ID A0A0C3QYX0_9AGAM Unreviewed; 760 AA.
AC A0A0C3QYX0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Conserved oligomeric Golgi complex subunit 6 {ECO:0000256|ARBA:ARBA00020973, ECO:0000256|RuleBase:RU365075};
DE Short=COG complex subunit 6 {ECO:0000256|RuleBase:RU365075};
DE AltName: Full=Component of oligomeric Golgi complex 6 {ECO:0000256|ARBA:ARBA00031348, ECO:0000256|RuleBase:RU365075};
GN ORFNames=M407DRAFT_13375 {ECO:0000313|EMBL:KIO34549.1};
OS Tulasnella calospora MUT 4182.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Tulasnellaceae; Tulasnella.
OX NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO34549.1, ECO:0000313|Proteomes:UP000054248};
RN [1] {ECO:0000313|EMBL:KIO34549.1, ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO34549.1,
RC ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RA Kuo A., Girlanda M., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a component of the peripheral membrane COG complex
CC that is involved in intra-Golgi protein trafficking. COG is located at
CC the cis-Golgi, and regulates tethering of retrograde intra-Golgi
CC vesicles and possibly a number of other membrane trafficking events.
CC {ECO:0000256|ARBA:ARBA00043873}.
CC -!- FUNCTION: Acts as component of the peripheral membrane COG complex that
CC is involved in intra-Golgi protein trafficking. COG is located at the
CC cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles
CC and possibly a number of other membrane trafficking events.
CC {ECO:0000256|RuleBase:RU365075}.
CC -!- SUBUNIT: Component of the conserved oligomeric Golgi complex.
CC {ECO:0000256|RuleBase:RU365075}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004395, ECO:0000256|RuleBase:RU365075};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395,
CC ECO:0000256|RuleBase:RU365075}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the COG6 family. {ECO:0000256|ARBA:ARBA00011023,
CC ECO:0000256|RuleBase:RU365075}.
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DR EMBL; KN822942; KIO34549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3QYX0; -.
DR STRING; 1051891.A0A0C3QYX0; -.
DR HOGENOM; CLU_011361_2_0_1; -.
DR OrthoDB; 276556at2759; -.
DR Proteomes; UP000054248; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017119; C:Golgi transport complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR010490; COG6.
DR InterPro; IPR048369; COG6_C.
DR InterPro; IPR048368; COG6_N.
DR PANTHER; PTHR21506; COMPONENT OF OLIGOMERIC GOLGI COMPLEX 6; 1.
DR PANTHER; PTHR21506:SF0; CONSERVED OLIGOMERIC GOLGI COMPLEX SUBUNIT 6; 1.
DR Pfam; PF20653; COG6_C; 1.
DR Pfam; PF06419; COG6_N; 1.
DR SMART; SM01087; COG6; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU365075};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365075};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365075};
KW Reference proteome {ECO:0000313|Proteomes:UP000054248};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365075}.
FT DOMAIN 140..243
FT /note="Conserved oligomeric complex COG6 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06419"
FT DOMAIN 278..704
FT /note="Conserved Oligomeric Golgi complex subunit 6 C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20653"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..213
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 83772 MW; CA539521E86C8D87 CRC64;
MKSPGVASPS ARGPPSALTT PSFFHTPPGN NRLPSTIPSK NPLALRLYKV LGANYSDAST
KEALETLSSF YSPVAATEPG ASASMLGAPV LKEPDRLTRD GPEDEEEEEE PDEVWGAEYA
RKARRKQTEM EQPVDGELAL RARKGLRRDI ETKLAESSRK FLTAFAEVDK KLDILQVHVG
EMQTRCDEAQ SKLQATNESC KHLLDRAEGL RAQREATAAR QSIISLFLSR FTLTEEETQA
VASRDVPVGP QVFAAMDRIE KIRIDCRVLM SGEEGETKAG LDIMSLTASL LDQAYNKLAR
WTSFEFRQMG KDASLDVAPL MQEAVLRLRQ RPELLNDSLK ILTEVRQATL LSSFLEALTR
GGPGGLPRPI ELHAHDPTRY VGDMLAWVHQ AMAGEREFLE SLFGVRGDNR MVGSVRQAKG
TEEEEYVAKL MDGDLEKLSM PLRVRVLQTV KSQEGSITAY KIANLLQFYL LTVSRTVGEE
ALLSKTLKAI TDAAYQVFFD TIDAQGRSLL RFLHPPDSDL SPPLALRDSS QVLREIMAVY
DSSLLGDEDP TEREAAFAQI LEAAVDPAME MCKRMSDLRE GMPTWDKAVF LVNCTTYMQN
MLQAYSFTST HVALLQKEVD RNIRTMVTEH SAFFLKESGL EPIVQAMDSK PEDTPLSRLP
SASSQALTAA LTQFDSFLST LDPSSSPRLS LLSPWRHRDS SSKRGASAPA SKVGNDATVQ
VYRIGCLAKI LGPGWGGRVH GVGVGCLEEF EKSLKLALGT
//