SED4_CANGA
ID SED4_CANGA Reviewed; 1029 AA.
AC Q6FPI5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Putative guanine nucleotide-exchange factor SED4;
GN Name=SED4; OrderedLocusNames=CAGL0J03564g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Putative guanine nucleotide-exchange factor (GEF) involved in
CC the formation or budding of transport vesicles from the ER. Positive
CC regulator of SAR1 probably through inhibition of the GTPase activation
CC by SEC23 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000250}; Single-pass type II membrane protein
CC {ECO:0000250}. Note=In the process of transport, SED4 itself may
CC migrate to the Golgi apparatus and function in subsequent transport
CC events. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC12 family. {ECO:0000305}.
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DR EMBL; CR380956; CAG60808.1; -; Genomic_DNA.
DR RefSeq; XP_447859.1; XM_447859.1.
DR AlphaFoldDB; Q6FPI5; -.
DR SMR; Q6FPI5; -.
DR STRING; 5478.XP_447859.1; -.
DR EnsemblFungi; CAG60808; CAG60808; CAGL0J03564g.
DR GeneID; 2889700; -.
DR KEGG; cgr:CAGL0J03564g; -.
DR CGD; CAL0133628; CAGL0J03564g.
DR VEuPathDB; FungiDB:CAGL0J03564g; -.
DR eggNOG; KOG0771; Eukaryota.
DR HOGENOM; CLU_294562_0_0_1; -.
DR InParanoid; Q6FPI5; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045260; Sec12-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR23284; PTHR23284; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; ER-Golgi transport; Glycoprotein; Golgi apparatus;
KW GTPase activation; Membrane; Protein transport; Reference proteome; Repeat;
KW Signal-anchor; Transmembrane; Transmembrane helix; Transport; WD repeat.
FT CHAIN 1..1029
FT /note="Putative guanine nucleotide-exchange factor SED4"
FT /id="PRO_0000295590"
FT TOPO_DOM 1..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 366..1029
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 257..296
FT /note="WD 1"
FT REPEAT 300..339
FT /note="WD 2"
FT REGION 579..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1026..1029
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 579..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 884
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1029 AA; 112470 MW; 022AB561C0683B59 CRC64;
MVFDSEYDLG YPVYGAQFLS DGMLLVAGGG GVGVMIPNKL TALRVNFEKK KVLKRYREIT
LDSQDDSPSN LGVAQNMILM GCNEGYDKIS STGENHHIRK FVFENDHLKF IGAIDFDGST
DPEVYTKLIC MSKDGTIAAI ASSKLPTVIR IIDPIDLTEK YEIETGRDVR DIHFSPDGKL
LVYITATSLE VVSVVTGRFL FRKTDFNKAT DLARVKFIND DDFVLASGFK DKAGIALTTF
RIRNTNPTIL SSKKVFKDYK KITAMDVDPK GQLIALTTDD NSLALLSVKK LNVIKLFKQV
HKDTITRVTV SPGGQYVATG STDKTVHIFK ISPDAMGGSN LWKSLLRFLF NVMKLAVVVI
WAHLFYKYDL HHKLYDVTKV QLEKRSIEFP SFLDGILGTT TTRSTIIEGD IVSVVTDTAP
ALTSSVFSED NKEYAKVEET TPSNSWSSVS ESYWPSEVSN DIESVQENFD DIENKILENE
DVVMKNDAIE TEDESVGFDI DDTIKPIAPI DIDLELDDPL ASTSVDTSEV LSSQVPVQLE
TLSGQSEIID DKPEHLDEEV SEGFLGDHSK ANLETEIENA STSISIEEST NSHSTFIESS
SSLEEGRNTT SESSREISSE TSIIKEDMLY PTENVSEQSA TDKVNKNQSI DKIDVSSSSS
IPTSSEGSSN SIVGDEAQMH ISSLSSIETE LSSSSIMINE ESTIRNADSV VDENHSESKL
PTEAKTSIVG SIDNENIDST ELNNLEEAVK TSSNESSLSQ VTEELVKNNE RVSNQSLSTV
STEHTEMKES SNLTEKKPES NSPESNLSES SLQTHDFSQI SDTERNIVSS SAFVTDLPSE
EASVNPGNTE GTIVNASLVD SQSSNSSVKT VETNVSQDEQ TSQNETLSVG AATIDVIQGS
YTSVSDSLDG MNNEEVGNKV HIEDVSNTLE IDSSASALSE QGDNQFSDST PEVVNVINEF
TTTPENETSS PLASSSTTFM TESPSPIAVA NEVIENIQQD EQVAQQMEDT NSGSSNFQDT
QHNVINDEL
