ID W6MRL5_9ASCO Unreviewed; 924 AA.
AC W6MRL5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Guanine nucleotide-exchange factor SEC12 {ECO:0000256|RuleBase:RU369019};
GN ORFNames=KUCA_T00004979001 {ECO:0000313|EMBL:CDK28993.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK28993.1};
RN [1] {ECO:0000313|EMBL:CDK28993.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28993.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK28993.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28993.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) required for the
CC formation or budding of transport vesicles from the ER.
CC {ECO:0000256|RuleBase:RU369019}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU369019}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU369019}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU369019}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU369019}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC12 family.
CC {ECO:0000256|RuleBase:RU369019}.
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DR EMBL; HG793130; CDK28993.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MRL5; -.
DR STRING; 1382522.W6MRL5; -.
DR HOGENOM; CLU_308174_0_0_1; -.
DR OrthoDB; 2031915at2759; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IEA:UniProtKB-UniRule.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR024977; Apc4-like_WD40_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR045260; Sec12-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR23284; PROLACTIN REGULATORY ELEMENT BINDING PROTEIN; 1.
DR PANTHER; PTHR23284:SF0; PROLACTIN REGULATORY ELEMENT-BINDING PROTEIN; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU369019};
KW Membrane {ECO:0000256|RuleBase:RU369019};
KW Protein transport {ECO:0000256|RuleBase:RU369019};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369019};
KW Transmembrane {ECO:0000256|RuleBase:RU369019};
KW Transmembrane helix {ECO:0000256|RuleBase:RU369019};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU369019};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|RuleBase:RU369019}.
FT TRANSMEM 341..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369019"
FT DOMAIN 268..348
FT /note="Anaphase-promoting complex subunit 4-like WD40"
FT /evidence="ECO:0000259|Pfam:PF12894"
FT REGION 511..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..694
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..766
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..849
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 98661 MW; 5C92FA7CB3D85970 CRC64;
MVLKQFSYDV GYPVYGAKFL NEDTLLITGG GGEGNNGIPN KLTALKVDFS RPKALKKFRE
LSLLDNEDSP MSLDASKGVI ILGVNQDSAS IKNGTNKHFR KFIYSNEHLK AVDSAQISDS
RVSTEYQKLT VLTPDGAKAV IAMSKDPSTI YVVDTNDLDV QFEIKASGDV KDICISPDGK
VACYITASTL ETVSTVTGRT VLKHDSFPEF ALGKVAFLDN NTILIAGVLK QGGGVVLAEF
SIPKSAVVKS RVVSKKLKGI TSMDVSHGLV ALAGSDTSIT IVRATSLKII STTSQVHNFA
ITKITFSSDG TYLASVSAAN TVNIILIPKN FASAKSKVSS VIGFLFWSVL LGVLAMFVQW
FIQSGNAAAI FEKSVKLIKK TPHDSTPYFK IEPIAPSETF IKISSSSAYS YRSSSTTTLS
EEMFTILPVG EPDVKIGKDE PEKVATILPV GEPDVKISSD EPEQLASILP VGQPIIHTNA
ETKYVPQPDL SSSTESVQES IYREPITNTQ FDTETPHLTD DDLSVGETKS AQSASSAIIP
PREAANASGI DSALAETVYS VTESVTDSGS DIETETEREA EVQADIGIET GTEVKRVTEA
ENEFQTETGT ELVTDIDFDT ETSTDALTET DTEIQTETET EVVTETGSET QVEISMETFT
KESSVTGVIS ETETESVTES EVESVTDSEA SETDAESDVG SVTESEVSET DTESGVEPSV
TASEVESEVE SVTESEVESL TDSEVSETDA ESDVESVTES EVSETDIESA TDSRVTETKD
SEAELENFTA EDATKAKSST VSASTAEEIT STGPEVAVTP TPVKAADGEE EDIDGEADEE
NDEDDEDETV TLEVTLTSTL TQTVTEDQPE TVVTKASKST ATAEWNSAAT ATATVVEILT
VFQTIVETIV ETVTAKPLPV HDDL
//
