ID F4P7L6_BATDJ Unreviewed; 903 AA.
AC F4P7L6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN ORFNames=BATDEDRAFT_35627 {ECO:0000313|EMBL:EGF78626.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF78626.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF78626.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) 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; GL882888; EGF78626.1; -; Genomic_DNA.
DR RefSeq; XP_006680775.1; XM_006680712.1.
DR AlphaFoldDB; F4P7L6; -.
DR STRING; 684364.F4P7L6; -.
DR GeneID; 18240830; -.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; F4P7L6; -.
DR OMA; IEDCEYN; -.
DR OrthoDB; 5260816at2759; -.
DR Proteomes; UP000007241; Unassembled WGS sequence.
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:0009306; P:protein secretion; IBA:GO_Central.
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:UP000007241};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT DOMAIN 20..534
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 636..786
FT /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT /evidence="ECO:0000259|Pfam:PF08752"
FT DOMAIN 788..902
FT /note="Coatomer subunit gamma C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16381"
FT REGION 586..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 903 AA; 99877 MW; 3F51FDE0C5A2E191 CRC64;
MSGKKHDEDT DGLFGGSLDK STVLQESRAF NESPINPKKC RIIITKIVYL LHQGQTYQSQ
EATDAFFSIS KLFQNPDVSL RQMVYLAIKE LAKTAQDVFV VTSSLTKDMN ARSDLIYRPN
SIRALCKITD ASMMQGIERF IKQAIVDKNV AVSSAALVSS IHLFQLNKEV VKRWANEAQE
AISSKGITAQ YHALGLLYLM RQHDRMAVIK MVQNYARGSL RSPHAIVMLI RYAWKIMEDE
DSSSRAFYEY LESWLRHKND MVVYEAARAI CSLKNVTPKE LFPAVSALQL MIVNHKPALR
FAAIRTLNRL AMIHPNAVFP CNLDMENLIT DSNRSIATFA ITTLLKTGNE ASVDRLMKQI
SGFMSEISDE FKIIVVDAVR SLCLKFPSKQ TLMLNFLSGV LRDDGGYFFK SAIVDAMFDI
IHSIPESKEF ALSHLCEFIE DCEFAKLAVR ILHVLGAEGP HASNPTKYIR FIYNRVILET
SIVRAAAVSA LAQFAVHLED ARPRICVLLD RCTDDSDDEV RDRAALFLRI LNNPDLSSKY
IANNSTFALA SLEANLSHYL KTPAGYDKPF DINSVAVVSK EQDQVERQRV KDAARDQSTA
GAGGVSNGAA ATHSSISAIS GSAGAASSAF DAQSVYATIM SNIPQLASLG PLYKSSQAVD
LTEAETEYIV TCVKHVFPQH FVFQFECKNT LDDSMLENVS VSMGLQSSDS QDIHELQPEF
IITAEKLVYD VPASIYVVYQ RLNNATPTAY FSNTLKFVVK DCDPNTGEPD EEGFDDEYLL
EDVEITLSDY MLPTYVADFD RAWNDAGEAG QVIEAYALTA VKGILQAVKS TCDMLGMQAL
NGCDNVSEKA TTHAMMMAGT FVNGVQVLTK ARMAFDPSSG VSMEICVRSQ DADISARVAN
AIS
//
