXYGENASE, MUTAGENESIS OF LYS-130 AND LYS-131.
[8]	"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, MASS SPECTROMETRY. Tissue: Hepatocyte.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

L54057 mRNA. Translation: AAA88022.1.
BT006968 mRNA. Translation: AAP35614.1.
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.

IPI

IPI00017704.

RefSeq

NP_066972.1.

UniGene

Hs.289092

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T2L	X-ray	2.80	A/B	2-142	[»]
1T3X	X-ray	2.00	A	2-142	[»]
1T3Y	X-ray	1.15	A	2-142	[»]
1TMW	NMR	-	A	2-142	[»]
1VFQ	X-ray	1.90	A	1-142	[»]
1WNJ	NMR	-	A	1-142	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14019. 5 interactions.

PTM databases

PhosphoSite

Q14019.

2-D gel databases

OGP

Q14019.

REPRODUCTION-2DPAGE

IPI00017704.

Proteomic databases

PeptideAtlas

Q14019.

PRIDE

Q14019.

Genome annotation databases

Ensembl

ENSG00000103187. Homo sapiens. [Contig view]

GeneID

23406.

KEGG

hsa:23406.

UCSC

uc002fid.1. human.

Organism-specific databases

GeneCards

GC16M083156.

H-InvDB

HIX0013299.
HIX0038574.

HGNC

HGNC:18304. COTL1.

MIM

606748. gene.

PharmGKB

PA38522.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q14019.

HOVERGEN

Q14019.

OMA

Q14019. KIDKEAC.

Gene expression databases

ArrayExpress

Q14019.

Bgee

Q14019.

CleanEx

HS_COTL1.

GermOnline

ENSG00000103187. Homo sapiens.

Family and domain databases

InterPro

IPR002108. Actin-bd_cofilin/tropomyosin.
[Graphical view]

Pfam

PF00241. Cofilin_ADF. 1 hit.
[Graphical view]

SMART

SM00102. ADF. 1 hit.
[Graphical view]

PROSITE

PS51263. ADF_H. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

45583.

SOURCE

Search...

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Entry information

Entry name

COTL1_HUMAN

Accession

Primary (citable) accession number: Q14019
Secondary accession number(s): Q86XM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 16

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents