COPZ2_MOUSE
ID COPZ2_MOUSE Reviewed; 205 AA.
AC Q9JHH9; A2A6D6;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Coatomer subunit zeta-2;
DE AltName: Full=Zeta-2-coat protein;
DE Short=Zeta-2 COP;
GN Name=Copz2;
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].
RX PubMed=11056392; DOI=10.1093/oxfordjournals.jbchem.a022817;
RA Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.;
RT "Identification and characterization of novel isoforms of COP I subunits.";
RL J. Biochem. 128:793-801(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hahn Y., Chung J.H.;
RT "Identification of zeta-COP genes from various organisms.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Whitney J.A., Kreis T.E.;
RT "Newly identified coatomer subunits reveal multiple COPI complexes in the
RT early secretory pathway.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17360540; DOI=10.1073/pnas.0611360104;
RA Moelleken J., Malsam J., Betts M.J., Movafeghi A., Reckmann I.,
RA Meissner I., Hellwig A., Russell R.B., Sollner T., Brugger B.,
RA Wieland F.T.;
RT "Differential localization of coatomer complex isoforms within the Golgi
RT apparatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4425-4430(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, 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 The zeta subunit may be involved in regulating the coat assembly and,
CC hence, the rate of biosynthetic protein transport due to its
CC association-dissociation properties with the coatomer complex.
CC {ECO:0000250|UniProtKB:P53600}.
CC -!- SUBUNIT: Oligomeric complex.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}.
CC Endoplasmic reticulum-Golgi intermediate compartment membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:17360540}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17360540}; Cytoplasmic side
CC {ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or
CC polymerized on the cytoplasmic side of the Golgi, as well as on the
CC vesicles/buds originating from it. Shows a significant preference for
CC ERGIC and cis-Golgi apparatus compared with trans-Golgi network.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC {ECO:0000305}.
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DR EMBL; AB047850; BAB17661.1; -; mRNA.
DR EMBL; AB040137; BAA92831.1; -; mRNA.
DR EMBL; AF237687; AAF37723.1; -; mRNA.
DR EMBL; AL596384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025122; AAH25122.1; -; mRNA.
DR CCDS; CCDS25305.1; -.
DR RefSeq; NP_063930.1; NM_019877.2.
DR AlphaFoldDB; Q9JHH9; -.
DR SMR; Q9JHH9; -.
DR BioGRID; 207922; 1.
DR STRING; 10090.ENSMUSP00000018816; -.
DR PhosphoSitePlus; Q9JHH9; -.
DR MaxQB; Q9JHH9; -.
DR PaxDb; Q9JHH9; -.
DR PeptideAtlas; Q9JHH9; -.
DR PRIDE; Q9JHH9; -.
DR ProteomicsDB; 284089; -.
DR Antibodypedia; 53378; 66 antibodies from 16 providers.
DR DNASU; 56358; -.
DR Ensembl; ENSMUST00000018816; ENSMUSP00000018816; ENSMUSG00000018672.
DR GeneID; 56358; -.
DR KEGG; mmu:56358; -.
DR UCSC; uc007lcu.1; mouse.
DR CTD; 51226; -.
DR MGI; MGI:1929008; Copz2.
DR VEuPathDB; HostDB:ENSMUSG00000018672; -.
DR eggNOG; KOG3343; Eukaryota.
DR GeneTree; ENSGT00390000004405; -.
DR HOGENOM; CLU_086803_2_0_1; -.
DR InParanoid; Q9JHH9; -.
DR OMA; KVNFRTD; -.
DR OrthoDB; 1522668at2759; -.
DR PhylomeDB; Q9JHH9; -.
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; 56358; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Copz2; mouse.
DR PRO; PR:Q9JHH9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JHH9; protein.
DR Bgee; ENSMUSG00000018672; Expressed in prostate gland ventral lobe and 209 other tissues.
DR ExpressionAtlas; Q9JHH9; baseline and differential.
DR Genevisible; Q9JHH9; MM.
DR GO; GO:0030126; C:COPI vesicle coat; ISO:MGI.
DR GO; GO:0030137; C:COPI-coated vesicle; ISS:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..205
FT /note="Coatomer subunit zeta-2"
FT /id="PRO_0000193832"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 205 AA; 22934 MW; 8BC358417A7F15D7 CRC64;
MQRPEAWPRP HPGEGASAAQ AGGAAPPTRA TEQREPSLYT IKAVFILDND GRRLLAKYYD
DTFPSVKEQM VFEKNVFNKT SRTESEIAFL GGMTIVYKSS IDIFLYVVGS SSENELMLMS
VLACLFDSLS HILRKNVEKR WLLENMDGAF LVLDETVDGG VILESDPQQV IQKVNFRTDD
SGLTEQSVAQ VLQSAKEQIK WSLLK
