ID A0A0K3CEE4_RHOTO Unreviewed; 910 AA.
AC A0A0K3CEE4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN Name=FGENESH: predicted gene_5.326 {ECO:0000313|EMBL:CTR06920.1};
GN ORFNames=AAT19DRAFT_14121 {ECO:0000313|EMBL:PRQ75099.1},
GN BN2166_0027810 {ECO:0000313|EMBL:CTR06920.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR06920.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR06920.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR06920.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PRQ75099.1, ECO:0000313|Proteomes:UP000239560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ75099.1,
RC ECO:0000313|Proteomes:UP000239560};
RX PubMed=29521624;
RA Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA Arkin A.P., Skerker J.M.;
RT "Functional genomics of lipid metabolism in the oleaginous yeast
RT Rhodosporidium toruloides.";
RL Elife 7:0-0(2018).
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; CWKI01000005; CTR06920.1; -; Genomic_DNA.
DR EMBL; LCTV02000005; PRQ75099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K3CEE4; -.
DR STRING; 5286.A0A0K3CEE4; -.
DR OMA; IEDCEYN; -.
DR OrthoDB; 5260816at2759; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR Proteomes; UP000239560; 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:UP000199069};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT DOMAIN 19..556
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 646..793
FT /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT /evidence="ECO:0000259|Pfam:PF08752"
FT DOMAIN 796..909
FT /note="Coatomer subunit gamma C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16381"
SQ SEQUENCE 910 AA; 99664 MW; ADB215FB539ED65A CRC64;
MSGYKKDEES GVGSFFQDKT TVIQEARVFN ETPISPRKCR ILLTKIVYLL YVGETFGTQE
ATTLFFGVTK LFQHKDSALR QMVYLVIKEL SGIAEDVIMV TSSIMKDMQP NLEVIYRPNA
IRALCRVIDG SMIVGLERFF KAAIVDRNVS IASAALVSSY HLQPIARDVI KRWANEASEA
VQNKSSSFAT YGGQGYAAGP TSSIIQYHAL GLLYLIRQGD RMAVTKMIQQ LAGVKGSGGT
LRNPYAICMV IRYAAKVMEE DPNVQRAMYE LIDGYLKHKS DMVNLEAARA ICEMKNVSAA
ELHRPISVLQ LFLSSPKAAL KFSAIRTLAK LAQTHPSAVA AVNLDMEKLI NDDNRSVATF
AITTLLKTGN EASVDRLMKQ ISAFMSEISD EFKVIVVNAI RALCLKFPAK QSVMLTFLSG
VLRDEGGYDF KRAVVEAIFD MIKFIADSKE AALAQLCEFI EDCEFTKLSV RILHLLGVEG
PKSPQPSKYI RYIYNRVILE NAIVRAAAVS SLAKFGINVA DNAVKRSIKV LLTRCLDDVD
DEVRDRAAFN LKLMQDEPLA NTFVRDDSTF SLDTLEARLT SYMADSSALE QPFDFTAVPK
ISKEQALEAA RHSRKDAIDS VAMASEASGV ASTSAAVPSA SETQSAYEKQ LTEVPEFASY
GPVFKSTRKP VELTERETEY VVSAVKHVFA EHVVFQFNVR NTVDAVHLEN VVVVMQPSEE
ADLTEDFIIP VASLGPNSDG VVYVSFTRNN PSTYATGSFG NTLRFLSKEI DPDTGEPEED
GYDDEYSLEE LDLGAADYIV PSYAAFATEW DRLRSGATAQ ETFALTALDS LKTACDSLIE
ILGMEALGGT EAPTSPTVHT LNMSGLVAGG GGKVLARARM TFQTGKGVTM ELTVRAEEEG
AAQLVINAIA
//
