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Database: UniProt
Entry: A0A2G5EJ00_AQUCA
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ID   A0A2G5EJ00_AQUCA        Unreviewed;       886 AA.
AC   A0A2G5EJ00;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN   ORFNames=AQUCO_00700185v1 {ECO:0000313|EMBL:PIA55700.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA55700.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA55700.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) 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; KZ305024; PIA55700.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5EJ00; -.
DR   STRING; 218851.A0A2G5EJ00; -.
DR   InParanoid; A0A2G5EJ00; -.
DR   OrthoDB; 5260816at2759; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT   DOMAIN          27..540
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          622..766
FT                   /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT                   /evidence="ECO:0000259|Pfam:PF08752"
FT   DOMAIN          769..883
FT                   /note="Coatomer subunit gamma C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16381"
FT   REGION          593..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   886 AA;  98514 MW;  A0844AE85910B0CE CRC64;
     MAQPLIKKDD DRDDEADYSP FLGIEKGAVL QEARVFNDPQ LDPRRCSQVI TKSLYLLNQG
     ETFTKVEATE VFFAVTKLFQ SRDLGLRRMV YLMIKELSPS ADEVIIVTSS LMKDMNSKTD
     MYRANAIRVL CRITDGTLLT QIERYLKQAI VDKNPVVASA ALVSGIHLLQ TNPEIVKRWS
     NEVQEAVQSR AALVQFHALA LLHQIRQNDR LAVSKLVTSL TKGTVRSPLA QCLLIRYTSQ
     VMRESNPNTA TGERPFFDYL ESCLRHKAEM VIFEAARAIT ELSDVHTREL TPAITVLQLF
     LSSSKPVLRF AAVRTLNKVA MTHPMAVTNC NIDMESLISD QNRSIATLAI TTLLKTGNES
     SVDRLMKQIT NFMSDIADEF KIVVVEAIRS LCLKFPLKYR SLMNFLSNIL REEGGFEYKK
     AIVDSIVILI RDIPDAKESG LFHLCEFIED CEFTYLSTQI LHFLGNEGPK TSDPSKYIRY
     IYNRVILENA TVRASAVSTL AKFGALVDSL KPRIYVLLRR CLFDCDDEVR DRATLYLNML
     VGDGSVVETG KDVKDFLFGS LNIPLINLET SLKNYEPSEE AFNIDSVPKE VKSQPLAEKK
     APGKKQSALG APPTAPTSSS DAYERILSAI PEFSTFGHLF KSSAPVELTE AETEYAVNVV
     KHIYDGHVVF QYNCTNTIPE QLLEDVMVVV DATEAEDFSE TASKPLKSLP YDSPGQTFVA
     FEKPEGAILG KFSNVLKFNV KEVDPSTGEA EEDSVEDEYQ LEDLEVVAAD YVLRVGVSNF
     RNAWEGMGPD CERVDEYGLG VRESLAEAVS AVINILGMQP CEGTEVVPNN SRSHTCLLSG
     VFIGNVKVLV RLSFGIDGPK QVAMKLAVRS EDQAVSDAIH EIVSSG
//
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