Q14019 (COTL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coactosin-like protein

Gene names

Name:	COTL1
Synonyms:	CLP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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

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.14 Ref.15
Subcellular location	Cytoplasm › cytoskeleton 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.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Membrane Nucleus
Ligand	Actin-binding
Molecular function	Chaperone
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	defense response to fungus Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	actin binding Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALOX5	P09917	4	EBI-79926,EBI-79934

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 142

141

Coactosin-like protein

PRO_0000214954

Regions

Domain

2 – 130

129

ADF-H

Region

66 – 75

10

Flexible and important for F-actin binding

Amino acid modifications

Modified residue

102

1

N6-acetyllysine Ref.10

Modified residue

126

1

N6-acetyllysine Ref.10

Experimental info

Mutagenesis

75

1

K → A: Abolishes actin-binding activity. Ref.8

Mutagenesis

130

1

K → A: No effect on 5LO-binding activity. Ref.9

Mutagenesis

131

1

K → A: Abolishes 5LO-binding activity. Ref.9

Mutagenesis

131

1

K → E: Abolishes 5LO-binding activity. Ref.9

Mutagenesis

131

1

K → R: No effect on 5LO-binding activity. Ref.9

Sequence conflict

38

1

P → H in AAH42970. Ref.5

Secondary structure

1

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142

Helix Strand Turn

Details...

Helix

7 – 18

12

Beta strand

20 – 23

4

Beta strand

26 – 32

7

Beta strand

35 – 44

10

Helix

45 – 51

7

Beta strand

54 – 56

3

Beta strand

57 – 66

10

Helix

69 – 71

3

Beta strand

73 – 82

10

Beta strand

84 – 86

3

Helix

88 – 101

14

Turn

102 – 104

3

Beta strand

109 – 114

6

Helix

117 – 120

4

Helix

122 – 131

10

Sequences

	Sequence		Length	Mass (Da)
	Q14019 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A4B881DD8E89A35D	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

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] [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. , 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. , 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, 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, MASS SPECTROMETRY.
[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]	"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.
[14]	"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.
[15]	"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.

IPI

IPI00017704.

RefSeq

NP_066972.1. NM_021149.2.

UniGene

Hs.289092.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q14019.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14019. 1 interaction.

STRING

9606.ENSP00000262428.

PTM databases

PhosphoSite

Q14019.

Polymorphism databases

DMDM

21759076.

2D gel databases

OGP

Q14019.

REPRODUCTION-2DPAGE

IPI00017704.

Proteomic databases

PaxDb

Q14019.

PeptideAtlas

Q14019.

PRIDE

Q14019.

Protocols and materials databases

DNASU

23406.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262428; ENSP00000262428; ENSG00000103187.

GeneID

23406.

KEGG

hsa:23406.

UCSC

uc002fid.3. human.

Organism-specific databases

CTD

23406.

GeneCards

GC16M084599.

H-InvDB

HIX0134273.

HGNC

HGNC:18304. COTL1.

HPA

HPA008918.

MIM

606748. gene.

neXtProt

NX_Q14019.

PharmGKB

PA38522.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG253317.

HOGENOM

HOG000007758.

HOVERGEN

HBG051082.

InParanoid

Q14019.

OMA

CTDDVRL.

OrthoDB

EOG4W0XFD.

PhylomeDB

Q14019.

Gene expression databases

ArrayExpress

Q14019.

Bgee

Q14019.

CleanEx

HS_COTL1.

Genevestigator

Q14019.

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

ChiTaRS

COTL1. human.

EvolutionaryTrace

Q14019.

GenomeRNAi

23406.

NextBio

45583.

SOURCE

Search...

Entry information

Entry name

COTL1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.