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Database: UniProt
Entry: A0A4S4M9G6_9AGAM
LinkDB: A0A4S4M9G6_9AGAM
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ID   A0A4S4M9G6_9AGAM        Unreviewed;       931 AA.
AC   A0A4S4M9G6;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   22-FEB-2023, entry version 11.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN   ORFNames=EW146_g1625 {ECO:0000313|EMBL:THH19580.1};
OS   Bondarzewia mesenterica.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Bondarzewiaceae; Bondarzewia.
OX   NCBI_TaxID=1095465 {ECO:0000313|EMBL:THH19580.1, ECO:0000313|Proteomes:UP000310158};
RN   [1] {ECO:0000313|EMBL:THH19580.1, ECO:0000313|Proteomes:UP000310158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 108281 {ECO:0000313|EMBL:THH19580.1,
RC   ECO:0000313|Proteomes:UP000310158};
RA   Buettner E., Kellner H.;
RT   "Genome sequencing of the rare red list fungi Bondarzewia mesenterica.";
RL   Submitted (FEB-2019) 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:THH19580.1}.
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DR   EMBL; SGPL01000041; THH19580.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S4M9G6; -.
DR   Proteomes; UP000310158; 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:UP000310158};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT   DOMAIN          20..574
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          661..813
FT                   /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT                   /evidence="ECO:0000259|Pfam:PF08752"
FT   DOMAIN          816..929
FT                   /note="Coatomer subunit gamma C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16381"
FT   REGION          623..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..644
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   931 AA;  101692 MW;  0393B795FDCBD0E6 CRC64;
     MSLASKKEEE GGLNSYYNNK TTILQEARVF NESPISPRKC RALLTRIVYL LYFGESFGTQ
     EATTLFFGTT KLFQHKDSAL RQMVYLAIKE LANTAEDVIM VTSSIMKDMQ PNSEVIYRPN
     AIRALCRIID PSMVQGVERF FKAAIVDRTP SISSAALVSS YHLFPAAKDV VKRWVNEVQE
     AVNAKSSTSF FGSSTPSSYL GFGSSSSSSN SGYSPMPSSS YITQYHALGL LYLIRQQDRM
     AVTKMIQQLG GGKSGAGTIL KNPMALCMLI RYAAKVIEED PNVQKQMLDM LEGWLRHKSD
     MVNLEAARAI CEMRGVTSAQ LTRSIAVLQL FLSSPKPTLK FAATRTLASL ALTHPTSVAT
     CNVDLENLIS DSNRSVATYA ITTLLKTGNE ASVDRLMKQI TGFMSEISDE FKVIIVDAIR
     SLCLKFPTKH VSMLGFLSGV LRDEGGYDFK RAVVEAIFDM IKFIGDCKEQ ALSHLCEFIE
     DCEFTKLSVR ILHLLGIEGP QAPQPAKYIR FIYNRVVLEN ATVRAAAVSS LAKFGISDDD
     SKLHNSVAVL LNRCLDDVDD EVRDRAAMYL KVLDAPPLAE TYIKDDSVFS LSALEAKLVS
     YVNDANAADT PFDFSSVPKV SRQQAEQEVA RPSTLDTIGT PSAKKSSPSP PPPTAEETQS
     AYLQQLAEVP ELASYGPVLN SSAKPVRLTE SETEYQVSCT KHIFKEHVVF QFNVSNTLPD
     TILEQVSVIM QPSTDSGLTE DFIIPLPSLS SSSSSSSPGI VYVSFTRDSP EEFATASFTC
     ILKFLSKEVD PSTGEPEEEG YEDEYQLEEV ELSAGGDYIV PSYANFSSEW DRLRGGASAT
     ETFSLSAMES IKAACDSIVE ILNMEPLGGS QTPTSTSVHT LQLSGLLTGG GGKVLVRCRM
     TFSHGQGVTL ELGVRAEKQE ACKLVLAAIG G
//
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