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Database: UniProt
Entry: A0A163LT80_ABSGL
LinkDB: A0A163LT80_ABSGL
Original site: A0A163LT80_ABSGL 
ID   A0A163LT80_ABSGL        Unreviewed;       947 AA.
AC   A0A163LT80;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN   Name=ABSGL_01776.1 scaffold 2142 {ECO:0000313|EMBL:SAL96378.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL96378.1};
RN   [1] {ECO:0000313|EMBL:SAL96378.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL96378.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-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}.
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DR   EMBL; LT550954; SAL96378.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163LT80; -.
DR   STRING; 4829.A0A163LT80; -.
DR   InParanoid; A0A163LT80; -.
DR   OMA; IEDCEYN; -.
DR   OrthoDB; 5260816at2759; -.
DR   Proteomes; UP000078561; 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:UP000078561};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT   DOMAIN          19..575
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          684..830
FT                   /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT                   /evidence="ECO:0000259|Pfam:PF08752"
FT   DOMAIN          833..946
FT                   /note="Coatomer subunit gamma C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16381"
FT   REGION          622..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   947 AA;  104277 MW;  6524D254002601F0 CRC64;
     MSYSKRDEDS GLFYHLDKTA VLQEARVFNN SPINARKCRI LLTKIIYLLS LGEPFASKEA
     TDLFFNVIKL FQSKDTSLRQ MMYLVIKELS GIAEDVIMVT QSLIKDIQSK QETIYRANAI
     RALCLITDPA MIQGIERILK ASIVDKNPSV SSAALVSSYH LFDVAKDIVR RWSNEVQEAV
     HAKSAGSGLS SAASYMSSFG AQPNNAPVVI SNSNITQYHA LGLLYVIRQH DRMAVTKLVQ
     TFSGSRSSGF LGGGGGSALK NPAAVCLLIR YACKVMEEDP GASARIYELL EGYLRHKSDM
     VNLEAARAIC DIPDASMKEL HPAIAVLQLF LSSPKPTLRF AAIRILNKLS LTNPAAVSPC
     NLDMENLITD QNRSVATFAI TTLLKTGNEA SVDRLMKQIS GFMSEISDEF KVIVVEAIRS
     LCLKFPAKQV VMLNFLSGVL RDEGGYEFKK AVVEAIFDMV KFITDSKDAA LSHLCEFIED
     CEFTKLSVRI LHVLGVEGPK AATPTKYIRY IYNRVILENS IIRAAAVSAL AKFGVNVPDP
     LVKKSVKVLL TRCLDDVDDE VRDRATLYLA FMENEDIGKQ YVQDDATFAL PTLERQLVEY
     VNSPLANDKE FDLAGVPMIS KAQEEDERRR LRTQDIISPS TPSVSAGATL GANGTSGSPS
     LASIGSTSTP HHHFAGSLDQ QAVYAEQLAQ IPAFQTFGTL FKSSSKPVPL TESETEYVVH
     CVKHTFARHV IFQFNCTNTL NDQLLENVHM VMQPMDDAPL VQVVEVPVPK LEYNVPGYIY
     VAFEQEDPED LAVGSFSNTL KFDVKDCDPT TGEPDPEGYD DEYQVEDIEL LVSDYTRPNY
     VSQFTQEWET LENELVETFA LDKEKAPSLK VACGSILDLL GMQALEDSAL PKSASVHTLL
     LAGTFLGGIK VLARCRMTFS NASGVAFELA VRSEDAFTTQ MVLSAIA
//
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