COPG1_MOUSE
ID COPG1_MOUSE Reviewed; 874 AA.
AC Q9QZE5; Q3U9F4; Q8BP96; Q8R1A7; Q922C6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 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=11018518; DOI=10.1016/s0014-5793(00)02033-0;
RA Hahn Y., Lee Y.J., Yun J.H., Yang S.K., Park C.W., Mita K., Huh T.-L.,
RA Rhee M., Chung J.H.;
RT "Duplication of genes encoding non-clathrin coat protein gamma-COP in
RT vertebrate, insect and plant evolution.";
RL FEBS Lett. 482:31-36(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Embryo, Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and 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 [4]
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 [5]
RP FUNCTION.
RX PubMed=19067489; DOI=10.1371/journal.pbio.0060292;
RA Beller M., Sztalryd C., Southall N., Bell M., Jackle H., Auld D.S.,
RA Oliver B.;
RT "COPI complex is a regulator of lipid homeostasis.";
RL PLoS Biol. 6:E292-E292(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 In mammals, the coatomer can only be recruited by membranes associated
CC to ADP-ribosylation factors (ARFs), which are small GTP-binding
CC proteins; the complex also influences the Golgi structural integrity,
CC as well as the processing, activity, and endocytic recycling of LDL
CC receptors (By similarity). Required for limiting lipid storage in lipid
CC droplets. Involved in lipid homeostasis by regulating the presence of
CC perilipin family members PLIN2 and PLIN3 at the lipid droplet surface
CC and promoting the association of adipocyte triglyceride lipase (PNPLA2)
CC with the lipid droplet surface to mediate lipolysis. {ECO:0000250,
CC ECO:0000269|PubMed:19067489}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Interacts with
CC ZNF289/ARFGAP2 through its C-terminal appendage domain (By similarity).
CC Interacts with EGFR upon EGF treatment; interaction is essential for
CC regulation of EGF-dependent nuclear transport of EGFR by retrograde
CC trafficking from the Golgi to the ER (By similarity). Interacts with
CC COPB1 (By similarity). Interacts with TMED10 (via C-terminus).
CC Interacts with TMED2, TMED3, TMED7 and TMED9 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}.
CC Golgi apparatus membrane {ECO:0000269|PubMed:17360540}; Peripheral
CC membrane protein {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. Predominantly located in the cis-
CC Golgi apparatus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36811.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF187079; AAF01325.1; -; mRNA.
DR EMBL; AK049417; BAC33743.1; -; mRNA.
DR EMBL; AK077461; BAC36811.1; ALT_FRAME; mRNA.
DR EMBL; AK147895; BAE28212.1; -; mRNA.
DR EMBL; AK151284; BAE30269.1; -; mRNA.
DR EMBL; AK151816; BAE30713.1; -; mRNA.
DR EMBL; AK153142; BAE31753.1; -; mRNA.
DR EMBL; AK164280; BAE37716.1; -; mRNA.
DR EMBL; AK169256; BAE41019.1; -; mRNA.
DR EMBL; AK171950; BAE42743.1; -; mRNA.
DR EMBL; AK172519; BAE43046.1; -; mRNA.
DR EMBL; BC008553; AAH08553.1; -; mRNA.
DR EMBL; BC024686; AAH24686.1; -; mRNA.
DR EMBL; BC024896; AAH24896.1; -; mRNA.
DR CCDS; CCDS39549.1; -.
DR RefSeq; NP_059505.1; NM_017477.2.
DR PDB; 5A1U; EM; 13.00 A; E=1-874.
DR PDB; 5A1V; EM; 21.00 A; E/M/V=1-874.
DR PDB; 5A1W; EM; 18.00 A; E=1-874.
DR PDB; 5A1X; EM; 23.00 A; E/M=1-874.
DR PDB; 5A1Y; EM; 21.00 A; E/M/V=1-874.
DR PDB; 5NZR; EM; 9.20 A; G/K=1-874.
DR PDB; 5NZS; EM; 10.10 A; G/K=1-874.
DR PDB; 5NZT; EM; 17.00 A; G/K=1-874.
DR PDB; 5NZU; EM; 15.00 A; G/K=1-874.
DR PDB; 5NZV; EM; 17.30 A; G/K/Q=1-874.
DR PDBsum; 5A1U; -.
DR PDBsum; 5A1V; -.
DR PDBsum; 5A1W; -.
DR PDBsum; 5A1X; -.
DR PDBsum; 5A1Y; -.
DR PDBsum; 5NZR; -.
DR PDBsum; 5NZS; -.
DR PDBsum; 5NZT; -.
DR PDBsum; 5NZU; -.
DR PDBsum; 5NZV; -.
DR AlphaFoldDB; Q9QZE5; -.
DR SMR; Q9QZE5; -.
DR BioGRID; 207587; 9.
DR CORUM; Q9QZE5; -.
DR STRING; 10090.ENSMUSP00000109237; -.
DR iPTMnet; Q9QZE5; -.
DR PhosphoSitePlus; Q9QZE5; -.
DR SwissPalm; Q9QZE5; -.
DR EPD; Q9QZE5; -.
DR jPOST; Q9QZE5; -.
DR MaxQB; Q9QZE5; -.
DR PaxDb; Q9QZE5; -.
DR PeptideAtlas; Q9QZE5; -.
DR PRIDE; Q9QZE5; -.
DR ProteomicsDB; 285248; -.
DR Antibodypedia; 46660; 150 antibodies from 26 providers.
DR DNASU; 54161; -.
DR Ensembl; ENSMUST00000113607; ENSMUSP00000109237; ENSMUSG00000030058.
DR GeneID; 54161; -.
DR KEGG; mmu:54161; -.
DR UCSC; uc009cug.1; mouse.
DR CTD; 22820; -.
DR MGI; MGI:1858696; Copg1.
DR VEuPathDB; HostDB:ENSMUSG00000030058; -.
DR eggNOG; KOG1078; Eukaryota.
DR GeneTree; ENSGT00390000016313; -.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; Q9QZE5; -.
DR OMA; RTIVECM; -.
DR OrthoDB; 255234at2759; -.
DR PhylomeDB; Q9QZE5; -.
DR TreeFam; TF300324; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 54161; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Copg1; mouse.
DR PRO; PR:Q9QZE5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QZE5; protein.
DR Bgee; ENSMUSG00000030058; Expressed in embryonic brain and 280 other tissues.
DR ExpressionAtlas; Q9QZE5; baseline and differential.
DR Genevisible; Q9QZE5; MM.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0051683; P:establishment of Golgi localization; ISO:MGI.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072384; P:organelle transport along microtubule; ISO:MGI.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 2.60.40.1480; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR032154; Coatomer_g_Cpla.
DR InterPro; IPR017106; Coatomer_gsu.
DR InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR InterPro; IPR037067; Coatomer_gsu_app_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10261; PTHR10261; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF16381; Coatomer_g_Cpla; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..874
FT /note="Coatomer subunit gamma-1"
FT /id="PRO_0000304939"
FT REPEAT 64..101
FT /note="HEAT 1"
FT REPEAT 283..320
FT /note="HEAT 2"
FT REPEAT 322..355
FT /note="HEAT 3"
FT REPEAT 356..392
FT /note="HEAT 4"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..874
FT /note="Interaction with ZNF289/ARFGAP2"
FT /evidence="ECO:0000250"
FT MOD_RES 594
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y678"
FT CONFLICT 811
FT /note="H -> P (in Ref. 3; AAH24896)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="L -> F (in Ref. 2; BAE31753/BAE30713/BAE30269)"
FT /evidence="ECO:0000305"
FT CONFLICT 843
FT /note="R -> H (in Ref. 2; BAC36811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 874 AA; 97513 MW; CAF3201AD1118728 CRC64;
MLKKFDKKDE ESGGGSNPLQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH
LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE DVIIVTSSLT KDMTGKEDNY
RGPAVRALCQ ITDSTMLQAV ERYMKQAIVD KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE
AQEAASSDNI MVQYHALGLL YHVRKNDRLA VSKMISKFTR HGLKSPFAYC MMIRVASKQL
EEEDGSRDSP LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDSNRSI ATLAITTLLK TGSESSIDRL
MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF LFTMLREEGG FEYKRAIVDC
IISIIEENSE SKETGLSHLC EFIEDCEFTV LATRILHLLG QEGPKTNNPS KYIRFIYNRV
VLEHEEVRAG AVSALAKFGA QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK
ALNAGYILNG LTVSIPGLEK ALQQYTLEPS EKPFDLKSVP LATTPMAEQR PESTATAAVK
QPEKVAATRQ EIFQEQLAAV PEFQGLGPLF KSSPEPVALT ESETEYVIRC TKHTFSDHLV
FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL SYVPARSLPY NQPGTCYTLV ALPTEDPTAV
ACTFSCVMKF TVKDCDPNTG EIDEEGYEDE YVLEDLEVTV ADHIQKVMKV NFEAAWDEVG
DEFEKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP ENKNTHTLLL AGVFRGGHDI
LVRSRLLLLD TVTMQVTARS SEELPVDIIL ASVG
