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Database: UniProt
Entry: A0A1D6HV53_MAIZE
LinkDB: A0A1D6HV53_MAIZE
Original site: A0A1D6HV53_MAIZE 
ID   A0A1D6HV53_MAIZE        Unreviewed;       842 AA.
AC   A0A1D6HV53;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN   ORFNames=ZEAMMB73_Zm00001d019106 {ECO:0000313|EMBL:ONM52171.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM52171.1};
RN   [1] {ECO:0000313|EMBL:ONM52171.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM52171.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000256|PIRNR:PIRNR037093}.
CC   -!- SUBUNIT: Oligomeric complex. {ECO:0000256|PIRNR:PIRNR037093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037093}. Golgi
CC       apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC       ECO:0000256|PIRNR:PIRNR037093}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR037093};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255,
CC       ECO:0000256|PIRNR:PIRNR037093}. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane {ECO:0000256|PIRNR:PIRNR037093}; Peripheral membrane
CC       protein {ECO:0000256|PIRNR:PIRNR037093}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR037093}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the COPG family. {ECO:0000256|ARBA:ARBA00010720,
CC       ECO:0000256|PIRNR:PIRNR037093}.
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DR   EMBL; CM007650; ONM52171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6HV53; -.
DR   ExpressionAtlas; A0A1D6HV53; baseline and differential.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
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; 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:SF0; COATOMER SUBUNIT GAMMA-2; 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.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR037093};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|PIRNR:PIRNR037093};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|PIRNR:PIRNR037093};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|PIRNR:PIRNR037093};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037093};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|PIRNR:PIRNR037093}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT   DOMAIN          28..540
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          623..768
FT                   /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT                   /evidence="ECO:0000259|Pfam:PF08752"
FT   DOMAIN          771..826
FT                   /note="Coatomer subunit gamma C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16381"
SQ   SEQUENCE   842 AA;  93963 MW;  192437DF74E0136D CRC64;
     MAQPLVVKKD DDLDEEEYYS PFLGIEKGAV LQEARVFHDP QLDARRCCQV ITKLLYLLNQ
     GDTFTKVEAT EVFFATTKLF QSKDAGLRRM VYLMIKELSP SADEVIIVTS SLMKDMNSKT
     DMYRANAIRV LCRIIDSTLL TQIERYLKQA IVDKNPVVAS AALVSGIYLL QTSPEVVKRW
     SNEVQEAVQS RAALVQFHAL ALLHQIRQND RLAVSKLVTS LTRGSVRSPL AQCLLIRYTS
     QVIRESGVYQ GGDRPFFDFL ESCLRNKAEM VILEAARAIT ELNGVTSREL TPAITVLQLF
     LSSSKPVLRF AAVRTLNKVA STHPLAVTNC NIDMESLISD QNRSVATLAI TTLLKTGNES
     SVDRLMKQMT NFMSDIADEF KIVVVEAIRS LCLKFPLKYR SLMNFLSNIL REEGGFEYKK
     AIVDSIIILI RDIPDAKESG LFHLCEFIED CEFTYLSTQI LHFLGNEGPK TSDPSKYIRY
     IYNRVILENA TVRASAVSTL AKFGALVDSL KPRIFVLLRR CLFDGDDEVR DRATLYLKLL
     GGEATVGETE KDVNEFLFGS LDVPLVNLET SLRNYEPSDV PFDISSVSKE TKSQPLAEKK
     STGKKSAGPA SAVSGSVSTV DASYEKLLSS IPEFADFGKL FKSSAPVELT EAETEYSVNV
     VKHIFDRHVV LQYNCTNTIP EQLLEQVIVL VDASEADEFL EVASKPLESL PYDSPGQTFV
     AFENPEGVIA TGKFSNILKF FVKEVDPSTG EAEDDGVEDE YQLEDLEIVS ADYMLKVGVS
     NFRNAWENMD PETERVDEYG LGVRESLAEA VSAVISILGM QPCEVSLFYH SFYCQMNATV
     IQ
//
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