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Protein

UDP-glucose:glycoprotein glucosyltransferase

Gene

gpt1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Selectively reglucosylates unfolded glycoproteins, thus providing quality control for protein transport out of the ER. Unfolded, denatured glycoproteins are substantially better substrates for glucosylation by this enzyme than are the corresponding native proteins. This protein and transient glucosylation may be involved in monitoring and/or assisting the folding and assembly of newly made glycoproteins, in order to identify glycoproteins that need assistance in folding from chaperones.1 Publication

Cofactori

Ca2+1 Publication, Mn2+1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

  • calcium ion binding Source: PomBase
  • mannose binding Source: PomBase
  • misfolded protein binding Source: PomBase
  • UDP-glucose:glycoprotein glucosyltransferase activity Source: PomBase

GO - Biological processi

  • (1->6)-beta-D-glucan biosynthetic process Source: PomBase
  • cellular response to misfolded protein Source: PomBase
  • endoplasmic reticulum unfolded protein response Source: PomBase
  • protein glycosylation Source: PomBase
  • UDP-glucosylation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-SPO-901032. ER Quality Control Compartment (ERQC).
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT24. Glycosyltransferase Family 24.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucose:glycoprotein glucosyltransferase (EC:2.4.1.-)
Alternative name(s):
UDP--Glc:glycoprotein glucosyltransferase
Short name:
UGT
Gene namesi
Name:gpt1
ORF Names:SPBPJ4664.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBPJ4664.06.
PomBaseiSPBPJ4664.06. gpt1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18182 PublicationsAdd
BLAST
Chaini19 – 14481430UDP-glucose:glycoprotein glucosyltransferasePRO_0000012275Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence analysis
Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence analysis
Glycosylationi880 – 8801N-linked (GlcNAc...)Sequence analysis
Glycosylationi1046 – 10461N-linked (GlcNAc...)Sequence analysis
Glycosylationi1441 – 14411N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ09140.
PRIDEiQ09140.

Interactioni

Subunit structurei

Monomer.1 Publication

GO - Molecular functioni

  • misfolded protein binding Source: PomBase

Protein-protein interaction databases

BioGridi277921. 14 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ09140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1149 – 1448300GlucosyltransferaseBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000184622.
InParanoidiQ09140.
KOiK11718.
OMAiNEAFANE.
OrthoDBiEOG7MSMX7.
PhylomeDBiQ09140.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view]
PANTHERiPTHR11226. PTHR11226. 1 hit.
PfamiPF01501. Glyco_transf_8. 1 hit.
PF06427. UDP-g_GGTase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q09140-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRWGFWFAIA TLITICYAAK PLDVKIAATF NAPSFSALIA ESLYQEKKEG
60 70 80 90 100
FIWYLNHLSD LLDAENTTEK ELYINVVNSL KREYVLSDEE LSSLQFSLGL
110 120 130 140 150
FSGAPKLQAF SSIVQSRSCD CDTWLQLDEE SQVCFSDLPK DSPLFSKLYS
160 170 180 190 200
KNPLDYEVVK TSATGIPYAV VVTSFERDLI PFHELYYKLA LEGKCNYVIR
210 220 230 240 250
YSPPSSSKLN SKLYVKGFGT HVSLKRTDYL VVDDREFPRE KGDNPASFTS
260 270 280 290 300
SRNKRSNERL FGMTSDSLQT VTPDKIAILD LLATQSIASS TDMLTAFREL
310 320 330 340 350
TQDFPIYAHY LSIQPDVSND LIEELNQFQS QYVPEGINTI WLNGLSLDLE
360 370 380 390 400
ETDAFSILSL IKKEKDMFDR FEALGIKSSK VLDIVTNEAF ANEDSDFKFV
410 420 430 440 450
KFHCQDDIED WKAIHWVNEI ESNPKYDNWP KSIQILLKPI YPGQLHMLGK
460 470 480 490 500
QLHTVIYPIF PSSPSSLPLL SELIQFSRRP SPVQTGMVCA ANDDDEFAQT
510 520 530 540 550
VCKSFFYISK ESGTDSALKF LYKCLNSDSS ADLYSLLEEH LPLSEHDDDT
560 570 580 590 600
LANLKKDLSS SFFDHYMSKS NSWVNRLGID SSASEVIVNG RIISHDENYD
610 620 630 640 650
RSMYGIFLED IPEVQIAVAE GKISEDDNLL DFILRDASLT RNPLVYPSAK
660 670 680 690 700
SSIKSIDIKR VLENVGSLNH EDILLIGSSN AKYSFWLVAD FNEKEGLEIL
710 720 730 740 750
SLLADLLSEN KDANLMLIQE GKNHVVPPLF AKLLSSPKRS SKHLQEILNS
760 770 780 790 800
SLDPSSGVVN DMDKALKFLK KSKAVVKELG LTGECKSALL LNGRMICSFS
810 820 830 840 850
VDSLNTADLK MLMQMEYDNY LSKLSNIAGS SRRLKNSRAI SFLSSYLKTL
860 870 880 890 900
ESTPMSTSSP TKEEKLFPRD FIYNKLGVGN ATFETDDFSK AYYQFVAVLD
910 920 930 940 950
PLSKDSQKWS AILEAVSKLN GVGVRIHFNP KQTLSELPLT RFYRYSISAE
960 970 980 990 1000
PEFDALGHLE ESYVEFDNLP ADTLLTMDIE ARDAWTVMQK DVDIDLFNIK
1010 1020 1030 1040 1050
LEHTSEAEAL DSHTAIYELK NILVQGYSQE EFRKSPPRGM QLKLGNLTNS
1060 1070 1080 1090 1100
HVTDTIVLSN LGYFQLKANP GVWTLEPMDG RSSQFYEILS LNKKNSYKDP
1110 1120 1130 1140 1150
QVIVDSFEGV TLNPVMRRKP GFESADIMDE DLSSHKFFDK IKKSLSFFNF
1160 1170 1180 1190 1200
KRKEASINIF SVASGHLYER FLYIMTKSVI EHTDKKVKFW FIENFLSPSF
1210 1220 1230 1240 1250
KSSIPAIAKK YNFEYEYITY NWPHWLRKQE EKQREIWGYK ILFLDVLFPL
1260 1270 1280 1290 1300
ELHKVIYVDA DQIVRADLQE LMDMDLHGAP YGYTPMCDSR EEMEGFRFWK
1310 1320 1330 1340 1350
KGYWKKFLRG LKYHISALYV VDLDRFRKMG AGDLLRRQYQ LLSADPNSLS
1360 1370 1380 1390 1400
NLDQDLPNHL QHLIPIYSLP QDWLWCETWC SDESLKTAKT IDLCQNPLTK
1410 1420 1430 1440
EKKLDRARRQ VSEWTSYDNE IASVLQTASS QSDKEFEEKD NNSSPDEL
Length:1,448
Mass (Da):165,469
Last modified:August 14, 2001 - v2
Checksum:i219B692FE6BE1966
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181S → T in AAB05993 (PubMed:8631292).Curated
Sequence conflicti291 – 2911T → A in AAB05993 (PubMed:8631292).Curated
Sequence conflicti295 – 2951T → S in AAB05993 (PubMed:8631292).Curated
Sequence conflicti320 – 3201D → H in AAB05993 (PubMed:8631292).Curated
Sequence conflicti928 – 9281F → L in AAB05993 (PubMed:8631292).Curated
Sequence conflicti1199 – 11991S → C in AAB05993 (PubMed:8631292).Curated
Sequence conflicti1261 – 12611Missing in AAB05993 (PubMed:8631292).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38417 Genomic DNA. Translation: AAB05993.1.
CU329671 Genomic DNA. Translation: CAC38351.1.
PIRiS63669.
RefSeqiNP_595281.1. NM_001021188.2.

Genome annotation databases

EnsemblFungiiSPBPJ4664.06.1; SPBPJ4664.06.1:pep; SPBPJ4664.06.
GeneIDi2541413.
KEGGispo:SPBPJ4664.06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38417 Genomic DNA. Translation: AAB05993.1.
CU329671 Genomic DNA. Translation: CAC38351.1.
PIRiS63669.
RefSeqiNP_595281.1. NM_001021188.2.

3D structure databases

ProteinModelPortaliQ09140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277921. 14 interactions.

Protein family/group databases

CAZyiGT24. Glycosyltransferase Family 24.

Proteomic databases

MaxQBiQ09140.
PRIDEiQ09140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBPJ4664.06.1; SPBPJ4664.06.1:pep; SPBPJ4664.06.
GeneIDi2541413.
KEGGispo:SPBPJ4664.06.

Organism-specific databases

EuPathDBiFungiDB:SPBPJ4664.06.
PomBaseiSPBPJ4664.06. gpt1.

Phylogenomic databases

HOGENOMiHOG000184622.
InParanoidiQ09140.
KOiK11718.
OMAiNEAFANE.
OrthoDBiEOG7MSMX7.
PhylomeDBiQ09140.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-SPO-901032. ER Quality Control Compartment (ERQC).

Miscellaneous databases

PROiQ09140.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view]
PANTHERiPTHR11226. PTHR11226. 1 hit.
PfamiPF01501. Glyco_transf_8. 1 hit.
PF06427. UDP-g_GGTase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new stress protein: synthesis of Schizosaccharomyces pombe UDP--Glc:glycoprotein glucosyltransferase mRNA is induced by stress conditions but the enzyme is not essential for cell viability."
    Fernandez F., Jannatipour M., Hellman U., Rokeach L.A., Parodi A.J.
    EMBO J. 15:705-713(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-31; 148-158; 401-412; 557-568; 723-730; 983-990 AND 1118-1130, FUNCTION, SUBCELLULAR LOCATION, COFACTOR, SUBUNIT, GLYCOSYLATION.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae."
    Fernandez F.S., Trombetta S.E., Hellman U., Parodi A.J.
    J. Biol. Chem. 269:30701-30706(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-31, CHARACTERIZATION.

Entry informationi

Entry nameiUGGG_SCHPO
AccessioniPrimary (citable) accession number: Q09140
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: August 14, 2001
Last modified: June 8, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.