COPZ1_MOUSE
ID COPZ1_MOUSE Reviewed; 177 AA.
AC P61924; Q9Y3C3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Coatomer subunit zeta-1;
DE AltName: Full=Zeta-1-coat protein;
DE Short=Zeta-1 COP;
GN Name=Copz1; Synonyms=Copz;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hahn Y., Chung J.H.;
RT "Murine Copz1 gene encoding nonclathrin coat protein zeta-COP.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000250}.
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; AB037370; BAA90303.1; -; mRNA.
DR EMBL; AK003302; BAB22703.1; -; mRNA.
DR EMBL; BC002246; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC058524; AAH58524.1; -; mRNA.
DR EMBL; BC085314; AAH85314.1; -; mRNA.
DR CCDS; CCDS27901.1; -.
DR RefSeq; NP_062791.1; NM_019817.1.
DR PDB; 5A1U; EM; 13.00 A; F=1-177.
DR PDB; 5A1V; EM; 21.00 A; F/N/W=1-177.
DR PDB; 5A1W; EM; 18.00 A; F=1-177.
DR PDB; 5A1X; EM; 23.00 A; F/N=1-177.
DR PDB; 5A1Y; EM; 21.00 A; F/N/W=1-177.
DR PDB; 5NZR; EM; 9.20 A; L/Z=1-177.
DR PDB; 5NZS; EM; 10.10 A; L/Z=1-177.
DR PDB; 5NZT; EM; 17.00 A; L/Z=1-177.
DR PDB; 5NZU; EM; 15.00 A; L/Z=1-177.
DR PDB; 5NZV; EM; 17.30 A; L/S/U/Z=1-177.
DR PDBsum; 5A1U; -.
DR PDBsum; 5A1V; -.
DR PDBsum; 5A1W; -.
DR PDBsum; 5A1X; -.
DR PDBsum; 5A1Y; -.
DR PDBsum; 5NZR; -.
DR PDBsum; 5NZS; -.
DR PDBsum; 5NZT; -.
DR PDBsum; 5NZU; -.
DR PDBsum; 5NZV; -.
DR AlphaFoldDB; P61924; -.
DR BMRB; P61924; -.
DR SMR; P61924; -.
DR BioGRID; 207987; 13.
DR CORUM; P61924; -.
DR IntAct; P61924; 2.
DR MINT; P61924; -.
DR STRING; 10090.ENSMUSP00000097738; -.
DR iPTMnet; P61924; -.
DR PhosphoSitePlus; P61924; -.
DR SwissPalm; P61924; -.
DR EPD; P61924; -.
DR jPOST; P61924; -.
DR PaxDb; P61924; -.
DR PeptideAtlas; P61924; -.
DR PRIDE; P61924; -.
DR ProteomicsDB; 283792; -.
DR Antibodypedia; 27430; 226 antibodies from 25 providers.
DR DNASU; 56447; -.
DR Ensembl; ENSMUST00000100162; ENSMUSP00000097738; ENSMUSG00000060992.
DR GeneID; 56447; -.
DR KEGG; mmu:56447; -.
DR UCSC; uc007xxv.1; mouse.
DR CTD; 22818; -.
DR MGI; MGI:1929063; Copz1.
DR VEuPathDB; HostDB:ENSMUSG00000060992; -.
DR eggNOG; KOG3343; Eukaryota.
DR GeneTree; ENSGT00390000004405; -.
DR HOGENOM; CLU_086803_2_0_1; -.
DR InParanoid; P61924; -.
DR OMA; NEQTIMS; -.
DR OrthoDB; 1522668at2759; -.
DR PhylomeDB; P61924; -.
DR TreeFam; TF300262; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 56447; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Copz1; mouse.
DR PRO; PR:P61924; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P61924; protein.
DR Bgee; ENSMUSG00000060992; Expressed in yolk sac and 264 other tissues.
DR ExpressionAtlas; P61924; baseline and differential.
DR Genevisible; P61924; MM.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR000804; Clathrin_sm-chain_CS.
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.
DR PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoplasmic vesicle;
KW ER-Golgi transport; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..177
FT /note="Coatomer subunit zeta-1"
FT /id="PRO_0000193826"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61923"
SQ SEQUENCE 177 AA; 20198 MW; 355530D032D3A049 CRC64;
MEALILEPSL YTVKAILILD NDGDRLFAKY YDDTYPSVKE QKAFEKNIFN KTHRTDSEIA
LLEGLTVVYK SSIDLYFYVI GSSYENELML MAVLNCLFDS LSQMLRKNVE KRALLENMEG
LFLAVDEIVD GGVILESDPQ QVVHRVALRG EDVPLTEQTV SQVLQSAKEQ IKWSLLR
