ID A0A094FWH4_9PEZI Unreviewed; 1637 AA.
AC A0A094FWH4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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|RuleBase:RU365075};
GN ORFNames=V500_02935 {ECO:0000313|EMBL:KFY95151.1};
OS Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY95151.1, ECO:0000313|Proteomes:UP000029284};
RN [1] {ECO:0000313|EMBL:KFY95151.1, ECO:0000313|Proteomes:UP000029284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules. {ECO:0000256|ARBA:ARBA00025471}.
CC -!- SUBUNIT: Component of the conserved oligomeric Golgi complex.
CC {ECO:0000256|RuleBase:RU365075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004255}. 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}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000256|ARBA:ARBA00008334}.
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:KFY95151.1}.
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DR EMBL; JPKC01000905; KFY95151.1; -; Genomic_DNA.
DR STRING; 1420913.A0A094FWH4; -.
DR HOGENOM; CLU_003195_0_0_1; -.
DR Proteomes; UP000029284; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017119; C:Golgi transport complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd01479; Sec24-like; 1.
DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR010490; COG6.
DR InterPro; IPR048369; COG6_C.
DR InterPro; IPR048368; COG6_N.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR006900; Sec23/24_helical_dom.
DR InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR InterPro; IPR006896; Sec23/24_trunk_dom.
DR InterPro; IPR012990; Sec23_24_beta_S.
DR InterPro; IPR041742; Sec24-like_trunk_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
DR PANTHER; PTHR13803:SF39; SECRETORY 24AB, ISOFORM A; 1.
DR Pfam; PF20653; COG6_C; 1.
DR Pfam; PF06419; COG6_N; 1.
DR Pfam; PF00626; Gelsolin; 1.
DR Pfam; PF08033; Sec23_BS; 1.
DR Pfam; PF04815; Sec23_helical; 1.
DR Pfam; PF04811; Sec23_trunk; 1.
DR Pfam; PF04810; zf-Sec23_Sec24; 1.
DR SMART; SM01087; COG6; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
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:UP000029284};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365075}.
FT DOMAIN 263..299
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 337..578
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 584..667
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 678..780
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 807..864
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 996..1109
FT /note="Conserved oligomeric complex COG6 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06419"
FT DOMAIN 1140..1636
FT /note="Conserved Oligomeric Golgi complex subunit 6 C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20653"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1637 AA; 180795 MW; FF0108879411D215 CRC64;
MSAPQEGYPP QGYPQQEQYG EQQPQPGFGA AAPAPAEEHH DGHGKKKKRG YAAQAYDFGA
GGNAALGGQP PNPENFAPVG APAYGGYPAP ADQPAYGGNQ PYTDTPQPST FGQSALGGLG
GYQAPQQPAA YPAPGAPPGG DVGGITQGMG QMGIAPQAGQ PGAGAVPRVA LNQLYPTDLL
NQPFNVAEIE LPPPPIILPP NSSVTPSPDA NCSHKYIRST LNAAPTTNNL LKKSKLPFAL
VIQPYTSLHD ADDPVPVVQD QIISRCRRCR TYINPYVTFL DHGHRWRCNM CNLTNDVPQG
FDWDAATQQS VDRWQRAELN HAVVEFVAPQ EYMVRPPQPL VYLFLFDVSY NAVNNGLLAT
SARTILDSLN RIPNADRRTR LGFMAVDSSL HYFTIPKDGE ENGETNMLVV SDLDEPFLPI
PQELLVPLSE SRTNIETFLT KLPSMFQNNV ITTSCMGSAL RAGHKLISPL GGKLVVLTAT
LPNVGYGKLD LREDPKALGT SKEGALLQTQ NSFYKSFAVE CSKNQVSIDM FLFSSQYQDV
ASLSNLPRYT GGQTYFYPGW SAVRSDDAIK FASEFSDYLS SEIGLEAVLR VRATTGLRMN
TFYGNFFNRS SDLCAFPAFP RDQAYVVEVA IDETLTKNFI CMQAAVLHTT SNGERRIRVM
TLSLPTTTIL ADLYASADQC AITTYFSHKA VERALSNGLE SARESLQSKL IELLQTFKKE
LAGGNMGGGG LQFPANLRGL PTLFLGLIKN LGLRKSAQIP TDLRSAALCL LSTLPLPLMM
QYIYPRLYSL HDMPDNVGVP DPETSEIVLP SPLNLSSERL VPYGLYLITD GQTQFLWVGR
DAVPQLLEDV FGVADRTQVK VQGRWKHNPT TPIYCKGGWR PKLEAVGANI VAGGQGRPGD
ELSAVDGDTE REGYAISAKA HNDSKPKYTT MATDDEMSVL WWAGGGQSPV DGRAASPALS
STAQTPIRSN ALSSKVNSVL SASYADLEIR DALQLLDERG IENTVETRRQ LRLDIQKDVI
DSNGLVIKEF GHVAEQLRRI GQSIANLNQG CEEMRRHITA AHQETAPVLD EASDLMARKK
DVEMKQKLLQ AFSAHFVMSD DDIATLTSTA EPVNDEFFIV LNRAKQIQVD CEILLSSENQ
RLGLEIMEQV TTNLNGAFQK LYRWIQREFK SLNLENPQIN ASIRRALRVL AERPSLFQNC
LDFFAEAREH ILSDSFYTAL TGLSVTGDED KTVKPLELVA HDPLRYVGDM LAWTHSATVS
EREALEVLFI SDGNEIAKGI QAGRDSEPWN KFTRDEEEDT VFDGQKALND LVDRDVAGVA
RVLKQRIEQV IQSHDETILV YKISNLVNFY RVMFSKILSE DSALLSTLQG LEDFGLRQFR
VLMRDHISGL QTETQQPPAD LGLPIFLQDG LKQLTDIMKT YDTSFTSAKS REENFKPVLE
DAFEPYIRGI ETMAKDMEMP SNSIFIINCL LSCRTTLESY QFTAERAEEL GKTVEQHSID
LIEYQYAFFL QSSGLQRLVE TLQSLDNEPD LKKLVSTKAF QPQALKDASQ ILDDFLPSAL
MDALDNLRQL QSSRLAREIT EEAADRFCED FELVEERITQ ADGVVDRSED SEEDGEEILG
LRALFPRTSG EIRVLLT
//
