Full text data of COPG1
COPG1
(COPG)
[Confidence: low (only semi-automatic identification from reviews)]
Coatomer subunit gamma-1 (Gamma-1-coat protein; Gamma-1-COP)
Coatomer subunit gamma-1 (Gamma-1-coat protein; Gamma-1-COP)
UniProt
Q9Y678
ID COPG1_HUMAN Reviewed; 874 AA.
AC Q9Y678; A8K6M8; B3KMF6; Q54AC4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Coatomer subunit gamma-1;
DE AltName: Full=Gamma-1-coat protein;
DE Short=Gamma-1-COP;
GN Name=COPG1; Synonyms=COPG;
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], INTERACTION WITH COPB1 AND TMED10, AND
RP SUBCELLULAR LOCATION.
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].
RC TISSUE=Pituitary;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [6]
RP FUNCTION, AND INTERACTION WITH EGFR.
RX PubMed=20674546; DOI=10.1016/j.bbrc.2010.07.096;
RA Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C.;
RT "COPI-mediated retrograde trafficking from the Golgi to the ER
RT regulates EGFR nuclear transport.";
RL Biochem. Biophys. Res. Commun. 399:498-504(2010).
RN [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 608-874, INTERACTION WITH
RP ZNF289, AND MUTAGENESIS OF TRP-776.
RX PubMed=14690497; DOI=10.1111/j.1600-0854.2004.00158.x;
RA Watson P.J., Frigerio G., Collins B.M., Duden R., Owen D.J.;
RT "Gamma-COP appendage domain -- structure and function.";
RL Traffic 5:79-88(2004).
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.
CC Required for limiting lipid storage in lipid droplets. Involved in
CC lipid homeostasis by regulating the presence of perilipin family
CC members PLIN2 and PLIN3 at the lipid droplet surface and promoting
CC the association of adipocyte triglyceride lipase (PNPLA2) with the
CC lipid droplet surface to mediate lipolysis (By similarity).
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC beta, beta', gamma, delta, epsilon and zeta subunits. Interacts
CC with ZNF289/ARFGAP2 through its C-terminal appendage domain.
CC Interacts with EGFR upon EGF treatment; interaction is essential
CC for regulation of EGF-dependent nuclear transport of EGFR by
CC retrograde trafficking from the Golgi to the ER. Interacts with
CC COPB1. Interacts with TMED10 (via C-terminus). Interacts with
CC TMED2, TMED3, TMED7 and TMED9.
CC -!- INTERACTION:
CC Q92538:GBF1; NbExp=2; IntAct=EBI-1049127, EBI-359050;
CC Q9NTJ5:SACM1L; NbExp=3; IntAct=EBI-1049127, EBI-3917235;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cytoplasmic
CC vesicle, COPI-coated vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side (By similarity). Note=The coatomer is
CC cytoplasmic or polymerized on the cytoplasmic side of the Golgi,
CC as well as on the vesicles/buds originating from it (By
CC similarity).
CC -!- SIMILARITY: Belongs to the COPG family.
CC -!- SIMILARITY: Contains 4 HEAT repeats.
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DR EMBL; AB047846; BAB17657.1; -; mRNA.
DR EMBL; AF100756; AAD43020.1; -; mRNA.
DR EMBL; AK001724; BAG50968.1; -; mRNA.
DR EMBL; AK291693; BAF84382.1; -; mRNA.
DR EMBL; CH471052; EAW79267.1; -; Genomic_DNA.
DR EMBL; BC066650; AAH66650.1; -; mRNA.
DR RefSeq; NP_057212.1; NM_016128.3.
DR UniGene; Hs.518250; -.
DR PDB; 1R4X; X-ray; 1.90 A; A=608-874.
DR PDBsum; 1R4X; -.
DR ProteinModelPortal; Q9Y678; -.
DR SMR; Q9Y678; 20-311, 608-873.
DR DIP; DIP-29872N; -.
DR IntAct; Q9Y678; 14.
DR MINT; MINT-4657598; -.
DR STRING; 9606.ENSP00000325002; -.
DR PhosphoSite; Q9Y678; -.
DR DMDM; 12229771; -.
DR PaxDb; Q9Y678; -.
DR PeptideAtlas; Q9Y678; -.
DR PRIDE; Q9Y678; -.
DR Ensembl; ENST00000314797; ENSP00000325002; ENSG00000181789.
DR GeneID; 22820; -.
DR KEGG; hsa:22820; -.
DR UCSC; uc003els.3; human.
DR CTD; 22820; -.
DR GeneCards; GC03P128970; -.
DR HGNC; HGNC:2236; COPG1.
DR HPA; HPA037867; -.
DR neXtProt; NX_Q9Y678; -.
DR PharmGKB; PA26752; -.
DR eggNOG; COG5240; -.
DR HOGENOM; HOG000184434; -.
DR HOVERGEN; HBG004368; -.
DR InParanoid; Q9Y678; -.
DR KO; K17267; -.
DR OMA; EYVVRCT; -.
DR OrthoDB; EOG75XGK5; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; COPG1; human.
DR EvolutionaryTrace; Q9Y678; -.
DR GeneWiki; COPG; -.
DR GenomeRNAi; 22820; -.
DR NextBio; 43212; -.
DR PRO; PR:Q9Y678; -.
DR ArrayExpress; Q9Y678; -.
DR Bgee; Q9Y678; -.
DR CleanEx; HS_COPG; -.
DR Genevestigator; Q9Y678; -.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
DR GO; GO:0051683; P:establishment of Golgi localization; ISS:BHF-UCL.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072384; P:organelle transport along microtubule; ISS:BHF-UCL.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1480; -; 1.
DR Gene3D; 3.30.310.30; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR015873; Clathrin_a/coatomer_app_sub_C.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
DR InterPro; IPR017106; Coatomer_gsu.
DR InterPro; IPR013040; Coatomer_gsu_app_Ig-like-sub.
DR PANTHER; PTHR10261; PTHR10261; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF08752; COP-gamma_platf; 1.
DR PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW ER-Golgi transport; Golgi apparatus; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1 874 Coatomer subunit gamma-1.
FT /FTId=PRO_0000193858.
FT REPEAT 64 101 HEAT 1.
FT REPEAT 283 320 HEAT 2.
FT REPEAT 322 355 HEAT 3.
FT REPEAT 356 392 HEAT 4.
FT REGION 609 874 Interaction with ZNF289/ARFGAP2.
FT VARIANT 681 681 M -> T (in dbSNP:rs15648).
FT /FTId=VAR_054039.
FT MUTAGEN 776 776 W->S: Loss of interaction with
FT ZNF289/ARFGAP2.
FT CONFLICT 622 622 E -> V (in Ref. 3; BAG50968).
FT CONFLICT 786 786 E -> G (in Ref. 3; BAG50968).
FT CONFLICT 842 842 V -> M (in Ref. 3; BAG50968).
FT CONFLICT 854 854 M -> T (in Ref. 3; BAF84382/BAG50968).
FT HELIX 609 618
FT HELIX 621 623
FT STRAND 644 654
FT STRAND 656 667
FT STRAND 672 686
FT STRAND 688 693
FT STRAND 695 698
FT STRAND 704 711
FT STRAND 714 716
FT STRAND 722 735
FT TURN 737 739
FT STRAND 747 752
FT STRAND 756 758
FT HELIX 760 763
FT STRAND 764 766
FT HELIX 772 779
FT STRAND 785 791
FT HELIX 797 808
FT TURN 814 817
FT STRAND 824 834
FT TURN 835 837
FT STRAND 838 862
FT HELIX 863 872
SQ SEQUENCE 874 AA; 97718 MW; A2FAB492C598EC98 CRC64;
MLKKFDKKDE ESGGGSNPFQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH
LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE DVIIVTSSLT KDMTGKEDNY
RGPAVRALCQ ITDSTMLQAI ERYMKQAIVD KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE
AQEAASSDNI MVQYHALGLL YHVRKNDRLA VNKMISKVTR HGLKSPFAYC MMIRVASKQL
EEEDGSRDSP LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDSNRSI ATLAITTLLK TGSESSIDRL
MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF LFTMLREEGG FEYKRAIVDC
IISIIEENSE SKETGLSHLC EFIEDCEFTV LATRILHLLG QEGPKTTNPS KYIRFIYNRV
VLEHEEVRAG AVSALAKFGA QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK
ALNAGYILNG LTVSIPGLER ALQQYTLEPS EKPFDLKSVP LATAPMAEQR TESTPITAVK
QPEKVAATRQ EIFQEQLAAV PEFRGLGPLF KSSPEPVALT ESETEYVIRC TKHTFTNHMV
FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL CYVPARSLPY NQPGTCYTLV ALPKEDPTAV
ACTFSCMMKF TVKDCDPTTG ETDDEGYEDE YVLEDLEVTV ADHIQKVMKL NFEAAWDEVG
DEFEKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP DNKNTHTLLL AGVFRGGHDI
LVRSRLLLLD TVTMQVTARS LEELPVDIIL ASVG
//
ID COPG1_HUMAN Reviewed; 874 AA.
AC Q9Y678; A8K6M8; B3KMF6; Q54AC4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Coatomer subunit gamma-1;
DE AltName: Full=Gamma-1-coat protein;
DE Short=Gamma-1-COP;
GN Name=COPG1; Synonyms=COPG;
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], INTERACTION WITH COPB1 AND TMED10, AND
RP SUBCELLULAR LOCATION.
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].
RC TISSUE=Pituitary;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [6]
RP FUNCTION, AND INTERACTION WITH EGFR.
RX PubMed=20674546; DOI=10.1016/j.bbrc.2010.07.096;
RA Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C.;
RT "COPI-mediated retrograde trafficking from the Golgi to the ER
RT regulates EGFR nuclear transport.";
RL Biochem. Biophys. Res. Commun. 399:498-504(2010).
RN [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 608-874, INTERACTION WITH
RP ZNF289, AND MUTAGENESIS OF TRP-776.
RX PubMed=14690497; DOI=10.1111/j.1600-0854.2004.00158.x;
RA Watson P.J., Frigerio G., Collins B.M., Duden R., Owen D.J.;
RT "Gamma-COP appendage domain -- structure and function.";
RL Traffic 5:79-88(2004).
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.
CC Required for limiting lipid storage in lipid droplets. Involved in
CC lipid homeostasis by regulating the presence of perilipin family
CC members PLIN2 and PLIN3 at the lipid droplet surface and promoting
CC the association of adipocyte triglyceride lipase (PNPLA2) with the
CC lipid droplet surface to mediate lipolysis (By similarity).
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC beta, beta', gamma, delta, epsilon and zeta subunits. Interacts
CC with ZNF289/ARFGAP2 through its C-terminal appendage domain.
CC Interacts with EGFR upon EGF treatment; interaction is essential
CC for regulation of EGF-dependent nuclear transport of EGFR by
CC retrograde trafficking from the Golgi to the ER. Interacts with
CC COPB1. Interacts with TMED10 (via C-terminus). Interacts with
CC TMED2, TMED3, TMED7 and TMED9.
CC -!- INTERACTION:
CC Q92538:GBF1; NbExp=2; IntAct=EBI-1049127, EBI-359050;
CC Q9NTJ5:SACM1L; NbExp=3; IntAct=EBI-1049127, EBI-3917235;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cytoplasmic
CC vesicle, COPI-coated vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side (By similarity). Note=The coatomer is
CC cytoplasmic or polymerized on the cytoplasmic side of the Golgi,
CC as well as on the vesicles/buds originating from it (By
CC similarity).
CC -!- SIMILARITY: Belongs to the COPG family.
CC -!- SIMILARITY: Contains 4 HEAT repeats.
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DR EMBL; AB047846; BAB17657.1; -; mRNA.
DR EMBL; AF100756; AAD43020.1; -; mRNA.
DR EMBL; AK001724; BAG50968.1; -; mRNA.
DR EMBL; AK291693; BAF84382.1; -; mRNA.
DR EMBL; CH471052; EAW79267.1; -; Genomic_DNA.
DR EMBL; BC066650; AAH66650.1; -; mRNA.
DR RefSeq; NP_057212.1; NM_016128.3.
DR UniGene; Hs.518250; -.
DR PDB; 1R4X; X-ray; 1.90 A; A=608-874.
DR PDBsum; 1R4X; -.
DR ProteinModelPortal; Q9Y678; -.
DR SMR; Q9Y678; 20-311, 608-873.
DR DIP; DIP-29872N; -.
DR IntAct; Q9Y678; 14.
DR MINT; MINT-4657598; -.
DR STRING; 9606.ENSP00000325002; -.
DR PhosphoSite; Q9Y678; -.
DR DMDM; 12229771; -.
DR PaxDb; Q9Y678; -.
DR PeptideAtlas; Q9Y678; -.
DR PRIDE; Q9Y678; -.
DR Ensembl; ENST00000314797; ENSP00000325002; ENSG00000181789.
DR GeneID; 22820; -.
DR KEGG; hsa:22820; -.
DR UCSC; uc003els.3; human.
DR CTD; 22820; -.
DR GeneCards; GC03P128970; -.
DR HGNC; HGNC:2236; COPG1.
DR HPA; HPA037867; -.
DR neXtProt; NX_Q9Y678; -.
DR PharmGKB; PA26752; -.
DR eggNOG; COG5240; -.
DR HOGENOM; HOG000184434; -.
DR HOVERGEN; HBG004368; -.
DR InParanoid; Q9Y678; -.
DR KO; K17267; -.
DR OMA; EYVVRCT; -.
DR OrthoDB; EOG75XGK5; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; COPG1; human.
DR EvolutionaryTrace; Q9Y678; -.
DR GeneWiki; COPG; -.
DR GenomeRNAi; 22820; -.
DR NextBio; 43212; -.
DR PRO; PR:Q9Y678; -.
DR ArrayExpress; Q9Y678; -.
DR Bgee; Q9Y678; -.
DR CleanEx; HS_COPG; -.
DR Genevestigator; Q9Y678; -.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
DR GO; GO:0051683; P:establishment of Golgi localization; ISS:BHF-UCL.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072384; P:organelle transport along microtubule; ISS:BHF-UCL.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1480; -; 1.
DR Gene3D; 3.30.310.30; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR015873; Clathrin_a/coatomer_app_sub_C.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
DR InterPro; IPR017106; Coatomer_gsu.
DR InterPro; IPR013040; Coatomer_gsu_app_Ig-like-sub.
DR PANTHER; PTHR10261; PTHR10261; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF08752; COP-gamma_platf; 1.
DR PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW ER-Golgi transport; Golgi apparatus; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1 874 Coatomer subunit gamma-1.
FT /FTId=PRO_0000193858.
FT REPEAT 64 101 HEAT 1.
FT REPEAT 283 320 HEAT 2.
FT REPEAT 322 355 HEAT 3.
FT REPEAT 356 392 HEAT 4.
FT REGION 609 874 Interaction with ZNF289/ARFGAP2.
FT VARIANT 681 681 M -> T (in dbSNP:rs15648).
FT /FTId=VAR_054039.
FT MUTAGEN 776 776 W->S: Loss of interaction with
FT ZNF289/ARFGAP2.
FT CONFLICT 622 622 E -> V (in Ref. 3; BAG50968).
FT CONFLICT 786 786 E -> G (in Ref. 3; BAG50968).
FT CONFLICT 842 842 V -> M (in Ref. 3; BAG50968).
FT CONFLICT 854 854 M -> T (in Ref. 3; BAF84382/BAG50968).
FT HELIX 609 618
FT HELIX 621 623
FT STRAND 644 654
FT STRAND 656 667
FT STRAND 672 686
FT STRAND 688 693
FT STRAND 695 698
FT STRAND 704 711
FT STRAND 714 716
FT STRAND 722 735
FT TURN 737 739
FT STRAND 747 752
FT STRAND 756 758
FT HELIX 760 763
FT STRAND 764 766
FT HELIX 772 779
FT STRAND 785 791
FT HELIX 797 808
FT TURN 814 817
FT STRAND 824 834
FT TURN 835 837
FT STRAND 838 862
FT HELIX 863 872
SQ SEQUENCE 874 AA; 97718 MW; A2FAB492C598EC98 CRC64;
MLKKFDKKDE ESGGGSNPFQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH
LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE DVIIVTSSLT KDMTGKEDNY
RGPAVRALCQ ITDSTMLQAI ERYMKQAIVD KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE
AQEAASSDNI MVQYHALGLL YHVRKNDRLA VNKMISKVTR HGLKSPFAYC MMIRVASKQL
EEEDGSRDSP LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDSNRSI ATLAITTLLK TGSESSIDRL
MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF LFTMLREEGG FEYKRAIVDC
IISIIEENSE SKETGLSHLC EFIEDCEFTV LATRILHLLG QEGPKTTNPS KYIRFIYNRV
VLEHEEVRAG AVSALAKFGA QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK
ALNAGYILNG LTVSIPGLER ALQQYTLEPS EKPFDLKSVP LATAPMAEQR TESTPITAVK
QPEKVAATRQ EIFQEQLAAV PEFRGLGPLF KSSPEPVALT ESETEYVIRC TKHTFTNHMV
FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL CYVPARSLPY NQPGTCYTLV ALPKEDPTAV
ACTFSCMMKF TVKDCDPTTG ETDDEGYEDE YVLEDLEVTV ADHIQKVMKL NFEAAWDEVG
DEFEKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP DNKNTHTLLL AGVFRGGHDI
LVRSRLLLLD TVTMQVTARS LEELPVDIIL ASVG
//