COPG_ANOGA
ID COPG_ANOGA Reviewed; 868 AA.
AC Q7PVF6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 25-MAY-2022, entry version 108.
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=AGAP009291;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000312|EMBL:EAA14827.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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 (By similarity). {ECO:0000250|UniProtKB:P32074,
CC ECO:0000250|UniProtKB:P53620, ECO:0000250|UniProtKB:P53622,
CC ECO:0000250|UniProtKB:Q8I0G5}.
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; AAAB01008984; EAA14827.2; -; Genomic_DNA.
DR RefSeq; XP_320089.2; XM_320089.4.
DR AlphaFoldDB; Q7PVF6; -.
DR SMR; Q7PVF6; -.
DR STRING; 7165.AGAP009291-PA; -.
DR PaxDb; Q7PVF6; -.
DR GeneID; 1280258; -.
DR KEGG; aga:AgaP_AGAP009291; -.
DR VEuPathDB; VectorBase:AGAP009291; -.
DR eggNOG; KOG1078; Eukaryota.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; Q7PVF6; -.
DR OrthoDB; 255234at2759; -.
DR PhylomeDB; Q7PVF6; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
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; IBA:GO_Central.
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: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; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
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..868
FT /note="Coatomer subunit gamma"
FT /id="PRO_0000405306"
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 REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 96561 MW; 609FA6407FDB5736 CRC64;
MWRTKRGRTR RRDAGGNPWQ NLEKTSVLQE TRMFNETPVN ARKCTHILTK ILYLLNQGEV
LGTREATECF FAMTKLFQSK DVVMRRMVYL GIKELSPIAD DVIIVTSSLT KDMTGKEDLY
RAPAIRALCS ITDSTMLQAV ERYMKQCIVD RNAPVSSGAL VSSLHLASTA GEVVKRWANE
AQEALNSDNI MVQYHGLGLL YHIRKADRLA VTKLVNKLTR QHLRSPYATC FLIRIACKIM
EEEDASGNAT EDSPLFNFVE CCLRNKSEMV VYEAAHAVVN LKRTNPRELS TAVSILQLFC
GSSKATLRFA AVRTMNKVAM LHPPAVNVCN LDLEGLIADS NRSVATLAIT TLLKTGAESS
VERLMKQIAT FVAEISDEFK LVVVQAIRSL CTKFPRKHAV TMNFLSGMLR EEGGLEYKTS
IVDTIILIIE ENPDAKEAGL GHLCEFIEDC EHTSLAVRIL HLLGKEGPYS KCPSRYIRFI
YNRVILENAT VRAAAVAAIA QFGACCPDLL PNVLVLLNRC QMDCDDEVRD RATYYYTILN
QSNPELNKRF IADHEIVSLP LLEKSLNEHL KGPLAERFDL SIVPKSQVIQ PEVNEEVMIM
NKAAPKIARV NREEVNTEKL LAIPGIHHVG ALHKSCAPVQ LTESETEYTV SCIKHCFAHH
IVFQFDCVNT LSDQLLENVR VDLELPEGFV SRAVIPCAKL PYGDKESTYV IVQFPEDVPS
SIATLGATLR FLVKDCDPAT GQPDSDEGYN DEYILEDIEV TVADQMQKSK KQNFLAAWES
ADTEEWVEAE DTFELSSVTS LQDAVNTILK FLGLAPANLS ENVPDGTFRG GVEVLVRSKL
AVADGVTMQL TVRSTDMDVA ELITSAVG
