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COPG_DROPS
ID   COPG_DROPS              Reviewed;         878 AA.
AC   Q29AE5;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000250|UniProtKB:Q8I0G5};
DE   AltName: Full=Gamma-coat protein {ECO:0000250|UniProtKB:Q8I0G5};
DE            Short=Gamma-COP {ECO:0000250|UniProtKB:Q8I0G5};
GN   Name=gammaCop {ECO:0000250|UniProtKB:Q8I0G5}; ORFNames=GA13624;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1] {ECO:0000312|EMBL:EAL27405.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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       Required for limiting lipid storage in lipid droplets. Involved in the
CC       expansion of luminal extracellular matrices and apical membrane during
CC       tubulogenesis. Required in the tracheal epithelium for luminal protein
CC       secretion and diametric tube growth. In salivary glands, required for
CC       deposition of O-glycans and luminal extracellular matrix assembly.
CC       Required for epidermal morphogenesis and cuticle development (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits.
CC       {ECO:0000250|UniProtKB:P32074, ECO:0000250|UniProtKB:P53622}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32074,
CC       ECO:0000250|UniProtKB:P53622, ECO:0000250|UniProtKB:Q8I0G5}. Golgi
CC       apparatus membrane {ECO:0000250|UniProtKB:P32074,
CC       ECO:0000250|UniProtKB:P53622, ECO:0000250|UniProtKB:Q8I0G5}; Peripheral
CC       membrane protein {ECO:0000250|UniProtKB:P32074,
CC       ECO:0000250|UniProtKB:P53622, ECO:0000250|UniProtKB:Q8I0G5};
CC       Cytoplasmic side {ECO:0000250|UniProtKB:P32074,
CC       ECO:0000250|UniProtKB:P53622, ECO:0000250|UniProtKB:Q8I0G5}.
CC       Cytoplasmic vesicle, COPI-coated vesicle membrane
CC       {ECO:0000250|UniProtKB:P32074, ECO:0000250|UniProtKB:P53622,
CC       ECO:0000250|UniProtKB:Q8I0G5}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P32074, ECO:0000250|UniProtKB:P53622,
CC       ECO:0000250|UniProtKB:Q8I0G5}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P32074, ECO:0000250|UniProtKB:P53622,
CC       ECO:0000250|UniProtKB:Q8I0G5}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P32074, ECO:0000250|UniProtKB:P53622,
CC       ECO:0000250|UniProtKB:Q8I0G5}. 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. {ECO:0000250|UniProtKB:P32074,
CC       ECO:0000250|UniProtKB:P53622, ECO:0000250|UniProtKB:Q8I0G5}.
CC   -!- SIMILARITY: Belongs to the COPG family. {ECO:0000255}.
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DR   EMBL; CM000070; EAL27405.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q29AE5; -.
DR   SMR; Q29AE5; -.
DR   STRING; 7237.FBpp0282417; -.
DR   eggNOG; KOG1078; Eukaryota.
DR   HOGENOM; CLU_010353_2_0_1; -.
DR   InParanoid; Q29AE5; -.
DR   OMA; YMTQYHA; -.
DR   PhylomeDB; Q29AE5; -.
DR   Proteomes; UP000001819; Genome assembly.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW   Golgi apparatus; Membrane; Protein transport; Reference proteome; Repeat;
KW   Transport.
FT   CHAIN           1..878
FT                   /note="Coatomer subunit gamma"
FT                   /id="PRO_0000405328"
FT   REPEAT          64..101
FT                   /note="HEAT 1"
FT   REPEAT          287..324
FT                   /note="HEAT 2"
FT   REPEAT          326..359
FT                   /note="HEAT 3"
FT   REPEAT          360..396
FT                   /note="HEAT 4"
FT   REPEAT          399..434
FT                   /note="HEAT 5"
FT   REPEAT          471..508
FT                   /note="HEAT 6"
SQ   SEQUENCE   878 AA;  97357 MW;  B25C075F7AEBECC0 CRC64;
     MGSFRRDKEE EDDGPTNAYQ NLEKTSVLQE TRTFNETPVN ARKCIHILTK ILYLINQGET
     LVPREATDCF FAMTKLFQSK DVVLRRMVYL GIKELSSVAE DVIIVTSSLT KDMTGKEDLY
     RAAAIRALCS ITDHTMLQAV ERYMKQCIVD KNAAVSCAAL VSSLRLATTA GDVVKRWANE
     AQEAMNSDNI MVQYHALGLL YHIRKSDRLA VSKLVNKLTR SSLKSPYAVC MLIRIACKLI
     EEEDIPSEEL SDSPLFTFIE TCLRHKSEMV IYEAAHAIVN LKNTNHRMLS PAFSILQLFC
     SSPKATLRFA AVRTLNKVAM THPAAVTTCN LDLEGLITDS NRSVATLAIT TLLKTGAESS
     VERLMKQIST FVAEISDEFK IVVVQAICAL CTKYPRKHTV LMNFLSGMLR EEGGLEYKTS
     IVDTIITIIE ENADAKESGL SHLCEFIEDC EHVSLAVRIL HLMGKEGPFA ATPSKYIRFI
     YNRVILESPI VRAAAVTALS QFGASCPALL TNILVLLGRC QMDPDDEVRD RATYYLTILN
     TERADLYKNY IIERENCSLA LLEKALVDHL NGDLEKRFDI SVVPKAAAVV RAEISNDVML
     VTSAPRPPKI TREEESASRL AQLPGIQVLG PVHRSTAPIQ LTESETEYTV QCIKHIFGQH
     VVFQFDCLNT LSDQFLENVR VELTLPEGFT TRAVVPCPKL PYNELQTTYV IVEFPPDAGS
     SIATFGATLR FVVKDCDPNT GEPDSEEGYD DEYMLEDMEI TVADQIQKSK KNNFQVAWDA
     ADSEEWLQAE DTFVLSAVTT LQDAVNTIMK ILGLGSANLS EKVPEGTHLH TLLCSGTFRG
     GAEVLVRAKL ALSEGVTLNL TVRSTDQDVA ELITAAIG
 
 
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