ID A0A1A0H7S7_9ASCO Unreviewed; 934 AA.
AC A0A1A0H7S7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN ORFNames=METBIDRAFT_79276 {ECO:0000313|EMBL:OBA19953.1};
OS Metschnikowia bicuspidata var. bicuspidata NRRL YB-4993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX NCBI_TaxID=869754 {ECO:0000313|EMBL:OBA19953.1, ECO:0000313|Proteomes:UP000092555};
RN [1] {ECO:0000313|EMBL:OBA19953.1, ECO:0000313|Proteomes:UP000092555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-4993 {ECO:0000313|EMBL:OBA19953.1,
RC ECO:0000313|Proteomes:UP000092555};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., LaButti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-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:OBA19953.1}.
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DR EMBL; LXTC01000005; OBA19953.1; -; Genomic_DNA.
DR RefSeq; XP_018710478.1; XM_018859029.1.
DR AlphaFoldDB; A0A1A0H7S7; -.
DR STRING; 869754.A0A1A0H7S7; -.
DR GeneID; 30032005; -.
DR OrthoDB; 5260816at2759; -.
DR Proteomes; UP000092555; 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:UP000092555};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT DOMAIN 19..569
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 667..820
FT /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT /evidence="ECO:0000259|Pfam:PF08752"
FT DOMAIN 822..932
FT /note="Coatomer subunit gamma C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16381"
FT REGION 630..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 103833 MW; 2ABCABAF53B3F248 CRC64;
MSTQNLKAAD GSGIVPDKMA VFQECLQQFN ALPVNTKKCR QLLAKLLRLI YQGEQFPLQE
STTLFFSISK LFQHKDTALR QLVYLTIKEL AASSQDILMV TSSIMKDIQS GDLIYKPNAI
RTLSKVLDPT TVSASERLFR NCLVDKNPIV SSAALISSYN LLPIAKDVVK RFSNETLETI
QSYKQFPANQ FQLHEYYGSA TTNLPTNSYM YQYHALGLLY QLRNHDKMSL MKLITSLHEG
SSLKNSLSII QLIRYINKVL TDDGSLSSHL YPILASFLKH KSDMVELEAC KTLISLLLLV
PDDGYMAVIL TLQKLLTVPR TATRFAAVRL INKVSLKHPE KILVVNLELE GLINDPNRSV
STLAITTLLK TLGAGTVEST SSESVDRLIS KMTSLMDEIT EDFKVVIIDA IENLALKFPS
KHKKLVAFLS DLLRDDGSLQ MKSRIVEALF DLIKYLPDES AKQLILMNLC EFIEDCEFTE
LSVRILHLLG DEGPKMSNAS YYIRHIYNRL VLENSIVRSS AVIALAKFAA VCEGEISRNV
KILLSRCLKD VDDEVRDRAT LSLSFIDNQK TKLIVNDSKY NLAALESKLT NYLKDENNFS
SSFDISEVPL LTFDEVKSLE YNKKLNKLEN AAEGATQSEN GDMSGNSNSR NSESAKPDSA
DEYLKQQEYA MALAQIPDFA DYGKLTKSSS HSIYLTDKEN EFVVTALKHF FMDTQKLVIQ
YVITNTLSTL VLQDVSLIVQ PDNALYQEDF VIPLAELRPD QTGSVYVSFS TPAIGDDDIL
AAFGNTISYN SKDVIDENGN IDPADEGIED EYQVEDLEVN AGDFISPLYN SNFTSVFEQL
PYEDSSVVTV GGVTSIESAV SKLLKTFNSM PLDGSDYVPS DTTSHVLKTM GKDVWGGRVG
AQIRLACTGK KVVAKLQVKA ETEGFAEVVA NGAT
//
