ID S9VTR3_SCHCR Unreviewed; 1418 AA.
AC S9VTR3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=UDP-glucose-glycoprotein glucosyltransferase Gpt1 {ECO:0000313|EMBL:EPY49450.1};
GN ORFNames=SPOG_01337 {ECO:0000313|EMBL:EPY49450.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY49450.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY49450.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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; KE546995; EPY49450.1; -; Genomic_DNA.
DR RefSeq; XP_013025479.1; XM_013170025.1.
DR STRING; 653667.S9VTR3; -.
DR EnsemblFungi; EPY49450; EPY49450; SPOG_01337.
DR GeneID; 25035666; -.
DR eggNOG; KOG1879; Eukaryota.
DR HOGENOM; CLU_002668_1_0_1; -.
DR OMA; DDLKYHI; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:EnsemblFungi.
DR GO; GO:0005537; F:mannose binding; IEA:EnsemblFungi.
DR GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IEA:EnsemblFungi.
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; 1.
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:UP000015464};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPY49450.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1418
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004558777"
FT DOMAIN 33..206
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 230..358
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 366..609
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 641..793
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1120..1386
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1392..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1418 AA; 162769 MW; 4949E55773CB6F53 CRC64;
MKWSIWLGFF PFISLCFAAK PIDVRVSTTF NKPSFVALLA ESLYEENRNS FLWFLDNLPL
IRTDGLSTDE HLYNRTVQYL KADNVLSQEE LTTFTYSVAL LSGVPKLAAF SSVVSSHPEG
CNTFLIFNDQ TNLCFSDLPQ GSFLYTGNYQ PTPLDYSVAY FSEALPVAVI VTDFGTDFDR
FHELYSSLAK NKECNYVIRY APAPNATMEK LYVIGSSDEK NEVLFDLASD QLETVTQDQI
ATLDMLAAEA IVTSKTPLKT LKLLVQDFPM YAQHLVSKVR LSEDLIEDVN NLQSYSIPEG
QNAVWLNGIP IDLQEADAFT ILSWLRKERQ ILSGFQKLGI EPSKASKVLS NEQFDISEAE
FKFARFHCQD DLEDNKAIFW MNEVETDTRY SKWPRSNMQL LTPIYPGQLH LIRKQLHTVI
YPIFPSSDSS FSLLSELIQF SRRPSPVQTG LVCVATEDDE FGKTICRAFH YVAKTSSKPN
ALKFLFKCLA SDPSAGAWAL VEEHMPVEDY DEETFPEIKK SLNSNIYDTI LLKSLQWSSR
LGLDPESQDV IVNGRIIAHD KHYDSNMYGI FIEDIPEIQL AVAQQMVLEE ENLLDYLLKD
AAHIRNPLIH PSSKSKVKQI DLLSLLDNIG FTYSDLLTVG NKNAKFSLLL VTDFASQEGL
GLTSMLAEVL SKFESSNLIL VQSDFDNELP TLISDLSSYT NPTNEDLRKL LKNNEKKKPA
KLTSKIKSKL AKYTEVSKAI VGNIDEPSQS MLILNGRLIN SFSIEKLGLE DLEMLLSQEK
GNYIDKLDNM LDNASQLQNQ GILPLLSSYL KKLEFDYVRG SVPGREKAMF PRDNFYNQLP
VSRLTIETEN FSSCMYQFVA ILDPLSKISQ KWSSILESIS HLDGVGVRIY LNPSKSLSDF
PLSRFYRYSI EYEPVFDNGG QFKDSLIRFD TLPADTLLTM DIESRDTWVV MQNEVDIDLY
NIKLDHTSPE ENVEPVSAVY EIKNILIQGY SQEEGLKTPP RGMQLALETP KQEHFADTIV
LANLGYFQLK ANPGIWNLKP LSGRSSQFYN IKALDKLDPS EEKQVVVDSF EGVTLYPVMR
RNPGFESSDI LDEDMSPQRF FDKMKQKLNI FKIGKKEPTI NIFSVASGHL YERFMYIMTK
SVMQHTNKKV KFWFIENFLS PSFKHSIPVL SRHYGFEYEY VTYNWPEWLR KQDEKQREIW
GYKILFLDVL FPLNLHKVIF VDADQIVRTD LQELMDLDLH GAPYGYTPMC DSREEMEGFR
FWKQGYWKKF LRGLKYHISA LYVVDLDRFR KMSAGDLLRR QYQLLSADPN SLSNLDQDLP
NNLQHLIPIY SLPQEWLWCE TWCSDQSLKK AKTIDLCQNP LTKEKKLDRA RRQVREWTTY
DNEIATLLRT AEEESSHLTS SPSVQDQPQN MEKDMDEL
//