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P17891

- CLC1_YEAST

UniProt

P17891 - CLC1_YEAST

Protein

Clathrin light chain

Gene

CLC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi. The yeast light chain is important for cell growth. The light chain may help to properly orient the assembly/ disassembly of the clathrin coats.

    GO - Molecular functioni

    1. structural molecule activity Source: SGD

    GO - Biological processi

    1. endocytosis Source: SGD
    2. intracellular protein transport Source: InterPro
    3. positive regulation of endocytosis Source: SGD
    4. vesicle-mediated transport Source: SGD

    Keywords - Ligandi

    Calcium, Calmodulin-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30865-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Clathrin light chain
    Short name:
    CLC
    Gene namesi
    Name:CLC1
    Ordered Locus Names:YGR167W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR167w.
    SGDiS000003399. CLC1.

    Subcellular locationi

    GO - Cellular componenti

    1. clathrin coat of coated pit Source: InterPro
    2. clathrin coat of trans-Golgi network vesicle Source: InterPro
    3. clathrin vesicle coat Source: SGD

    Keywords - Cellular componenti

    Coated pit, Cytoplasmic vesicle, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 233233Clathrin light chainPRO_0000205776Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491Phosphothreonine1 Publication
    Modified residuei52 – 521Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP17891.
    PaxDbiP17891.
    PeptideAtlasiP17891.

    Expressioni

    Gene expression databases

    GenevestigatoriP17891.

    Interactioni

    Subunit structurei

    Clathrin coats are formed from molecules containing 3 heavy chains and 3 light chains. Interacts with the auxilin-like clathrin uncoating factor SWA2.1 Publication

    Protein-protein interaction databases

    BioGridi33419. 399 interactions.
    DIPiDIP-2280N.
    IntActiP17891. 12 interactions.
    MINTiMINT-527297.
    STRINGi4932.YGR167W.

    Structurei

    3D structure databases

    ProteinModelPortaliP17891.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni144 – 20461Involved in binding clathrin heavy chainSequence AnalysisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili125 – 18662Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the clathrin light chain family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG251359.
    HOGENOMiHOG000190326.
    OMAiSTFESQF.
    OrthoDBiEOG7Z95XB.

    Family and domain databases

    InterProiIPR000996. Clathrin_L-chain.
    [Graphical view]
    PANTHERiPTHR10639. PTHR10639. 1 hit.
    PfamiPF01086. Clathrin_lg_ch. 1 hit.
    [Graphical view]
    PROSITEiPS00581. CLATHRIN_LIGHT_CHN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P17891-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEKFPPLED QNIDFTPNDK KDDDTDFLKR EAEILGDEFK TEQDDILETE    50
    ASPAKDDDEI RDFEEQFPDI NSANGAVSSD QNGSATVSSG NDNGEADDDF 100
    STFEGANQST ESVKEDRSEV VDQWKQRRAV EIHEKDLKDE ELKKELQDEA 150
    IKHIDDFYDS YNKKKEQQLE DAAKEAEAFL KKRDEFFGQD NTTWDRALQL 200
    INQDDADIIG GRDRSKLKEI LLRLKGNAKA PGA 233
    Length:233
    Mass (Da):26,532
    Last modified:November 1, 1990 - v1
    Checksum:i27BAB175780EC8B3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52272 Genomic DNA. Translation: CAA36515.1.
    Z72952 Genomic DNA. Translation: CAA97192.1.
    Z72953 Genomic DNA. Translation: CAA97193.1.
    AY558272 Genomic DNA. Translation: AAS56598.1.
    BK006941 Genomic DNA. Translation: DAA08261.1.
    PIRiA36425.
    RefSeqiNP_011683.3. NM_001181296.3.

    Genome annotation databases

    EnsemblFungiiYGR167W; YGR167W; YGR167W.
    GeneIDi853077.
    KEGGisce:YGR167W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52272 Genomic DNA. Translation: CAA36515.1 .
    Z72952 Genomic DNA. Translation: CAA97192.1 .
    Z72953 Genomic DNA. Translation: CAA97193.1 .
    AY558272 Genomic DNA. Translation: AAS56598.1 .
    BK006941 Genomic DNA. Translation: DAA08261.1 .
    PIRi A36425.
    RefSeqi NP_011683.3. NM_001181296.3.

    3D structure databases

    ProteinModelPortali P17891.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33419. 399 interactions.
    DIPi DIP-2280N.
    IntActi P17891. 12 interactions.
    MINTi MINT-527297.
    STRINGi 4932.YGR167W.

    Proteomic databases

    MaxQBi P17891.
    PaxDbi P17891.
    PeptideAtlasi P17891.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR167W ; YGR167W ; YGR167W .
    GeneIDi 853077.
    KEGGi sce:YGR167W.

    Organism-specific databases

    CYGDi YGR167w.
    SGDi S000003399. CLC1.

    Phylogenomic databases

    eggNOGi NOG251359.
    HOGENOMi HOG000190326.
    OMAi STFESQF.
    OrthoDBi EOG7Z95XB.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30865-MONOMER.

    Miscellaneous databases

    NextBioi 973038.

    Gene expression databases

    Genevestigatori P17891.

    Family and domain databases

    InterProi IPR000996. Clathrin_L-chain.
    [Graphical view ]
    PANTHERi PTHR10639. PTHR10639. 1 hit.
    Pfami PF01086. Clathrin_lg_ch. 1 hit.
    [Graphical view ]
    PROSITEi PS00581. CLATHRIN_LIGHT_CHN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Yeast clathrin has a distinctive light chain that is important for cell growth."
      Silveira L.A., Wong D.H., Masiarz F.R., Schekman R.
      J. Cell Biol. 111:1437-1449(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-39.
    2. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
      Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
      Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "The auxilin-like phosphoprotein Swa2p is required for clathrin function in yeast."
      Gall W.E., Higginbotham M.A., Chen C.-Y., Ingram M.F., Cyr D.M., Graham T.R.
      Curr. Biol. 10:1349-1358(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SWA2.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49 AND SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCLC1_YEAST
    AccessioniPrimary (citable) accession number: P17891
    Secondary accession number(s): D6VUV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    CLC1 binds calcium, and calmodulin in presence of calcium.
    Present with 3490 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3