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Coatomer subunit gamma-1 (Gamma-1-coat protein) (Gamma-1-COP)

 COPG1_HUMAN             Reviewed;         874 AA.
Q9Y678; A8K6M8; B3KMF6; Q54AC4;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
10-OCT-2018, entry version 159.
RecName: Full=Coatomer subunit gamma-1;
AltName: Full=Gamma-1-coat protein;
Short=Gamma-1-COP;
Name=COPG1; Synonyms=COPG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH COPB1 AND TMED10, AND
SUBCELLULAR LOCATION.
PubMed=11056392; DOI=10.1093/oxfordjournals.jbchem.a022817;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, AND INTERACTION WITH EGFR.
PubMed=20674546; DOI=10.1016/j.bbrc.2010.07.096;
Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C.;
"COPI-mediated retrograde trafficking from the Golgi to the ER
regulates EGFR nuclear transport.";
Biochem. Biophys. Res. Commun. 399:498-504(2010).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-594, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 608-874, INTERACTION WITH
ZNF289, AND MUTAGENESIS OF TRP-776.
PubMed=14690497; DOI=10.1111/j.1600-0854.2004.00158.x;
Watson P.J., Frigerio G., Collins B.M., Duden R., Owen D.J.;
"Gamma-COP appendage domain -- structure and function.";
Traffic 5:79-88(2004).
-!- FUNCTION: The coatomer is a cytosolic protein complex that binds
to dilysine motifs and reversibly associates with Golgi non-
clathrin-coated vesicles, which further mediate biosynthetic
protein transport from the ER, via the Golgi up to the trans Golgi
network. Coatomer complex is required for budding from Golgi
membranes, and is essential for the retrograde Golgi-to-ER
transport of dilysine-tagged proteins. In mammals, the coatomer
can only be recruited by membranes associated to ADP-ribosylation
factors (ARFs), which are small GTP-binding proteins; the complex
also influences the Golgi structural integrity, as well as the
processing, activity, and endocytic recycling of LDL receptors.
Required for limiting lipid storage in lipid droplets. Involved in
lipid homeostasis by regulating the presence of perilipin family
members PLIN2 and PLIN3 at the lipid droplet surface and promoting
the association of adipocyte triglyceride lipase (PNPLA2) with the
lipid droplet surface to mediate lipolysis (By similarity).
{ECO:0000250, ECO:0000269|PubMed:20674546}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits. Interacts
with ZNF289/ARFGAP2 through its C-terminal appendage domain.
Interacts with EGFR upon EGF treatment; interaction is essential
for regulation of EGF-dependent nuclear transport of EGFR by
retrograde trafficking from the Golgi to the ER. Interacts with
COPB1. Interacts with TMED10 (via C-terminus). Interacts with
TMED2, TMED3, TMED7 and TMED9. {ECO:0000269|PubMed:11056392,
ECO:0000269|PubMed:14690497, ECO:0000269|PubMed:20674546}.
-!- INTERACTION:
Q92538:GBF1; NbExp=2; IntAct=EBI-1049127, EBI-359050;
Q96RS6:NUDCD1; NbExp=2; IntAct=EBI-1049127, EBI-2512429;
Q9NTJ5:SACM1L; NbExp=3; IntAct=EBI-1049127, EBI-3917235;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11056392}.
Golgi apparatus membrane {ECO:0000269|PubMed:11056392}; Peripheral
membrane protein {ECO:0000269|PubMed:11056392}; Cytoplasmic side
{ECO:0000269|PubMed:11056392}. Cytoplasmic vesicle, COPI-coated
vesicle membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer
is cytoplasmic or polymerized on the cytoplasmic side of the
Golgi, as well as on the vesicles/buds originating from it.
Predominantly located in the cis-Golgi apparatus. {ECO:0000250}.
-!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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EMBL; AB047846; BAB17657.1; -; mRNA.
EMBL; AF100756; AAD43020.1; -; mRNA.
EMBL; AK001724; BAG50968.1; -; mRNA.
EMBL; AK291693; BAF84382.1; -; mRNA.
EMBL; CH471052; EAW79267.1; -; Genomic_DNA.
EMBL; BC066650; AAH66650.1; -; mRNA.
CCDS; CCDS33851.1; -.
RefSeq; NP_057212.1; NM_016128.3.
UniGene; Hs.518250; -.
PDB; 1R4X; X-ray; 1.90 A; A=608-874.
PDBsum; 1R4X; -.
ProteinModelPortal; Q9Y678; -.
SMR; Q9Y678; -.
BioGrid; 116496; 82.
DIP; DIP-29872N; -.
IntAct; Q9Y678; 44.
MINT; Q9Y678; -.
STRING; 9606.ENSP00000325002; -.
DrugBank; DB03963; S-(Dimethylarsenic)Cysteine.
iPTMnet; Q9Y678; -.
PhosphoSitePlus; Q9Y678; -.
SwissPalm; Q9Y678; -.
BioMuta; COPG1; -.
DMDM; 12229771; -.
EPD; Q9Y678; -.
MaxQB; Q9Y678; -.
PaxDb; Q9Y678; -.
PeptideAtlas; Q9Y678; -.
PRIDE; Q9Y678; -.
ProteomicsDB; 86615; -.
Ensembl; ENST00000314797; ENSP00000325002; ENSG00000181789.
GeneID; 22820; -.
KEGG; hsa:22820; -.
UCSC; uc003els.4; human.
CTD; 22820; -.
DisGeNET; 22820; -.
EuPathDB; HostDB:ENSG00000181789.14; -.
GeneCards; COPG1; -.
HGNC; HGNC:2236; COPG1.
HPA; HPA037866; -.
HPA; HPA037867; -.
HPA; HPA045712; -.
MIM; 615525; gene.
neXtProt; NX_Q9Y678; -.
OpenTargets; ENSG00000181789; -.
PharmGKB; PA26752; -.
eggNOG; KOG1078; Eukaryota.
eggNOG; COG5240; LUCA.
GeneTree; ENSGT00390000016313; -.
HOGENOM; HOG000184434; -.
HOVERGEN; HBG004368; -.
InParanoid; Q9Y678; -.
KO; K17267; -.
OMA; KSEMVNF; -.
OrthoDB; EOG091G0HWQ; -.
PhylomeDB; Q9Y678; -.
TreeFam; TF300324; -.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
ChiTaRS; COPG1; human.
EvolutionaryTrace; Q9Y678; -.
GeneWiki; COPG; -.
GenomeRNAi; 22820; -.
PRO; PR:Q9Y678; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000181789; Expressed in 224 organ(s), highest expression level in adenohypophysis.
CleanEx; HS_COPG; -.
ExpressionAtlas; Q9Y678; baseline and differential.
Genevisible; Q9Y678; HS.
GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; ISS:BHF-UCL.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0051683; P:establishment of Golgi localization; ISS:BHF-UCL.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0072384; P:organelle transport along microtubule; ISS:BHF-UCL.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
Gene3D; 1.25.10.10; -; 2.
Gene3D; 2.60.40.1480; -; 1.
Gene3D; 3.30.310.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR013041; Clathrin_app_Ig-like_sf.
InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
InterPro; IPR032154; Coatomer_g_Cpla.
InterPro; IPR017106; Coatomer_gsu.
InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
InterPro; IPR037067; Coatomer_gsu_app_sf.
InterPro; IPR012295; TBP_dom_sf.
PANTHER; PTHR10261; PTHR10261; 1.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF16381; Coatomer_g_Cpla; 1.
Pfam; PF08752; COP-gamma_platf; 1.
PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49348; SSF49348; 1.
SUPFAM; SSF55711; SSF55711; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Repeat;
Transport.
CHAIN 1 874 Coatomer subunit gamma-1.
/FTId=PRO_0000193858.
REPEAT 64 101 HEAT 1.
REPEAT 283 320 HEAT 2.
REPEAT 322 355 HEAT 3.
REPEAT 356 392 HEAT 4.
REGION 609 874 Interaction with ZNF289/ARFGAP2.
{ECO:0000269|PubMed:14690497}.
MOD_RES 594 594 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VARIANT 681 681 M -> T (in dbSNP:rs15648).
/FTId=VAR_054039.
MUTAGEN 776 776 W->S: Loss of interaction with
ZNF289/ARFGAP2.
{ECO:0000269|PubMed:14690497}.
CONFLICT 622 622 E -> V (in Ref. 3; BAG50968).
{ECO:0000305}.
CONFLICT 786 786 E -> G (in Ref. 3; BAG50968).
{ECO:0000305}.
CONFLICT 842 842 V -> M (in Ref. 3; BAG50968).
{ECO:0000305}.
CONFLICT 854 854 M -> T (in Ref. 3; BAF84382/BAG50968).
{ECO:0000305}.
HELIX 609 618 {ECO:0000244|PDB:1R4X}.
HELIX 621 623 {ECO:0000244|PDB:1R4X}.
STRAND 644 654 {ECO:0000244|PDB:1R4X}.
STRAND 656 667 {ECO:0000244|PDB:1R4X}.
STRAND 672 686 {ECO:0000244|PDB:1R4X}.
STRAND 688 693 {ECO:0000244|PDB:1R4X}.
STRAND 695 698 {ECO:0000244|PDB:1R4X}.
STRAND 704 711 {ECO:0000244|PDB:1R4X}.
STRAND 714 716 {ECO:0000244|PDB:1R4X}.
STRAND 722 735 {ECO:0000244|PDB:1R4X}.
TURN 737 739 {ECO:0000244|PDB:1R4X}.
STRAND 747 752 {ECO:0000244|PDB:1R4X}.
STRAND 756 758 {ECO:0000244|PDB:1R4X}.
HELIX 760 763 {ECO:0000244|PDB:1R4X}.
STRAND 764 766 {ECO:0000244|PDB:1R4X}.
HELIX 772 779 {ECO:0000244|PDB:1R4X}.
STRAND 785 791 {ECO:0000244|PDB:1R4X}.
HELIX 797 808 {ECO:0000244|PDB:1R4X}.
TURN 814 817 {ECO:0000244|PDB:1R4X}.
STRAND 824 834 {ECO:0000244|PDB:1R4X}.
TURN 835 837 {ECO:0000244|PDB:1R4X}.
STRAND 838 862 {ECO:0000244|PDB:1R4X}.
HELIX 863 872 {ECO:0000244|PDB:1R4X}.
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


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EIAAB06090 CACNG6,CACNG8,Homo sapiens,Human,Neuronal voltage-gated calcium channel gamma-8 subunit,TARP gamma-8,Transmembrane AMPAR regulatory protein gamma-8,Voltage-dependent calcium channel gamma-8 subunit


 

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