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   24-JAN-2024, entry version 162.
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;
RC   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,
RC   Pancreas, 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   EMDB; EMD-2985; -.
DR   EMDB; EMD-2986; -.
DR   EMDB; EMD-2987; -.
DR   EMDB; EMD-2988; -.
DR   EMDB; EMD-2989; -.
DR   EMDB; EMD-3720; -.
DR   EMDB; EMD-3721; -.
DR   EMDB; EMD-3722; -.
DR   EMDB; EMD-3723; -.
DR   EMDB; EMD-3724; -.
DR   SMR; Q9QZE5; -.
DR   BioGRID; 207587; 10.
DR   CORUM; Q9QZE5; -.
DR   STRING; 10090.ENSMUSP00000109237; -.
DR   GlyGen; Q9QZE5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9QZE5; -.
DR   PhosphoSitePlus; Q9QZE5; -.
DR   SwissPalm; Q9QZE5; -.
DR   EPD; Q9QZE5; -.
DR   jPOST; Q9QZE5; -.
DR   MaxQB; Q9QZE5; -.
DR   PaxDb; 10090-ENSMUSP00000109237; -.
DR   PeptideAtlas; Q9QZE5; -.
DR   ProteomicsDB; 285248; -.
DR   Pumba; Q9QZE5; -.
DR   Antibodypedia; 46660; 169 antibodies from 26 providers.
DR   DNASU; 54161; -.
DR   Ensembl; ENSMUST00000113607.10; ENSMUSP00000109237.4; ENSMUSG00000030058.18.
DR   GeneID; 54161; -.
DR   KEGG; mmu:54161; -.
DR   UCSC; uc009cug.1; mouse.
DR   AGR; MGI:1858696; -.
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; 5260816at2759; -.
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; 26 hits in 77 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 284 other cell types or tissues.
DR   ExpressionAtlas; Q9QZE5; baseline and differential.
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; 2.60.40.1480; Coatomer, gamma subunit, appendage domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   Gene3D; 3.30.310.10; TATA-Binding Protein; 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; COATOMER SUBUNIT GAMMA; 1.
DR   PANTHER; PTHR10261:SF3; COATOMER SUBUNIT GAMMA-1; 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; ARM repeat; 1.
DR   SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
DR   SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1.
DR   Genevisible; Q9QZE5; MM.
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
//