ID A0A5N5D627_9PEZI Unreviewed; 919 AA.
AC A0A5N5D627;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 24-JAN-2024, entry version 8.
DE RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN Name=sec21 {ECO:0000313|EMBL:KAB2572770.1};
GN ORFNames=DBV05_g8586 {ECO:0000313|EMBL:KAB2572770.1};
OS Lasiodiplodia theobromae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Lasiodiplodia.
OX NCBI_TaxID=45133 {ECO:0000313|EMBL:KAB2572770.1, ECO:0000313|Proteomes:UP000325902};
RN [1] {ECO:0000313|EMBL:KAB2572770.1, ECO:0000313|Proteomes:UP000325902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LA-SOL3 {ECO:0000313|EMBL:KAB2572770.1,
RC ECO:0000313|Proteomes:UP000325902};
RX PubMed=31511626; DOI=.1038/s41598-019-49551-w;
RA Felix C., Meneses R., Goncalves M.F.M., Tilleman L., Duarte A.S.,
RA Jorrin-Novo J.V., Van de Peer Y., Deforce D., Van Nieuwerburgh F.,
RA Esteves A.C., Alves A.;
RT "A multi-omics analysis of the grapevine pathogen Lasiodiplodia theobromae
RT reveals that temperature affects the expression of virulence- and
RT pathogenicity-related genes.";
RL Sci. Rep. 9:13144-13144(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 -!- 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:KAB2572770.1}.
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DR EMBL; VCHE01000071; KAB2572770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5D627; -.
DR Proteomes; UP000325902; 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:UP000325902};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT DOMAIN 21..558
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 652..803
FT /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT /evidence="ECO:0000259|Pfam:PF08752"
FT DOMAIN 805..918
FT /note="Coatomer subunit gamma C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16381"
FT REGION 606..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 919 AA; 100976 MW; 4DE2D3C57B008833 CRC64;
MSYNKKDEDS EGAIVKVDRT SVFQEARVFN SSPISPRRCR ILLTKIALLL FTGEKFPTNE
ATSLFFGISK LFQNKDASLR QMVYLVIKEL ANTAEDVIMV TSSIMKDTAV GSDVVYRANA
IRALCRVIDS STVPAIERLI KTAIVDKTPS VSSAALVSSY HLLPVARDVV RRWQSETQEA
ASATKSSGGF SLGFGTSHSN LAAANTNFMT QYHAIGLLYQ MRSHDRMALV KMVQQYSAAG
VVKSPAATVL LVRLAAKLAE EDPNLRRPMM QLLDGWLRHK SEMVNFEAAK AICDMKDVSD
SEIVQAVHVL QLFLTSPRAV TKFAAIRILH NFASFKPDAV RQCNPDIEAL ITNSNRSIAT
FAITTLLKTG NESSVDRLMK QISGFMAEIT DEFKVTIVEA IRTLCLKFPS KQAGMLAFLS
GILRDEGGYE FKRAVVESMF DLIKFVPESK EDALAHLCEF IEDCEFTKLS VRILHLLGME
GPKTPQPTKY IRYIYNRVVL ENSIVRAAAV TALAKFGVGQ KDPEVKRSVR VLLTRCLDDT
DDEVRDRAAL NMRLMDDDDE DAHKFIRNDS MFSLPTLEHQ LVMYVTADDK ETFSQPFDLS
KVPVVTREQA DAEDRTKKLT SATPTLKAPS TGPKPAARSG ADAAASATAA AQKYAAQLQA
IPEIAAFGGV LKSSPIVELT ESETEYVVSA IKHIFKEHIV LQYDIKNTLP DTVLADVTMV
VSPTEEEESG LEEEFIIPAP ALKTDEPGTV YVSFKRIEGE ATYVASSFTN ILKFTLKEID
PSTNEPEEGG YEDEYQVEDL DLNGADYIVP AYAGSFDNVW EQSGAGEEAT ETLQLSALKS
IQDAVEQIPK TLSLQPLEGT DVALSTSTHT LKLYGKTITG GKVAAQVRMA FASKTGVTMK
INVRSEEEGV ATLVINSVA
//
