ID A0A1C7NQT0_9FUNG Unreviewed; 938 AA.
AC A0A1C7NQT0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN Name=copg2 {ECO:0000313|EMBL:OBZ91477.1};
GN ORFNames=A0J61_00441 {ECO:0000313|EMBL:OBZ91477.1};
OS Choanephora cucurbitarum.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC Choanephora.
OX NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ91477.1, ECO:0000313|Proteomes:UP000093000};
RN [1] {ECO:0000313|EMBL:OBZ91477.1, ECO:0000313|Proteomes:UP000093000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ91477.1,
RC ECO:0000313|Proteomes:UP000093000};
RA Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT "Choanephora cucurbitarum.";
RL Submitted (MAR-2016) 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}.
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:OBZ91477.1}.
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DR EMBL; LUGH01000010; OBZ91477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7NQT0; -.
DR STRING; 101091.A0A1C7NQT0; -.
DR InParanoid; A0A1C7NQT0; -.
DR OrthoDB; 5260816at2759; -.
DR Proteomes; UP000093000; 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:UP000093000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT DOMAIN 21..574
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 673..820
FT /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT /evidence="ECO:0000259|Pfam:PF08752"
FT DOMAIN 823..937
FT /note="Coatomer subunit gamma C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16381"
FT REGION 620..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 103489 MW; B2002BDFA77C7859 CRC64;
MSYAKRDEDS GEVSIFSQIN KSTVLQEARA FNDSPINVRK CRLLLTKIIY LLSLGEPFNT
QEATDLFFNV IKLFQSKDTS LRQMMYLVIK ELSGIAQDVI MVTQSLIKDI QSKQETIYRA
NAIRALCLIT DPSMIQGIER IIKASIVDKN PSVSAAALVS SYHLFGASKE IVRRWATEVQ
EAAYAKQSGG FASAATSYIT SFGGGGNNQN QAVVSTSSIA QYHAMGLLYL IRQQDRMAVA
KLVQTFSGTG RGSNSGTLKN PAAVCILIRY ACKVMEDDPG STKRIYELLE GYLKHKSDMV
NLEAARAICE MKDATAKELY PAISVLQISL SSPKPTLRFA AIRILNNLAL SKPSAVSPCN
LDIENLVADQ NRSIATFAIT TLLKTGNEAS VDRLMKQISS FMGEISDEFK VIVVEAIRSL
CLKFPNKQAI MLSFLSGVLR DEGGYEFKKA VVEAIFDMVR HIPESKDTAL SYLCEFIEDC
EFTKLSVRVL HLLGAEGPKA PTPTKYIRYI YNRVILENSI IRGAAVSALT KFGINCPDTN
VKQSVRVLLA RCQDDVDDEV RDRATLALEM MKDESLAKAY NVGDSTFALP ILERELVEYV
NKQESDQSFN LSAIPVISKA QEEEERRRNR PQDLATATLA ISSPTVTGAS SSASPATPKA
DQAGKSQMDQ QAAYADALAA IPEIAAYGPL FKSSAKIPIT ESETEYSVQC IKHTFAKHIV
FQFDCLNTLN DQLLENVEMI MQIDYEEAGL VRVLEIPAAQ LAYDVPGQIY VGYEREDPDD
YPIASFSNSL KFIIKDCDPT TGEPDEEGYE DEYQVEDIDL LTSDYIRSTY ISNFEEEFES
LSENEAIETL ALDREKAPSL QAACTSIIDL LGMQPLNDTA LPRNPNVHTL LMAGTFLTGE
KILARCRMTF NSSSGVAFEM SVRSEDATVS QIVLSAIA
//
