ID A0A0D3D3T1_BRAOL Unreviewed; 887 AA.
AC A0A0D3D3T1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN Name=106306081 {ECO:0000313|EnsemblPlants:Bo7g019770.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo7g019770.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo7g019770.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo7g019770.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 RefSeq; XP_013598004.1; XM_013742550.1.
DR AlphaFoldDB; A0A0D3D3T1; -.
DR STRING; 109376.A0A0D3D3T1; -.
DR EnsemblPlants; Bo7g019770.1; Bo7g019770.1; Bo7g019770.
DR GeneID; 106306081; -.
DR Gramene; Bo7g019770.1; Bo7g019770.1; Bo7g019770.
DR KEGG; boe:106306081; -.
DR eggNOG; KOG1078; Eukaryota.
DR HOGENOM; CLU_010353_2_0_1; -.
DR OMA; ISKVTWH; -.
DR OrthoDB; 5260816at2759; -.
DR Proteomes; UP000032141; Chromosome C7.
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:SF8; COATOMER SUBUNIT GAMMA; 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:UP000032141};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT DOMAIN 27..542
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 622..767
FT /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT /evidence="ECO:0000259|Pfam:PF08752"
FT DOMAIN 770..884
FT /note="Coatomer subunit gamma C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16381"
FT REGION 584..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 98507 MW; F6BBA7D2DF004CE2 CRC64;
MAQPLVKKDD DLDDELEFSP FMGIEKGAVL QEARVFNDPQ LDPRRCSQVI TKLLYLLNQG
ESFTKVEATE VFFSVTKLFQ SKDTGLRRMV YLIIKELSPG SDEVIIVTSS LMKDMNSKID
MYRANAIRVL CRIIDGTLLT QIERYLKQAI VDKNPVVSSA ALVSGLHMLK SNPEIVKRWS
NEVQEAVQSR AALVQFHALA LLHQIRQNDR LAVSKLVGSL TKGAVRSPLA QCLLIRYTSQ
IIRDMGNHSQ SGERPFYDFL ESCLRHKAEM VILEAARAIT ELDGVSSREL TPAITVLQLF
LSSPKPVLRF AAVRTLNKVA MTHPMAVTNC NIDMESLISD QNRSIATLAI TTLLKTGNES
SVERLMKQIT NFMSDIADEF KIVVVEAIRS LCVKFPLKYR SLMNFLSNIL REEGGFEYKR
AIVDSIVTII RDIPDAKENG LLHLCEFIED CEFTYLSTQI LHFLGIEGPN TSDPSKYIRY
IYNRVHLENA TVRAAAVCTL AKFGFMVEAL KPRITVLLKR CIYDSDDEVR DRATLFLSIL
GNDDGLVETD NDSREFLFGS LEAPLVNMET SLKNYEPSEE AFDVDSVPKE VKSQPLAEKK
AKGKKPTGLG APPPAPVSGF DAYERLLSSI PEFATFGKLF KSSSPVELTE AETEYSVNVV
KHIFGSHVVF QYNCTNTVPE QLLERVNVIV DASEAEEFSE LSSKPLNSLP YDSPGQAFVA
FEKPEGVPAV GKFSNTLTFV VKEVDPNTGE AEEDGVEDEY QLEDLEIVPA DYMVNVGVSN
FRNAWESMDP ENELVDEYGL GPRESLGEAV KAVTDVLGMQ SCEGTETVAS NARSHTSLLS
GLYIGNVKVL VKAQFGMDNR KEIAMKLAVR ADDQSVSEAI HAIVSGG
//
