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COPZ_SCHPO
ID   COPZ_SCHPO              Reviewed;         190 AA.
AC   O74891;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Probable coatomer subunit zeta;
DE   AltName: Full=Zeta-coat protein;
DE            Short=Zeta-COP;
GN   Name=ret3; ORFNames=SPCC576.07;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC       dilysine motifs and reversibly associates with Golgi non-clathrin-
CC       coated vesicles, which further mediate biosynthetic protein transport
CC       from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC       complex is required for budding from Golgi membranes, and is essential
CC       for the retrograde Golgi-to-ER transport of dilysine-tagged proteins
CC       (By similarity). The zeta subunit may be involved in regulating the
CC       coat assembly and, hence, the rate of biosynthetic protein transport
CC       due to its association-dissociation properties with the coatomer
CC       complex (By similarity). {ECO:0000250|UniProtKB:P53600}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC       the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC       originating from it. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAA21186.1; -; Genomic_DNA.
DR   PIR; T41417; T41417.
DR   RefSeq; NP_588434.1; NM_001023425.2.
DR   AlphaFoldDB; O74891; -.
DR   SMR; O74891; -.
DR   BioGRID; 276084; 2.
DR   STRING; 4896.SPCC576.07.1; -.
DR   iPTMnet; O74891; -.
DR   MaxQB; O74891; -.
DR   PaxDb; O74891; -.
DR   PRIDE; O74891; -.
DR   EnsemblFungi; SPCC576.07.1; SPCC576.07.1:pep; SPCC576.07.
DR   GeneID; 2539522; -.
DR   KEGG; spo:SPCC576.07; -.
DR   PomBase; SPCC576.07; ret3.
DR   VEuPathDB; FungiDB:SPCC576.07; -.
DR   eggNOG; KOG3343; Eukaryota.
DR   HOGENOM; CLU_086803_0_0_1; -.
DR   InParanoid; O74891; -.
DR   OMA; NEQTIMS; -.
DR   PhylomeDB; O74891; -.
DR   Reactome; R-SPO-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   PRO; PR:O74891; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0030126; C:COPI vesicle coat; ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:PomBase.
DR   InterPro; IPR022775; AP_mu_sigma_su.
DR   InterPro; IPR039652; Coatomer_zeta.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   PANTHER; PTHR11043; PTHR11043; 1.
DR   Pfam; PF01217; Clat_adaptor_s; 1.
DR   SUPFAM; SSF64356; SSF64356; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..190
FT                   /note="Probable coatomer subunit zeta"
FT                   /id="PRO_0000193829"
SQ   SEQUENCE   190 AA;  21686 MW;  F0CCBFA254DF430F CRC64;
     MNLTLYAVNA FLILDSSGKR IFTKYYAPPH LKEGEGGVFN SVKEEKTFEK GLFEKTWKTQ
     NDILTYDGKL VVMLTVMDVI FYIVGGMEEN EVMLYECLRS IRDALELLFK YVPDKRTLLE
     NYDQLVIVVD ETIDDGVILE TEPALIAARV TKGPVSEAQA IVSDFKEMGF MNSFQKAREK
     ITERILKGTF
 
 
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