Full text data of COPZ1
COPZ1
(COPZ)
[Confidence: low (only semi-automatic identification from reviews)]
Coatomer subunit zeta-1 (Zeta-1-coat protein; Zeta-1 COP)
Coatomer subunit zeta-1 (Zeta-1-coat protein; Zeta-1 COP)
UniProt
P61923
ID COPZ1_HUMAN Reviewed; 177 AA.
AC P61923; Q549N6; Q9Y3C3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Coatomer subunit zeta-1;
DE AltName: Full=Zeta-1-coat protein;
DE Short=Zeta-1 COP;
GN Name=COPZ1; Synonyms=COPZ; ORFNames=CGI-120, HSPC181;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11056392;
RA Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.;
RT "Identification and characterization of novel isoforms of COP I
RT subunits.";
RL J. Biochem. 128:793-801(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tu Q., Yu L., Hu P.R., Zhang H.L., Huang J., Zhao S.Y.;
RT "Cloning and expression of a new human cDNA homology to B.taurus z-cop
RT mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 1-14, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP STRUCTURE BY NMR, SUBUNIT, AND MUTAGENESIS OF 58-LYS-ILE-59 AND
RP 87-GLU-LEU-88.
RX PubMed=19167404; DOI=10.1016/j.jmb.2008.12.083;
RA Yu W., Lin J., Jin C., Xia B.;
RT "Solution structure of human zeta-COP: direct evidences for structural
RT similarity between COP I and clathrin-adaptor coats.";
RL J. Mol. Biol. 386:903-912(2009).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds
CC to dilysine motifs and reversibly associates with Golgi non-
CC clathrin-coated vesicles, which further mediate biosynthetic
CC protein transport from the ER, via the Golgi up to the trans Golgi
CC network. Coatomer complex is required for budding from Golgi
CC membranes, and is essential for the retrograde Golgi-to-ER
CC transport of dilysine-tagged proteins. In mammals, the coatomer
CC can only be recruited by membranes associated to ADP-ribosylation
CC factors (ARFs), which are small GTP-binding proteins; the complex
CC also influences the Golgi structural integrity, as well as the
CC processing, activity, and endocytic recycling of LDL receptors (By
CC similarity).
CC -!- FUNCTION: The zeta subunit may be involved in regulating the coat
CC assembly and, hence, the rate of biosynthetic protein transport
CC due to its association-dissociation properties with the coatomer
CC complex.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC beta, beta', gamma, delta, epsilon and zeta subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC membrane; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side (By similarity).
CC Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
CC side of the Golgi, as well as on the vesicles/buds originating
CC from it (By similarity).
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB047848; BAB17659.1; -; mRNA.
DR EMBL; AF151878; AAD34115.1; -; mRNA.
DR EMBL; AF161529; AAF29144.1; -; mRNA.
DR EMBL; AF086911; AAP97141.1; -; mRNA.
DR EMBL; CH471054; EAW96774.1; -; Genomic_DNA.
DR EMBL; BC002849; AAH02849.1; -; mRNA.
DR RefSeq; NP_001258663.1; NM_001271734.1.
DR RefSeq; NP_001258664.1; NM_001271735.1.
DR RefSeq; NP_001258665.1; NM_001271736.1.
DR RefSeq; NP_057141.1; NM_016057.2.
DR UniGene; Hs.505652; -.
DR PDB; 2HF6; NMR; -; A=1-149.
DR PDBsum; 2HF6; -.
DR ProteinModelPortal; P61923; -.
DR SMR; P61923; 1-149.
DR DIP; DIP-29873N; -.
DR IntAct; P61923; 1.
DR STRING; 9606.ENSP00000262061; -.
DR PhosphoSite; P61923; -.
DR DMDM; 48428830; -.
DR PaxDb; P61923; -.
DR PRIDE; P61923; -.
DR DNASU; 22818; -.
DR Ensembl; ENST00000262061; ENSP00000262061; ENSG00000111481.
DR GeneID; 22818; -.
DR KEGG; hsa:22818; -.
DR UCSC; uc001sfs.2; human.
DR CTD; 22818; -.
DR GeneCards; GC12P054718; -.
DR HGNC; HGNC:2243; COPZ1.
DR MIM; 615472; gene.
DR neXtProt; NX_P61923; -.
DR PharmGKB; PA26760; -.
DR eggNOG; COG5541; -.
DR HOGENOM; HOG000214428; -.
DR HOVERGEN; HBG051077; -.
DR InParanoid; P61923; -.
DR PhylomeDB; P61923; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; COPZ1; human.
DR EvolutionaryTrace; P61923; -.
DR GeneWiki; COPZ1; -.
DR GenomeRNAi; 22818; -.
DR NextBio; 43208; -.
DR PRO; PR:P61923; -.
DR ArrayExpress; P61923; -.
DR Bgee; P61923; -.
DR CleanEx; HS_COPZ1; -.
DR Genevestigator; P61923; -.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:UniProtKB.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR000804; Clathrin_sm-chain_CS.
DR InterPro; IPR011012; Longin-like_dom.
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; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; ER-Golgi transport;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 177 Coatomer subunit zeta-1.
FT /FTId=PRO_0000193825.
FT MOD_RES 1 1 N-acetylmethionine.
FT MUTAGEN 58 59 EI->KA: Reduced interaction with gamma
FT subunit.
FT MUTAGEN 87 88 EL->KA: Reduced interaction with gamma
FT subunit.
FT STRAND 14 20
FT STRAND 25 30
FT HELIX 38 52
FT STRAND 59 62
FT STRAND 65 72
FT STRAND 75 81
FT HELIX 88 105
FT HELIX 111 115
FT HELIX 118 128
FT HELIX 139 148
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
//
ID COPZ1_HUMAN Reviewed; 177 AA.
AC P61923; Q549N6; Q9Y3C3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Coatomer subunit zeta-1;
DE AltName: Full=Zeta-1-coat protein;
DE Short=Zeta-1 COP;
GN Name=COPZ1; Synonyms=COPZ; ORFNames=CGI-120, HSPC181;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11056392;
RA Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.;
RT "Identification and characterization of novel isoforms of COP I
RT subunits.";
RL J. Biochem. 128:793-801(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tu Q., Yu L., Hu P.R., Zhang H.L., Huang J., Zhao S.Y.;
RT "Cloning and expression of a new human cDNA homology to B.taurus z-cop
RT mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 1-14, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP STRUCTURE BY NMR, SUBUNIT, AND MUTAGENESIS OF 58-LYS-ILE-59 AND
RP 87-GLU-LEU-88.
RX PubMed=19167404; DOI=10.1016/j.jmb.2008.12.083;
RA Yu W., Lin J., Jin C., Xia B.;
RT "Solution structure of human zeta-COP: direct evidences for structural
RT similarity between COP I and clathrin-adaptor coats.";
RL J. Mol. Biol. 386:903-912(2009).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds
CC to dilysine motifs and reversibly associates with Golgi non-
CC clathrin-coated vesicles, which further mediate biosynthetic
CC protein transport from the ER, via the Golgi up to the trans Golgi
CC network. Coatomer complex is required for budding from Golgi
CC membranes, and is essential for the retrograde Golgi-to-ER
CC transport of dilysine-tagged proteins. In mammals, the coatomer
CC can only be recruited by membranes associated to ADP-ribosylation
CC factors (ARFs), which are small GTP-binding proteins; the complex
CC also influences the Golgi structural integrity, as well as the
CC processing, activity, and endocytic recycling of LDL receptors (By
CC similarity).
CC -!- FUNCTION: The zeta subunit may be involved in regulating the coat
CC assembly and, hence, the rate of biosynthetic protein transport
CC due to its association-dissociation properties with the coatomer
CC complex.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC beta, beta', gamma, delta, epsilon and zeta subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC membrane; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side (By similarity).
CC Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
CC side of the Golgi, as well as on the vesicles/buds originating
CC from it (By similarity).
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB047848; BAB17659.1; -; mRNA.
DR EMBL; AF151878; AAD34115.1; -; mRNA.
DR EMBL; AF161529; AAF29144.1; -; mRNA.
DR EMBL; AF086911; AAP97141.1; -; mRNA.
DR EMBL; CH471054; EAW96774.1; -; Genomic_DNA.
DR EMBL; BC002849; AAH02849.1; -; mRNA.
DR RefSeq; NP_001258663.1; NM_001271734.1.
DR RefSeq; NP_001258664.1; NM_001271735.1.
DR RefSeq; NP_001258665.1; NM_001271736.1.
DR RefSeq; NP_057141.1; NM_016057.2.
DR UniGene; Hs.505652; -.
DR PDB; 2HF6; NMR; -; A=1-149.
DR PDBsum; 2HF6; -.
DR ProteinModelPortal; P61923; -.
DR SMR; P61923; 1-149.
DR DIP; DIP-29873N; -.
DR IntAct; P61923; 1.
DR STRING; 9606.ENSP00000262061; -.
DR PhosphoSite; P61923; -.
DR DMDM; 48428830; -.
DR PaxDb; P61923; -.
DR PRIDE; P61923; -.
DR DNASU; 22818; -.
DR Ensembl; ENST00000262061; ENSP00000262061; ENSG00000111481.
DR GeneID; 22818; -.
DR KEGG; hsa:22818; -.
DR UCSC; uc001sfs.2; human.
DR CTD; 22818; -.
DR GeneCards; GC12P054718; -.
DR HGNC; HGNC:2243; COPZ1.
DR MIM; 615472; gene.
DR neXtProt; NX_P61923; -.
DR PharmGKB; PA26760; -.
DR eggNOG; COG5541; -.
DR HOGENOM; HOG000214428; -.
DR HOVERGEN; HBG051077; -.
DR InParanoid; P61923; -.
DR PhylomeDB; P61923; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; COPZ1; human.
DR EvolutionaryTrace; P61923; -.
DR GeneWiki; COPZ1; -.
DR GenomeRNAi; 22818; -.
DR NextBio; 43208; -.
DR PRO; PR:P61923; -.
DR ArrayExpress; P61923; -.
DR Bgee; P61923; -.
DR CleanEx; HS_COPZ1; -.
DR Genevestigator; P61923; -.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:UniProtKB.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR000804; Clathrin_sm-chain_CS.
DR InterPro; IPR011012; Longin-like_dom.
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; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; ER-Golgi transport;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 177 Coatomer subunit zeta-1.
FT /FTId=PRO_0000193825.
FT MOD_RES 1 1 N-acetylmethionine.
FT MUTAGEN 58 59 EI->KA: Reduced interaction with gamma
FT subunit.
FT MUTAGEN 87 88 EL->KA: Reduced interaction with gamma
FT subunit.
FT STRAND 14 20
FT STRAND 25 30
FT HELIX 38 52
FT STRAND 59 62
FT STRAND 65 72
FT STRAND 75 81
FT HELIX 88 105
FT HELIX 111 115
FT HELIX 118 128
FT HELIX 139 148
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
//
MIM
615472
*RECORD*
*FIELD* NO
615472
*FIELD* TI
*615472 COATOMER PROTEIN COMPLEX, SUBUNIT ZETA-1; COPZ1
;;COPZ
*FIELD* TX
DESCRIPTION
read more
Intracellular cargo transport is mediated by vesicles decorated with
protein complexes, such as coat protein complex I (COPI; see 601924).
COPI consists of a 7-subunit coatomer subcomplex plus the small G
protein ARF1 (103180). COPZ1 and COPZ2 (615526) are paralogous isoforms
of the zeta subunit of the coatomer subcomplex (Moelleken et al., 2007).
CLONING
Zhang et al. (2000) cloned COPZ1, which they designated HSPC181, from
CD34 (142230)-positive hematopoietic stem/progenitor cells. The deduced
177-amino acid protein contains a clathrin adaptor complex small chain
(see 603531) signature. Low to moderate COPZ1 expression was present in
all cell lines examined. Orthologs of COPZ1 were detected in mammals,
bacteria, nematode, fly, and yeast, but not in plants.
Using transfected rat hepatocytes, Futatsumori et al. (2000) found that
epitope-tagged human zeta-1 COP colocalized with beta-COP (COPB; 600959)
in the paranuclear region, characteristic of Golgi localization.
GENE FUNCTION
Kuge et al. (1993) found that antibodies directed against bovine
zeta-COP blocked coatomer binding to Chinese hamster ovary Golgi
membranes and prevented assembly of COP-coated vesicles on Golgi
cisternae. They concluded that zeta-COP has a dual role in coat assembly
in budding and in coupling fusion to budding.
Using yeast 2-hybrid analysis, Futatsumori et al. (2000) showed that
both human gamma-1 (COPG1; 615525) and gamma-2 COP (COPG2; 604355)
interacted directly with both human zeta-1 and zeta-2 COP. None of the
gamma or zeta subunits interacted with other COP subunits or with
subunits of the AP1 clathrin adaptor complex (see 603531).
By immunoprecipitation and immunoelectron microscopy of mouse and rat
cells, Moelleken et al. (2007) found a preference for Copg1/Copz1- and
Copg1/Copz2-containing coatomer complexes in the early Golgi apparatus
and Copg2/Copz1-containing coatomer complexes in the late Golgi
apparatus. They concluded that different coatomer isoforms may serve
different intracellular transport routes.
MAPPING
Hartz (2013) mapped the COPZ1 gene to chromosome 12q13.13 based on an
alignment of the COPZ1 sequence (GenBank GENBANK AF086911) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Futatsumori, M.; Kasai, K.; Takatsu, H.; Shin, H.-W.; Nakayama,
K.: Identification and characterization of novel isoforms of COP
I subunits. J. Biochem. 128: 793-801, 2000.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/9/2013.
3. Kuge, O.; Hara-Kuge, S.; Orci, L.; Ravazzola, M.; Amherdt, M.;
Tanigawa, G.; Wieland, F. T.; Rothman, J. E.: Zeta-COP, a subunit
of coatomer, is required for COP-coated vesicle assembly. J. Cell
Biol. 123: 1727-1734, 1993.
4. Moelleken, J.; Malsam, J.; Betts, M. F.; Movafeghi, A.; Reckmann,
I.; Meissner, I.; Hellwig, A.; Russell, R. B.; Sollner, T.; Brugger,
B.; Wieland, F. T.: Differential localization of coatomer complex
isoforms within the Golgi apparatus. Proc. Nat. Acad. Sci. 104:
4425-4430, 2007.
5. Zhang, Q.-H.; Ye, M.; Wu, X.-Y.; Ren, S.-X.; Zhao, M.; Zhao, C.-J.;
Fu, G.; Shen, Y.; Fan, H.-Y.; Lu, G.; Zhong, M.; Xu, X.-R.; and 9
others: Cloning and functional analysis of cDNAs with open reading
frames for 300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells. Genome Res. 10: 1546-1560, 2000.
*FIELD* CD
Patricia A. Hartz: 10/10/2013
*FIELD* ED
mgross: 11/19/2013
mcolton: 11/13/2013
mgross: 10/21/2013
tpirozzi: 10/10/2013
*RECORD*
*FIELD* NO
615472
*FIELD* TI
*615472 COATOMER PROTEIN COMPLEX, SUBUNIT ZETA-1; COPZ1
;;COPZ
*FIELD* TX
DESCRIPTION
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Intracellular cargo transport is mediated by vesicles decorated with
protein complexes, such as coat protein complex I (COPI; see 601924).
COPI consists of a 7-subunit coatomer subcomplex plus the small G
protein ARF1 (103180). COPZ1 and COPZ2 (615526) are paralogous isoforms
of the zeta subunit of the coatomer subcomplex (Moelleken et al., 2007).
CLONING
Zhang et al. (2000) cloned COPZ1, which they designated HSPC181, from
CD34 (142230)-positive hematopoietic stem/progenitor cells. The deduced
177-amino acid protein contains a clathrin adaptor complex small chain
(see 603531) signature. Low to moderate COPZ1 expression was present in
all cell lines examined. Orthologs of COPZ1 were detected in mammals,
bacteria, nematode, fly, and yeast, but not in plants.
Using transfected rat hepatocytes, Futatsumori et al. (2000) found that
epitope-tagged human zeta-1 COP colocalized with beta-COP (COPB; 600959)
in the paranuclear region, characteristic of Golgi localization.
GENE FUNCTION
Kuge et al. (1993) found that antibodies directed against bovine
zeta-COP blocked coatomer binding to Chinese hamster ovary Golgi
membranes and prevented assembly of COP-coated vesicles on Golgi
cisternae. They concluded that zeta-COP has a dual role in coat assembly
in budding and in coupling fusion to budding.
Using yeast 2-hybrid analysis, Futatsumori et al. (2000) showed that
both human gamma-1 (COPG1; 615525) and gamma-2 COP (COPG2; 604355)
interacted directly with both human zeta-1 and zeta-2 COP. None of the
gamma or zeta subunits interacted with other COP subunits or with
subunits of the AP1 clathrin adaptor complex (see 603531).
By immunoprecipitation and immunoelectron microscopy of mouse and rat
cells, Moelleken et al. (2007) found a preference for Copg1/Copz1- and
Copg1/Copz2-containing coatomer complexes in the early Golgi apparatus
and Copg2/Copz1-containing coatomer complexes in the late Golgi
apparatus. They concluded that different coatomer isoforms may serve
different intracellular transport routes.
MAPPING
Hartz (2013) mapped the COPZ1 gene to chromosome 12q13.13 based on an
alignment of the COPZ1 sequence (GenBank GENBANK AF086911) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Futatsumori, M.; Kasai, K.; Takatsu, H.; Shin, H.-W.; Nakayama,
K.: Identification and characterization of novel isoforms of COP
I subunits. J. Biochem. 128: 793-801, 2000.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/9/2013.
3. Kuge, O.; Hara-Kuge, S.; Orci, L.; Ravazzola, M.; Amherdt, M.;
Tanigawa, G.; Wieland, F. T.; Rothman, J. E.: Zeta-COP, a subunit
of coatomer, is required for COP-coated vesicle assembly. J. Cell
Biol. 123: 1727-1734, 1993.
4. Moelleken, J.; Malsam, J.; Betts, M. F.; Movafeghi, A.; Reckmann,
I.; Meissner, I.; Hellwig, A.; Russell, R. B.; Sollner, T.; Brugger,
B.; Wieland, F. T.: Differential localization of coatomer complex
isoforms within the Golgi apparatus. Proc. Nat. Acad. Sci. 104:
4425-4430, 2007.
5. Zhang, Q.-H.; Ye, M.; Wu, X.-Y.; Ren, S.-X.; Zhao, M.; Zhao, C.-J.;
Fu, G.; Shen, Y.; Fan, H.-Y.; Lu, G.; Zhong, M.; Xu, X.-R.; and 9
others: Cloning and functional analysis of cDNAs with open reading
frames for 300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells. Genome Res. 10: 1546-1560, 2000.
*FIELD* CD
Patricia A. Hartz: 10/10/2013
*FIELD* ED
mgross: 11/19/2013
mcolton: 11/13/2013
mgross: 10/21/2013
tpirozzi: 10/10/2013