ID A0A5C3NHE8_9AGAM Unreviewed; 930 AA.
AC A0A5C3NHE8;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 22-FEB-2023, entry version 9.
DE RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN ORFNames=OE88DRAFT_1650271 {ECO:0000313|EMBL:TFK56803.1};
OS Heliocybe sulcata.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Heliocybe.
OX NCBI_TaxID=5364 {ECO:0000313|EMBL:TFK56803.1, ECO:0000313|Proteomes:UP000305948};
RN [1] {ECO:0000313|EMBL:TFK56803.1, ECO:0000313|Proteomes:UP000305948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OMC1185 {ECO:0000313|EMBL:TFK56803.1,
RC ECO:0000313|Proteomes:UP000305948};
RX PubMed=30886374; DOI=.1038/s41559-019-0834-1;
RA Varga T., Krizsan K., Foldi C., Dima B., Sanchez-Garcia M.,
RA Sanchez-Ramirez S., Szollosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA Damon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA Grigoriev I.V., Vagvolgyi C., Papp T., Martin F.M., Miettinen O.,
RA Hibbett D.S., Nagy L.G.;
RT "Megaphylogeny resolves global patterns of mushroom evolution.";
RL Nat. Ecol. Evol. 3:668-678(2019).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ML213503; TFK56803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C3NHE8; -.
DR STRING; 5364.A0A5C3NHE8; -.
DR Proteomes; UP000305948; 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:UP000305948};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT DOMAIN 20..575
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 659..806
FT /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT /evidence="ECO:0000259|Pfam:PF08752"
FT DOMAIN 809..907
FT /note="Coatomer subunit gamma C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16381"
FT REGION 628..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 102055 MW; CA84163458666E7B CRC64;
MALLIKKEDE SGLSSYYNNK TTIIQEARVF NESPISPRKC RALLTRVVYL LYVGETFGTQ
EATELFFGTT KLFQHKDSAL RQMVYLAIKE LATTAEDVIM VTSSIMKDMQ PNSEVIYRSN
AIRALCRIID PSMAQGIERF FKAAIVDRNP SISSAALVSS YHLFPDAKDV VKRWSNEAQE
AVSGKSAGSF FGGNSGGGYL GGWGSQAQAQ SGYQAIPSTS YITQYHALGL LYLIRQQDRM
AVTKMIQQLG GGKSGSGTTL KNPMALCMLI RYAAKVMEED PNVQRQMLEL LEGWLRHKSD
MVNLEAARVI CEMKNVSPAQ LTRAIAVLQL FLSSPKSTLK FAATRTLASL ALTHPASVAS
CNIELENLIS DPNRSVATYA ITTLLKTGNE ASVDRLMKQI TGFMSEISDE FKVIIVDAIR
SLCLKFPAKH ASMLGFLSGV LRDEGGYDFK RAVVEAIFDM IKFISDAKEQ ALSHLCEFIE
DCEFTKLSVR ILHLLGMEGP KSSQPAKYIR YIYNRVVLEN ATVRSAAVAS LAKFGVDAQD
SALQKRISVL LNRCLDDVDD EVRDRAAMYL KVVKEPELAN VYVKEESIPS LAALESKLVV
YVNEPEAAEQ PFDFASIPRV SRAQAVSEAA RPSTLDTMSA PTTKKSATPP PTAAETQSAY
AQQLTEVPEF ASFGPVLYSS SKPTPLTESE TEYQVSCVKH FFKDHIVFQL NVSNTLADSV
LEQVAVVMQP STDSGLTEDF IIQLESLSPS SSGVIYVSFT RDRPEEYATA SFQCVLKFVS
KECDPSTGEP EEEGYPDEYE LEELELAASD YIVPTYATFS SEWDRLRGGA SATETFALSG
MESLKAACDS IIEILNMEPL GGSEVPTSSS VHTLQLSGLL PVGGGRVLVR SRMTYSRGQG
VTLELGVQPC GGGHWRLEAW RDPFPCSVDT
//
