COPZ2_HUMAN
ID COPZ2_HUMAN Reviewed; 210 AA.
AC Q9P299;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Coatomer subunit zeta-2;
DE AltName: Full=Zeta-2-coat protein;
DE Short=Zeta-2 COP;
GN Name=COPZ2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
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 "Homo sapiens COPZ2 gene encoding nonclathrin coat protein zeta-COP.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
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).
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 {ECO:0000250}. Endoplasmic reticulum-
CC Golgi intermediate compartment membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi
CC apparatus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle,
CC COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is
CC cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as
CC well as on the vesicles/buds originating from it. Shows a significant
CC preference for ERGIC and cis-Golgi apparatus compared with trans-Golgi
CC network. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC {ECO:0000305}.
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DR EMBL; AB047849; BAB17660.1; -; mRNA.
DR EMBL; AB037938; BAA90670.1; -; mRNA.
DR EMBL; BC015924; AAH15924.1; -; mRNA.
DR CCDS; CCDS74092.1; -.
DR RefSeq; NP_057513.1; NM_016429.3.
DR AlphaFoldDB; Q9P299; -.
DR SMR; Q9P299; -.
DR BioGRID; 119390; 13.
DR STRING; 9606.ENSP00000480707; -.
DR iPTMnet; Q9P299; -.
DR PhosphoSitePlus; Q9P299; -.
DR BioMuta; COPZ2; -.
DR DMDM; 20532038; -.
DR jPOST; Q9P299; -.
DR MassIVE; Q9P299; -.
DR MaxQB; Q9P299; -.
DR PaxDb; Q9P299; -.
DR PeptideAtlas; Q9P299; -.
DR PRIDE; Q9P299; -.
DR ProteomicsDB; 83762; -.
DR Antibodypedia; 53378; 66 antibodies from 16 providers.
DR DNASU; 51226; -.
DR Ensembl; ENST00000621465.5; ENSP00000480707.1; ENSG00000005243.10.
DR GeneID; 51226; -.
DR KEGG; hsa:51226; -.
DR MANE-Select; ENST00000621465.5; ENSP00000480707.1; NM_016429.4; NP_057513.1.
DR UCSC; uc032flu.2; human.
DR CTD; 51226; -.
DR DisGeNET; 51226; -.
DR GeneCards; COPZ2; -.
DR HGNC; HGNC:19356; COPZ2.
DR HPA; ENSG00000005243; Low tissue specificity.
DR MIM; 615526; gene.
DR neXtProt; NX_Q9P299; -.
DR OpenTargets; ENSG00000005243; -.
DR PharmGKB; PA134862698; -.
DR VEuPathDB; HostDB:ENSG00000005243; -.
DR eggNOG; KOG3343; Eukaryota.
DR GeneTree; ENSGT00390000004405; -.
DR HOGENOM; CLU_086803_2_0_1; -.
DR InParanoid; Q9P299; -.
DR OMA; KVNFRTD; -.
DR OrthoDB; 1522668at2759; -.
DR PhylomeDB; Q9P299; -.
DR TreeFam; TF300262; -.
DR PathwayCommons; Q9P299; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; Q9P299; -.
DR BioGRID-ORCS; 51226; 6 hits in 253 CRISPR screens.
DR GenomeRNAi; 51226; -.
DR Pharos; Q9P299; Tdark.
DR PRO; PR:Q9P299; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9P299; protein.
DR Bgee; ENSG00000005243; Expressed in tendon of biceps brachii and 175 other tissues.
DR ExpressionAtlas; Q9P299; baseline and differential.
DR Genevisible; Q9P299; HS.
DR GO; GO:0005801; C:cis-Golgi network; NAS:UniProtKB.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..210
FT /note="Coatomer subunit zeta-2"
FT /id="PRO_0000193831"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 23548 MW; 2DD9D47E482C15DB CRC64;
MQRPEAWPRP HPGEGAAAAQ AGGPAPPARA GEPSGLRLQE PSLYTIKAVF ILDNDGRRLL
AKYYDDTFPS MKEQMVFEKN VFNKTSRTES EIAFFGGMTI VYKNSIDLFL YVVGSSYENE
LMLMSVLTCL FESLNHMLRK NVEKRWLLEN MDGAFLVLDE IVDGGVILES DPQQVIQKVN
FRADDGGLTE QSVAQVLQSA KEQIKWSLLK
