ID G8B775_CANPC Unreviewed; 1453 AA.
AC G8B775;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=CPAR2_103460 {ECO:0000313|CGD:CAL0000152967,
GN ECO:0000313|EMBL:CCE40308.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE40308.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
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; HE605203; CCE40308.1; -; Genomic_DNA.
DR STRING; 578454.G8B775; -.
DR EnsemblFungi; CPAR2_103460-T; CPAR2_103460-T-p1; CPAR2_103460.
DR CGD; CAL0000152967; CPAR2_103460.
DR VEuPathDB; FungiDB:CPAR2_103460; -.
DR eggNOG; KOG1879; Eukaryota.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000005221; Chromosome 1.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR PANTHER; PTHR11226; UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11226:SF0; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 55..246
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 293..416
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 449..666
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 1144..1411
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1427..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1453 AA; 166334 MW; 4A788DEB6070E75D CRC64;
MACKWSVSFF KIMIPWQWTT KVLLIVSTFS IYSSANDTGL LTVDVKAPWK RIDFVSNFIE
SIAGFNASLY IPTLEAIFGL GDSDVSEGRT DKEIYDYTMK QLSLEPSAID FVNFNLVYKK
YSPRVASHYF HYETTLQQFG DRLKTECTKD SFGNQVETKN GLVPAWVLYN DKIYCSVNDL
FALQTDKSNQ ETFLFDRVIG DSDDAPLLTF YGDPTVDQTR EFLKVLYEEA QNGKLRFVWR
YIPSVSKRVD SLPGFAVEVP TKNIEYYAHS KLDLNKDFDT IKSSRAISKI GNNVNELGIK
LTSFILSNKI KLSKFELLQT ILNNMPIFYS YLNKLPQSIN YKKVQSKVVG NEQVGLSKES
FGIYINGSPI HPLELDVYKL YDKISDELST VKNLVELGFN SVQAKLLLAK FGLLSAVKQA
QFRTGNTLMG NNENRFKVFQ HAFNRNDATK GGVVFINDIE SDRNYGEYST DRQEAYLGVE
SRKLKPNQIP PLKENVHDLI FALNLASKKQ LKAFFTFSKI ILDSGIPQQV GVLPIIGEDP
LDEQLAIRLY HITKLSDQKE ALALLYKYME STGPDEIQEL LKKVDVPTNF RVDFDTVLNK
FSIDQPSVVV NGVIHDLFSS NWQVAMSKQI EQDNSLIKTQ LRQGDVNGNL KDIIYNNAKS
ERNLRIHPLD PSEIIYKKID HDLMRSSIAF KKVDKELNNH ATIWLVSDFR DSKMIDQLVT
LLNLMKRKSI QVRVFNVGNT KLFSKLAGKM RLTVLTNADI NAIISTLKEG GEVSTGLNED
LVHSLEQKHM PVRHSYLLVN SRYFRLDPVI LNMEELSQLI EYELTQRLRL INEICVTYVD
EFPQALYEYN SMGSGLDDMD WFDLVSSIVT KSFHVDDKTF VNDVNRYDFG SLDMSNSIDY
KKHDESKQVD VLVIMDPLED NSQKLINILD AVKDFSFVNV RALFQPKLEY AREELTERFY
QGVFPPSIPY FEGSGKWDDT FLATFDALPV ATCSINMDVP KRWVVVAKSA PSDIDLNSFK
LDKNPISVSF EITNLLIEGN ARDVNTGKAP NDLQLQISNG THTDNTLVMT ALNYFQLKAL
PGVHSLSVKS NHSLLSASDN KFDPNIVEIE TAPMSLFSLN GLVLQIRVSS NRERIVEKSK
HADINIFTIA GGHEYEKLVS IMIASVKSHN LKKSIKFWIL SNFISPQFKV LIPHLIEKYS
VEIELVTYKW PTFLRKQSNR QREIWAYKIL FLDELFPQDL DRVIFVDADQ VCRTDLTELV
NMDLEGAPYA FTPMCESNKE TEGFRFWKSG YWAEVLQDDL KYHISALYVV DLSKFKSVEA
GNRLRAHYQK LSSDPNSLSN LDQDLPNNMQ RQIKIKSLPQ EWLWCETWCS SETFNEAKMI
DLCNNPLTKE NKIDTAKRLI PEWVNYEKEV LALIDQVTDT VEEEVEEDEE NFTIDESHGE
VDSDDDALYH DEL
//
