Reviewed, UniProtKB/Swiss-Prot Q09140 (UGGG_SCHPO)

Names and origin

Protein names

Recommended name:
    UDP-glucose:glycoprotein glucosyltransferase
    EC=2.4.1.-
Alternative name(s):
    UDP--Glc:glycoprotein glucosyltransferase
      Short name=UGT

Gene names

Name:	gpt1
ORF Names:	SPBPJ4664.06

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	1448 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.1
Cofactor	Calcium or manganese. Ref.1
Pathway	Protein modification; protein glycosylation.
Subunit structure	Monomer. Ref.1
Subcellular location	Endoplasmic reticulum lumen. Ref.1
Post-translational modification	Glycosylated. Ref.1
Sequence similarities	Belongs to the glycosyltransferase 8 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular response to stress Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe protein amino acid glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Ref.1 Traceable author statement. Source: GeneDB_SPombe endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-glucose:glycoprotein glucosyltransferase activity Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Ref.1 Ref.3
	Chain	19 – 1448	1430	UDP-glucose:glycoprotein glucosyltransferase		PRO_0000012275
Regions
	Region	1149 – 1448	300	Glucosyltransferase By similarity
Amino acid modifications
	Glycosylation	66	1	N-linked (GlcNAc...) Potential
	Glycosylation	749	1	N-linked (GlcNAc...) Potential
	Glycosylation	880	1	N-linked (GlcNAc...) Potential
	Glycosylation	1046	1	N-linked (GlcNAc...) Potential
	Glycosylation	1441	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	118	1	S → T in AAB05993. Ref.1
	Sequence conflict	291	1	T → A in AAB05993. Ref.1
	Sequence conflict	295	1	T → S in AAB05993. Ref.1
	Sequence conflict	320	1	D → H in AAB05993. Ref.1
	Sequence conflict	928	1	F → L in AAB05993. Ref.1
	Sequence conflict	1199	1	S → C in AAB05993. Ref.1
	Sequence conflict	1261	1	Missing in AAB05993. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q09140-1 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: 219B692FE6BE1966	FASTA	1,448	165,469
	10 20 30 40 50 60 MRWGFWFAIA TLITICYAAK PLDVKIAATF NAPSFSALIA ESLYQEKKEG FIWYLNHLSD 70 80 90 100 110 120 LLDAENTTEK ELYINVVNSL KREYVLSDEE LSSLQFSLGL FSGAPKLQAF SSIVQSRSCD 130 140 150 160 170 180 CDTWLQLDEE SQVCFSDLPK DSPLFSKLYS KNPLDYEVVK TSATGIPYAV VVTSFERDLI 190 200 210 220 230 240 PFHELYYKLA LEGKCNYVIR YSPPSSSKLN SKLYVKGFGT HVSLKRTDYL VVDDREFPRE 250 260 270 280 290 300 KGDNPASFTS SRNKRSNERL FGMTSDSLQT VTPDKIAILD LLATQSIASS TDMLTAFREL 310 320 330 340 350 360 TQDFPIYAHY LSIQPDVSND LIEELNQFQS QYVPEGINTI WLNGLSLDLE ETDAFSILSL 370 380 390 400 410 420 IKKEKDMFDR FEALGIKSSK VLDIVTNEAF ANEDSDFKFV KFHCQDDIED WKAIHWVNEI 430 440 450 460 470 480 ESNPKYDNWP KSIQILLKPI YPGQLHMLGK QLHTVIYPIF PSSPSSLPLL SELIQFSRRP 490 500 510 520 530 540 SPVQTGMVCA ANDDDEFAQT VCKSFFYISK ESGTDSALKF LYKCLNSDSS ADLYSLLEEH 550 560 570 580 590 600 LPLSEHDDDT LANLKKDLSS SFFDHYMSKS NSWVNRLGID SSASEVIVNG RIISHDENYD 610 620 630 640 650 660 RSMYGIFLED IPEVQIAVAE GKISEDDNLL DFILRDASLT RNPLVYPSAK SSIKSIDIKR 670 680 690 700 710 720 VLENVGSLNH EDILLIGSSN AKYSFWLVAD FNEKEGLEIL SLLADLLSEN KDANLMLIQE 730 740 750 760 770 780 GKNHVVPPLF AKLLSSPKRS SKHLQEILNS SLDPSSGVVN DMDKALKFLK KSKAVVKELG 790 800 810 820 830 840 LTGECKSALL LNGRMICSFS VDSLNTADLK MLMQMEYDNY LSKLSNIAGS SRRLKNSRAI 850 860 870 880 890 900 SFLSSYLKTL ESTPMSTSSP TKEEKLFPRD FIYNKLGVGN ATFETDDFSK AYYQFVAVLD 910 920 930 940 950 960 PLSKDSQKWS AILEAVSKLN GVGVRIHFNP KQTLSELPLT RFYRYSISAE PEFDALGHLE 970 980 990 1000 1010 1020 ESYVEFDNLP ADTLLTMDIE ARDAWTVMQK DVDIDLFNIK LEHTSEAEAL DSHTAIYELK 1030 1040 1050 1060 1070 1080 NILVQGYSQE EFRKSPPRGM QLKLGNLTNS HVTDTIVLSN LGYFQLKANP GVWTLEPMDG 1090 1100 1110 1120 1130 1140 RSSQFYEILS LNKKNSYKDP QVIVDSFEGV TLNPVMRRKP GFESADIMDE DLSSHKFFDK 1150 1160 1170 1180 1190 1200 IKKSLSFFNF KRKEASINIF SVASGHLYER FLYIMTKSVI EHTDKKVKFW FIENFLSPSF 1210 1220 1230 1240 1250 1260 KSSIPAIAKK YNFEYEYITY NWPHWLRKQE EKQREIWGYK ILFLDVLFPL ELHKVIYVDA 1270 1280 1290 1300 1310 1320 DQIVRADLQE LMDMDLHGAP YGYTPMCDSR EEMEGFRFWK KGYWKKFLRG LKYHISALYV 1330 1340 1350 1360 1370 1380 VDLDRFRKMG AGDLLRRQYQ LLSADPNSLS NLDQDLPNHL QHLIPIYSLP QDWLWCETWC 1390 1400 1410 1420 1430 1440 SDESLKTAKT IDLCQNPLTK EKKLDRARRQ VSEWTSYDNE IASVLQTASS QSDKEFEEKD NNSSPDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8631292] [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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[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: 7982990] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-31, CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U38417 Genomic DNA. Translation: AAB05993.1. CU329671 Genomic DNA. Translation: CAC38351.1.
PIR	S63669.
RefSeq	NP_595281.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT24. Glycosyltransferase Family 24.
Genome annotation databases
GeneID	2541413.
KEGG	spo:SPBPJ4664.06.
NMPDR	fig|4896.1.peg.1147.
Organism-specific databases
GeneDB_Spombe	SPBPJ4664.06.
Phylogenomic databases
OMA	Q09140. EASINIF.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003364-MON.
Gene expression databases
ArrayExpress	Q09140.
Family and domain databases
InterPro	IPR009448. UDP-g_GGtrans. [Graphical view]
PANTHER	PTHR11226. UDP-g_GGtrans. 1 hit.
Pfam	PF06427. UDP-g_GGTase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UGGG_SCHPO

Accession

Primary (citable) accession number: Q09140

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	August 14, 2001
Last modified:	June 16, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)