ID SEC12_CANGA Reviewed; 459 AA.
AC Q6FIY2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Guanine nucleotide-exchange factor SEC12;
DE AltName: Full=Protein transport protein SEC12;
GN Name=SEC12; OrderedLocusNames=CAGL0M10703g;
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138;
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: Guanine nucleotide-exchange factor (GEF) required for the
CC formation or budding of transport vesicles from the ER. This function
CC involves the cytoplasmic domain of the protein, which is thought to
CC interact with the small GTP-binding protein SAR1. Required for
CC autophagy (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}. Golgi apparatus,
CC cis-Golgi network membrane {ECO:0000250}; Single-pass type II membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC12 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR380959; CAG62790.1; -; Genomic_DNA.
DR RefSeq; XP_449812.1; XM_449812.1.
DR AlphaFoldDB; Q6FIY2; -.
DR SMR; Q6FIY2; -.
DR STRING; 284593.Q6FIY2; -.
DR GlyCosmos; Q6FIY2; 1 site, No reported glycans.
DR EnsemblFungi; CAGL0M10703g-T; CAGL0M10703g-T-p1; CAGL0M10703g.
DR GeneID; 2891377; -.
DR KEGG; cgr:CAGL0M10703g; -.
DR CGD; CAL0137173; CAGL0M10703g.
DR VEuPathDB; FungiDB:CAGL0M10703g; -.
DR eggNOG; KOG0771; Eukaryota.
DR HOGENOM; CLU_033006_0_0_1; -.
DR InParanoid; Q6FIY2; -.
DR OMA; RVEIYDW; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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 SUPFAM; SSF69322; Tricorn protease domain 2; 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..459
FT /note="Guanine nucleotide-exchange factor SEC12"
FT /id="PRO_0000295526"
FT TOPO_DOM 1..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 352..370
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000250"
FT TOPO_DOM 371..459
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REPEAT 256..291
FT /note="WD 1"
FT REPEAT 294..334
FT /note="WD 2"
FT REGION 417..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 459 AA; 50383 MW; D93B2360677EBBFB CRC64;
MKFHTKLYKV GYPLYGAKFV CDDQFVVTGG GGEGNNGVDN KLTVLKVGSS EGNGLRVDEV
CDATLPANDD SPTALDAVGD TILIGCNENS AKVKSGAGNS HVRKFRYDGK SLKFESAADI
DKSTNPEDYT KVIRLSKDGS EAAIASSKNP PSMAIIDPRN YSVKYEIETG RDVKDLHFSP
NGKLIGYITE SSLEIISTVT GSCVVRKTDF DRKIILSKMK FLDDNNVLIA ATWASSKGIL
LTKISIKSGK TTVFWSRQIS SKFKGITAMD VNDQMNLVML ATNDNSVLLV KLRNLSVGKT
FTQVHGFAIT RVIFSPDSRY AVSISAAETV HVIEIPSDFA DSRSLSESTT QWLMNTIMVL
FLAFVLNSMY KEDMHKNVLN YFRSVKSIDS SSILSMEDME QVTLVGTIST SVRSTTQRFE
SSKSVSSTSV VARTNVSEKE RSQQDPVKKS PEQHQQNQQ
//
