ID   COPG1_RAT               Reviewed;         874 AA.
AC   Q4AEF8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Fischer 344/DuCrj, and LEC/Crj;
RX   PubMed=15978772; DOI=10.1016/j.ygeno.2005.05.007;
RA   Tsuji A.B., Sugyo A., Ogiu T., Sagara M., Kimura T., Ishikawa A., Sudo H.,
RA   Ohtsuki M., Aburatani H., Imai T., Harada Y.N.;
RT   "Fine mapping of radiation susceptibility and gene expression analysis of
RT   LEC congenic rat lines.";
RL   Genomics 86:271-279(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [3]
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).
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. Required for limiting lipid storage in lipid droplets.
CC       Involved in lipid homeostasis by regulating the presence of perilipin
CC       family members PLIN2 and PLIN3 at the lipid droplet surface and
CC       promoting the association of adipocyte triglyceride lipase (PNPLA2)
CC       with the lipid droplet surface to mediate lipolysis (By similarity).
CC       {ECO:0000250}.
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:0000250}. Golgi apparatus
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is
CC       cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as
CC       well as on the vesicles/buds originating from it (By similarity). About
CC       70% of the COPG1-containing coatomers are found in the cis-Golgi
CC       apparatus. {ECO:0000250, ECO:0000269|PubMed:17360540}.
CC   -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR   EMBL; AB158425; BAE16997.1; -; mRNA.
DR   EMBL; AB158426; BAE16998.1; -; mRNA.
DR   EMBL; BC129074; AAI29075.1; -; mRNA.
DR   RefSeq; NP_001026992.1; NM_001031822.3.
DR   AlphaFoldDB; Q4AEF8; -.
DR   SMR; Q4AEF8; -.
DR   BioGRID; 255579; 3.
DR   IntAct; Q4AEF8; 4.
DR   MINT; Q4AEF8; -.
DR   STRING; 10116.ENSRNOP00000016137; -.
DR   iPTMnet; Q4AEF8; -.
DR   PhosphoSitePlus; Q4AEF8; -.
DR   SwissPalm; Q4AEF8; -.
DR   jPOST; Q4AEF8; -.
DR   PaxDb; Q4AEF8; -.
DR   PRIDE; Q4AEF8; -.
DR   GeneID; 297428; -.
DR   KEGG; rno:297428; -.
DR   CTD; 22820; -.
DR   RGD; 1565292; Copg1.
DR   VEuPathDB; HostDB:ENSRNOG00000010474; -.
DR   eggNOG; KOG1078; Eukaryota.
DR   HOGENOM; CLU_010353_2_0_1; -.
DR   InParanoid; Q4AEF8; -.
DR   OrthoDB; 255234at2759; -.
DR   PhylomeDB; Q4AEF8; -.
DR   TreeFam; TF300324; -.
DR   Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   PRO; PR:Q4AEF8; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000010474; Expressed in cerebellum and 19 other tissues.
DR   ExpressionAtlas; Q4AEF8; baseline and differential.
DR   Genevisible; Q4AEF8; RN.
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:0000139; C:Golgi membrane; IDA:BHF-UCL.
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; IMP:BHF-UCL.
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; IMP:BHF-UCL.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW   Transport.
FT   CHAIN           1..874
FT                   /note="Coatomer subunit gamma-1"
FT                   /id="PRO_0000304940"
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"
SQ   SEQUENCE   874 AA;  97614 MW;  A4C2AD19A74E7D63 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 LATTPMTEQR PESTSTAAVK
     QPEKVAATRQ EIFQEQLAAV PEFQGLGPLF KSSPEPVALT ESETEYVIRC TKHTFSDHLV
     FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL SYVPVRSLPY NQPGTCYTLV ALPKEDPTAV
     ACTFSCVMKF TVKDCDPNTG EIDEEGYEDE YVLEDLEVTV ADHIQKVMKV NFEAAWDEVG
     DEFEKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP ENKNTHTLLL AGVFRGGHDI
     LVRSRLLLLD TVTMQVTARS SEELPVDIIL ASVG