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Database: UniProt
Entry: A0A1E3P489_WICAA
LinkDB: A0A1E3P489_WICAA
Original site: A0A1E3P489_WICAA 
ID   A0A1E3P489_WICAA        Unreviewed;      1430 AA.
AC   A0A1E3P489;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Glycosyltransferase family 24 protein {ECO:0000313|EMBL:ODQ60014.1};
GN   ORFNames=WICANDRAFT_30048 {ECO:0000313|EMBL:ODQ60014.1};
OS   Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL
OS   Y-366-8) (Yeast) (Hansenula anomala).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=683960 {ECO:0000313|EMBL:ODQ60014.1, ECO:0000313|Proteomes:UP000094112};
RN   [1] {ECO:0000313|EMBL:ODQ60014.1, ECO:0000313|Proteomes:UP000094112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8
RC   {ECO:0000313|Proteomes:UP000094112};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC       {ECO:0000256|ARBA:ARBA00006351}.
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DR   EMBL; KV454210; ODQ60014.1; -; Genomic_DNA.
DR   RefSeq; XP_019039221.1; XM_019181679.1.
DR   STRING; 683960.A0A1E3P489; -.
DR   GeneID; 30198925; -.
DR   OrthoDB; 1734at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000094112; Unassembled WGS sequence.
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   CDD; cd06432; GT8_HUGT1_C_like; 1.
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   InterPro; IPR040525; UGGT_TRXL_4.
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; 2.
DR   Pfam; PF18403; Thioredoxin_15; 1.
DR   Pfam; PF06427; UDP-g_GGTase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094112};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ODQ60014.1}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1430
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009133646"
FT   DOMAIN          30..220
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18400"
FT   DOMAIN          273..405
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18401"
FT   DOMAIN          420..534
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18402"
FT   DOMAIN          558..624
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18402"
FT   DOMAIN          649..821
FT                   /note="UDP-glucose:glycoprotein glucosyltransferase
FT                   thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18403"
FT   DOMAIN          1125..1392
FT                   /note="Glucosyltransferase 24 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF18404"
FT   REGION          1404..1430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1430 AA;  163942 MW;  878E0853AD422242 CRC64;
     MLRSILVTTL LFASTVLGQI DIQLQANWEN PPFTLRLLET ITSENESYYL QALSKISSIS
     LDEEDSELQE DLNDEDLYNS LFDLLTPTER SLYNIPLANK YYSPRIITHY KYYNETVLPE
     FESKLQKKCG AVPKTWVQFN DVVYCKPDDV FALMTDGGSD ESESLLPFDR IIGDSGPLLV
     LYGDVNDSEF KPFISNLYDS AKYGKLRFVW RYVPQNVDQR EQLAGYGVDL TLKRTDYIVI
     DDRDAEINQK NKLKQQQVLK DQDTPSSFLD IYQQDIPAVS KEALKDLDLK IASFAVASKN
     SSENYENLVK AVQDLPKYSS YLSELEINED LIEQAEFNEK IGLTSDSSAI FINGLPVDDA
     DLNVFGLYKT VKRELNFVKQ LNDVGIDSNT AKTVLGKFAL LSISKNRRGS KTRYDIEAGE
     NNPVIFFNDI ENDPIYTHLL DDLSVYLERQ QFGQIPLYRG NVHDVVFAIN FGDDDQYKIL
     KRLSQAILQR GIPQRIGIIP LVNSEEDAIH ANNIYYLLEN GGLKKVLKYV NKIGTGSPKR
     LTDGDFVSKY VDPFVSSFDV QNPSIVVNGV FFNLDDNWPY ALTRQVTEDV NLIATLVYTN
     TIKESDSVKE KAFEGAATFR NTIVVPENRA DIQYKAITPQ FQEAMKSSSN YIFEFSNSKR
     AKPVQTLTFG GNLGSKIGLQ QLVEILKFAF AANYDMKIRV INNSDEATFI GKIRQALNRS
     IDHAIDVIQE IIEEHEFTET DENQGIKDLL KLADIESTKF LLLNGRYIEL KDELLKSDAL
     EYLSNYEFEM RLELVGKVIK NHGIPEHGEY HDWFESFSSI LTKTFYIGTD LFTPAPLPRF
     DFGAIKKDYA ISFGDQGQSD LHVLLVIDPV EEISQKLLFL IQSIKDLSFV SLDILIQPQK
     DLESLPIKRF FRGNYKSGVE FKDGKVFESP FVSFDKAPEK TLFTLDLDVP SSWIVVPKES
     ISDLDNVLLD QSGPVTGIYE LENIAVEGNS FDINTREPPT GLSVQIKGSD TNVMTNYGYL
     QLKGNPGLWD FEIKQGKSSE IYSLLSIDDF ESEELEKHDK IQFSVLNLDG VRIFPRVMKN
     PGKENESLVL SDSSISTQVE KQEEENKPGF LQKLFQKKTK KQADINIFTI ASGHLYERFL
     SIMTASVMRH TKHTVKFWLI ENYMSPSFKK FLPHLAKKYG FEYELITYKW PSWLRGQREK
     QRTIWGYKIL FLDVLFPQDL DKVIFVDADQ IVRTDLKELV DMDLEGAPYG YTPMGDSREE
     MEGFRFWKQG YWAKFLGDEM KYHISALYVV DLKRFREIAA GDMLRQHYQA LSKDPNSLSN
     LDQDLPNNLQ TRLKIFSLPQ DWLWCETWCD DESLKTAKTI DLCNNPLTKE PKLDRARRQI
     PEWTKYDNEI AALRDQVRKL EHIYEETTES YDESTSTGVP ESENTVHDEL
//
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