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Database: UniProt
Entry: A0A0C3QYX0_9AGAM
LinkDB: A0A0C3QYX0_9AGAM
Original site: A0A0C3QYX0_9AGAM 
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
//
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