UGGG_SCHPO
ID UGGG_SCHPO Reviewed; 1448 AA.
AC Q09140;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase;
DE EC=2.4.1.-;
DE AltName: Full=UDP--Glc:glycoprotein glucosyltransferase;
DE Short=UGT;
DE Flags: Precursor;
GN Name=gpt1; ORFNames=SPBPJ4664.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-31; 148-158;
RP 401-412; 557-568; 723-730; 983-990 AND 1118-1130, FUNCTION, SUBCELLULAR
RP LOCATION, COFACTOR, SUBUNIT, AND GLYCOSYLATION.
RX PubMed=8631292; DOI=10.1002/j.1460-2075.1996.tb00406.x;
RA Fernandez F., Jannatipour M., Hellman U., Rokeach L.A., Parodi A.J.;
RT "A new stress protein: synthesis of Schizosaccharomyces pombe UDP-
RT Glc:glycoprotein glucosyltransferase mRNA is induced by stress conditions
RT but the enzyme is not essential for cell viability.";
RL EMBO J. 15:705-713(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PROTEIN SEQUENCE OF 19-31, AND CHARACTERIZATION.
RX PubMed=7982990; DOI=10.1016/s0021-9258(18)43870-7;
RA Fernandez F.S., Trombetta S.E., Hellman U., Parodi A.J.;
RT "Purification to homogeneity of UDP-glucose:glycoprotein
RT glucosyltransferase from Schizosaccharomyces pombe and apparent absence of
RT the enzyme from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 269:30701-30706(1994).
CC -!- FUNCTION: Selectively reglucosylates unfolded glycoproteins, thus
CC providing quality control for protein transport out of the ER.
CC Unfolded, denatured glycoproteins are substantially better substrates
CC for glucosylation by this enzyme than are the corresponding native
CC proteins. This protein and transient glucosylation may be involved in
CC monitoring and/or assisting the folding and assembly of newly made
CC glycoproteins, in order to identify glycoproteins that need assistance
CC in folding from chaperones. {ECO:0000269|PubMed:8631292}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:8631292};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:8631292};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8631292}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:8631292}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:8631292}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; U38417; AAB05993.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC38351.1; -; Genomic_DNA.
DR PIR; S63669; S63669.
DR RefSeq; NP_595281.1; NM_001021188.2.
DR AlphaFoldDB; Q09140; -.
DR SMR; Q09140; -.
DR BioGRID; 277921; 18.
DR STRING; 4896.SPBPJ4664.06.1; -.
DR CAZy; GT24; Glycosyltransferase Family 24.
DR iPTMnet; Q09140; -.
DR MaxQB; Q09140; -.
DR PaxDb; Q09140; -.
DR PRIDE; Q09140; -.
DR EnsemblFungi; SPBPJ4664.06.1; SPBPJ4664.06.1:pep; SPBPJ4664.06.
DR GeneID; 2541413; -.
DR KEGG; spo:SPBPJ4664.06; -.
DR PomBase; SPBPJ4664.06; gpt1.
DR VEuPathDB; FungiDB:SPBPJ4664.06; -.
DR eggNOG; KOG1879; Eukaryota.
DR HOGENOM; CLU_002668_1_0_1; -.
DR InParanoid; Q09140; -.
DR OMA; EFAIDIR; -.
DR PhylomeDB; Q09140; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q09140; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; EXP:PomBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:PomBase.
DR GO; GO:0005537; F:mannose binding; IDA:PomBase.
DR GO; GO:0051787; F:misfolded protein binding; IDA:PomBase.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IDA:PomBase.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:PomBase.
DR GO; GO:0006491; P:N-glycan processing; EXP:PomBase.
DR GO; GO:0006486; P:protein glycosylation; IDA:PomBase.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 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; PTHR11226; 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; SSF53448; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Reference proteome; Signal; Transferase.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:7982990,
FT ECO:0000269|PubMed:8631292"
FT CHAIN 19..1448
FT /note="UDP-glucose:glycoprotein glucosyltransferase"
FT /id="PRO_0000012275"
FT REGION 1149..1448
FT /note="Glucosyltransferase"
FT /evidence="ECO:0000250"
FT REGION 1428..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1046
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 118
FT /note="S -> T (in Ref. 1; AAB05993)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="T -> A (in Ref. 1; AAB05993)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="T -> S (in Ref. 1; AAB05993)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="D -> H (in Ref. 1; AAB05993)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="F -> L (in Ref. 1; AAB05993)"
FT /evidence="ECO:0000305"
FT CONFLICT 1199
FT /note="S -> C (in Ref. 1; AAB05993)"
FT /evidence="ECO:0000305"
FT CONFLICT 1261
FT /note="Missing (in Ref. 1; AAB05993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1448 AA; 165469 MW; 219B692FE6BE1966 CRC64;
MRWGFWFAIA TLITICYAAK PLDVKIAATF NAPSFSALIA ESLYQEKKEG FIWYLNHLSD
LLDAENTTEK ELYINVVNSL KREYVLSDEE LSSLQFSLGL FSGAPKLQAF SSIVQSRSCD
CDTWLQLDEE SQVCFSDLPK DSPLFSKLYS KNPLDYEVVK TSATGIPYAV VVTSFERDLI
PFHELYYKLA LEGKCNYVIR YSPPSSSKLN SKLYVKGFGT HVSLKRTDYL VVDDREFPRE
KGDNPASFTS SRNKRSNERL FGMTSDSLQT VTPDKIAILD LLATQSIASS TDMLTAFREL
TQDFPIYAHY LSIQPDVSND LIEELNQFQS QYVPEGINTI WLNGLSLDLE ETDAFSILSL
IKKEKDMFDR FEALGIKSSK VLDIVTNEAF ANEDSDFKFV KFHCQDDIED WKAIHWVNEI
ESNPKYDNWP KSIQILLKPI YPGQLHMLGK QLHTVIYPIF PSSPSSLPLL SELIQFSRRP
SPVQTGMVCA ANDDDEFAQT VCKSFFYISK ESGTDSALKF LYKCLNSDSS ADLYSLLEEH
LPLSEHDDDT LANLKKDLSS SFFDHYMSKS NSWVNRLGID SSASEVIVNG RIISHDENYD
RSMYGIFLED IPEVQIAVAE GKISEDDNLL DFILRDASLT RNPLVYPSAK SSIKSIDIKR
VLENVGSLNH EDILLIGSSN AKYSFWLVAD FNEKEGLEIL SLLADLLSEN KDANLMLIQE
GKNHVVPPLF AKLLSSPKRS SKHLQEILNS SLDPSSGVVN DMDKALKFLK KSKAVVKELG
LTGECKSALL LNGRMICSFS VDSLNTADLK MLMQMEYDNY LSKLSNIAGS SRRLKNSRAI
SFLSSYLKTL ESTPMSTSSP TKEEKLFPRD FIYNKLGVGN ATFETDDFSK AYYQFVAVLD
PLSKDSQKWS AILEAVSKLN GVGVRIHFNP KQTLSELPLT RFYRYSISAE PEFDALGHLE
ESYVEFDNLP ADTLLTMDIE ARDAWTVMQK DVDIDLFNIK LEHTSEAEAL DSHTAIYELK
NILVQGYSQE EFRKSPPRGM QLKLGNLTNS HVTDTIVLSN LGYFQLKANP GVWTLEPMDG
RSSQFYEILS LNKKNSYKDP QVIVDSFEGV TLNPVMRRKP GFESADIMDE DLSSHKFFDK
IKKSLSFFNF KRKEASINIF SVASGHLYER FLYIMTKSVI EHTDKKVKFW FIENFLSPSF
KSSIPAIAKK YNFEYEYITY NWPHWLRKQE EKQREIWGYK ILFLDVLFPL ELHKVIYVDA
DQIVRADLQE LMDMDLHGAP YGYTPMCDSR EEMEGFRFWK KGYWKKFLRG LKYHISALYV
VDLDRFRKMG AGDLLRRQYQ LLSADPNSLS NLDQDLPNHL QHLIPIYSLP QDWLWCETWC
SDESLKTAKT IDLCQNPLTK EKKLDRARRQ VSEWTSYDNE IASVLQTASS QSDKEFEEKD
NNSSPDEL
