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Database: UniProt
Entry: G1XCT2_ARTOA
LinkDB: G1XCT2_ARTOA
Original site: G1XCT2_ARTOA 
ID   G1XCT2_ARTOA            Unreviewed;       925 AA.
AC   G1XCT2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN   ORFNames=AOL_s00079g252 {ECO:0000313|EMBL:EGX49031.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX49031.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX49031.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGX49031.1}.
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DR   EMBL; ADOT01000138; EGX49031.1; -; Genomic_DNA.
DR   RefSeq; XP_011122429.1; XM_011124127.1.
DR   AlphaFoldDB; G1XCT2; -.
DR   STRING; 756982.G1XCT2; -.
DR   GeneID; 22893333; -.
DR   eggNOG; KOG1078; Eukaryota.
DR   HOGENOM; CLU_010353_2_0_1; -.
DR   InParanoid; G1XCT2; -.
DR   OMA; NYMTQYH; -.
DR   OrthoDB; 5260816at2759; -.
DR   Proteomes; UP000008784; 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:UP000008784};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT   DOMAIN          19..552
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          652..806
FT                   /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT                   /evidence="ECO:0000259|Pfam:PF08752"
FT   DOMAIN          808..924
FT                   /note="Coatomer subunit gamma C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16381"
FT   REGION          606..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   925 AA;  101295 MW;  D3071412ECF3B667 CRC64;
     MSYSKKDEDG DQTIFKVDRS TVFQEARIFN TSPISPRKCR IQLTKITYLL HTGERFPTPE
     ATTLFFGITK LFQHRDPSLR QMVYLVIKEL ASTAEDVIMV TASIMKDTAV GSDVVYRPNA
     IRALCRVIDA TNVQAIERLI KTAIVDKTPS VSSAALVSSY HLLPLARDVV RRWANETQEA
     VLSNKSGGGF LGLGSSSSSI GPPTGYMTQY HAIGLLYQMR AHDRMSLVKM VQQFGSQNAS
     AIKSPAAVMM LVRLAGKIAI EDPNLRKPMA QLLEGWLRHK SEMVNFEAAK VICELPDVTD
     AEVAPAVHVL QLFLTSPRAV TKFAAIRILH HIASFKPNTL QHCNMDIETL ISNSNRSIAT
     FAITTLLKTG NEASVDRLMK QISGFMADIT DEFKITIVEA IRTLCLKFPS KQAGMLAFLS
     GILRDEGGYE FKKSVVESMF DLIKFVPDSK EEGKLFIEDC EFTKLAVRVL HLLGQEGPKT
     SHPTKYIRYI YNRVVLENAV VRAAAVTALA KFGVGQKDEE VKRSVVVLLT RCLDDPDDEV
     RDRAALNLKL VTGASEYGAK FIHNDSIFSL PIFEHQLVMY VTGDQSTFSK PFDIASIPVV
     TRAEADAEDK SKKMRPASDM PTLKAPTISA PGARPSAAPI SEAAVNAAAA SQQYAATLSA
     IPEIKALGQL LKSSRVVELT EAEMEYVVTS VKHIFKDHIV LQYNVKNTLT DSVLENVTVQ
     VTVAEEDEEE PLVEEFYVPA PKIAVDSPGT IYVAFKRPQS EEGAGYTTTT FNNVLKFTTK
     EIDPSTGEAE DGGYDDEYEV EDLELTGGDY VVPAFCGNFG TVWEQVGTAG EEVTETYGLP
     QENVKNLEEA CNLLASALSL QPMEGTDVPM STTSHVLKLF GKTISGGRVV AMVKMVFSSK
     SGVTVKITVR SEESGVGQLV VSAVA
//
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