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Q14019

- COTL1_HUMAN

UniProt

Q14019 - COTL1_HUMAN

Protein

Coactosin-like protein

Gene

COTL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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
    3. protein binding Source: IntAct

    GO - Biological processi

    1. defense response to fungus Source: Ensembl

    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: 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: UniProt
    4. nuclear membrane Source: UniProtKB-SubCell

    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

    ArrayExpressiQ14019.
    BgeeiQ14019.
    CleanExiHS_COTL1.
    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. 8 interactions.
    IntActiQ14019. 1 interaction.
    STRINGi9606.ENSP00000262428.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000007758.
    HOVERGENiHBG051082.
    InParanoidiQ14019.
    OMAiEYANDKE.
    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

    MATKIDKEAC RAAYNLVRDD GSAVIWVTFK YDGSTIVPGE QGAEYQHFIQ    50
    QCTDDVRLFA FVRFTTGDAM SKRSKFALIT WIGENVSGLQ RAKTGTDKTL 100
    VKEVVQNFAK EFVISDRKEL EEDFIKSELK KAGGANYDAQ TE 142
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10947.1.
    RefSeqi NP_066972.1. NM_021149.3.
    UniGenei Hs.289092.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali Q14019.
    SMRi Q14019. Positions 1-131.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116979. 8 interactions.
    IntActi Q14019. 1 interaction.
    STRINGi 9606.ENSP00000262428.

    PTM databases

    PhosphoSitei Q14019.

    Polymorphism databases

    DMDMi 21759076.

    2D gel databases

    OGPi Q14019.
    REPRODUCTION-2DPAGE IPI00017704.

    Proteomic databases

    MaxQBi Q14019.
    PaxDbi Q14019.
    PeptideAtlasi Q14019.
    PRIDEi Q14019.

    Protocols and materials databases

    DNASUi 23406.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262428 ; ENSP00000262428 ; ENSG00000103187 .
    GeneIDi 23406.
    KEGGi hsa:23406.
    UCSCi uc002fid.3. human.

    Organism-specific databases

    CTDi 23406.
    GeneCardsi GC16M084599.
    H-InvDB HIX0134273.
    HGNCi HGNC:18304. COTL1.
    HPAi HPA008918.
    MIMi 606748. gene.
    neXtProti NX_Q14019.
    PharmGKBi PA38522.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG253317.
    HOGENOMi HOG000007758.
    HOVERGENi HBG051082.
    InParanoidi Q14019.
    OMAi EYANDKE.
    OrthoDBi EOG7R56V4.
    PhylomeDBi Q14019.
    TreeFami TF324318.

    Miscellaneous databases

    ChiTaRSi COTL1. human.
    EvolutionaryTracei Q14019.
    GeneWikii COTL1.
    GenomeRNAii 23406.
    NextBioi 45583.
    PROi Q14019.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14019.
    Bgeei Q14019.
    CleanExi HS_COTL1.
    Genevestigatori Q14019.

    Family and domain databases

    Gene3Di 3.40.20.10. 1 hit.
    InterProi IPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    [Graphical view ]
    Pfami PF00241. Cofilin_ADF. 1 hit.
    [Graphical view ]
    SMARTi SM00102. ADF. 1 hit.
    [Graphical view ]
    PROSITEi PS51263. ADF_H. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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(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.

    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: October 1, 2014
    This is version 128 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