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P61924

- COPZ1_MOUSE

UniProt

P61924 - COPZ1_MOUSE

Protein

Coatomer subunit zeta-1

Gene

Copz1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors By similarity.By similarity
    The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.By similarity

    GO - Biological processi

    1. intracellular protein transport Source: InterPro
    2. intra-Golgi vesicle-mediated transport Source: UniProtKB

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_227904. COPI Mediated Transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coatomer subunit zeta-1
    Alternative name(s):
    Zeta-1-coat protein
    Short name:
    Zeta-1 COP
    Gene namesi
    Name:Copz1
    Synonyms:Copz
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1929063. Copz1.

    Subcellular locationi

    Cytoplasm By similarity. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicleCOPI-coated vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it.By similarity

    GO - Cellular componenti

    1. COPI vesicle coat Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 177177Coatomer subunit zeta-1PRO_0000193826Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP61924.
    PaxDbiP61924.
    PRIDEiP61924.

    PTM databases

    PhosphoSiteiP61924.

    Expressioni

    Gene expression databases

    ArrayExpressiP61924.
    BgeeiP61924.
    CleanExiMM_COPZ1.
    GenevestigatoriP61924.

    Interactioni

    Subunit structurei

    Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.By similarity

    Protein-protein interaction databases

    BioGridi207987. 1 interaction.
    IntActiP61924. 1 interaction.
    MINTiMINT-1864573.

    Structurei

    3D structure databases

    ProteinModelPortaliP61924.
    SMRiP61924. Positions 1-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5541.
    HOGENOMiHOG000214428.
    HOVERGENiHBG051077.
    InParanoidiP61924.
    OMAiMGSSHEN.
    OrthoDBiEOG75TMD6.
    PhylomeDBiP61924.
    TreeFamiTF300262.

    Family and domain databases

    InterProiIPR022775. AP_mu_sigma_su.
    IPR000804. Clathrin_sm-chain_CS.
    IPR011012. Longin-like_dom.
    [Graphical view]
    PfamiPF01217. Clat_adaptor_s. 1 hit.
    [Graphical view]
    SUPFAMiSSF64356. SSF64356. 1 hit.
    PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P61924-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEALILEPSL YTVKAILILD NDGDRLFAKY YDDTYPSVKE QKAFEKNIFN    50
    KTHRTDSEIA LLEGLTVVYK SSIDLYFYVI GSSYENELML MAVLNCLFDS 100
    LSQMLRKNVE KRALLENMEG LFLAVDEIVD GGVILESDPQ QVVHRVALRG 150
    EDVPLTEQTV SQVLQSAKEQ IKWSLLR 177
    Length:177
    Mass (Da):20,198
    Last modified:June 7, 2004 - v1
    Checksum:i355530D032D3A049
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037370 mRNA. Translation: BAA90303.1.
    AK003302 mRNA. Translation: BAB22703.1.
    BC002246 mRNA. No translation available.
    BC058524 mRNA. Translation: AAH58524.1.
    BC085314 mRNA. Translation: AAH85314.1.
    CCDSiCCDS27901.1.
    RefSeqiNP_062791.1. NM_019817.1.
    UniGeneiMm.29473.

    Genome annotation databases

    EnsembliENSMUST00000100162; ENSMUSP00000097738; ENSMUSG00000060992.
    GeneIDi56447.
    KEGGimmu:56447.
    UCSCiuc007xxv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037370 mRNA. Translation: BAA90303.1 .
    AK003302 mRNA. Translation: BAB22703.1 .
    BC002246 mRNA. No translation available.
    BC058524 mRNA. Translation: AAH58524.1 .
    BC085314 mRNA. Translation: AAH85314.1 .
    CCDSi CCDS27901.1.
    RefSeqi NP_062791.1. NM_019817.1.
    UniGenei Mm.29473.

    3D structure databases

    ProteinModelPortali P61924.
    SMRi P61924. Positions 1-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207987. 1 interaction.
    IntActi P61924. 1 interaction.
    MINTi MINT-1864573.

    PTM databases

    PhosphoSitei P61924.

    Proteomic databases

    MaxQBi P61924.
    PaxDbi P61924.
    PRIDEi P61924.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000100162 ; ENSMUSP00000097738 ; ENSMUSG00000060992 .
    GeneIDi 56447.
    KEGGi mmu:56447.
    UCSCi uc007xxv.1. mouse.

    Organism-specific databases

    CTDi 22818.
    MGIi MGI:1929063. Copz1.

    Phylogenomic databases

    eggNOGi COG5541.
    HOGENOMi HOG000214428.
    HOVERGENi HBG051077.
    InParanoidi P61924.
    OMAi MGSSHEN.
    OrthoDBi EOG75TMD6.
    PhylomeDBi P61924.
    TreeFami TF300262.

    Enzyme and pathway databases

    Reactomei REACT_227904. COPI Mediated Transport.

    Miscellaneous databases

    ChiTaRSi COPZ1. mouse.
    NextBioi 312654.
    PROi P61924.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61924.
    Bgeei P61924.
    CleanExi MM_COPZ1.
    Genevestigatori P61924.

    Family and domain databases

    InterProi IPR022775. AP_mu_sigma_su.
    IPR000804. Clathrin_sm-chain_CS.
    IPR011012. Longin-like_dom.
    [Graphical view ]
    Pfami PF01217. Clat_adaptor_s. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64356. SSF64356. 1 hit.
    PROSITEi PS00989. CLAT_ADAPTOR_S. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Murine Copz1 gene encoding nonclathrin coat protein zeta-COP."
      Hahn Y., Chung J.H.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6 and C57BL/6J.
      Tissue: Brain and Embryo.

    Entry informationi

    Entry nameiCOPZ1_MOUSE
    AccessioniPrimary (citable) accession number: P61924
    Secondary accession number(s): Q9Y3C3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3