Q9JLA3 (UGGG1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-glucose:glycoprotein glucosyltransferase 1
Short name=UGT1
Short name=rUGT1
EC=2.4.1.-

Alternative name(s):
UDP--Glc:glycoprotein glucosyltransferase
UDP-glucose ceramide glucosyltransferase-like 1

Gene names

Name:	Uggt1
Synonyms:	Gt, Ugcgl1, Uggt, Ugt1, Ugtr

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1551 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	Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Ref.2 Ref.7 Ref.8
Cofactor	Calcium. Ref.5
Pathway	Protein modification; protein glycosylation.
Subunit structure	Monomer as well as in a tight complex with SEP15. Ref.4
Subcellular location	Endoplasmic reticulum lumen. Endoplasmic reticulum-Golgi intermediate compartment Ref.6.
Domain	N-terminal non-catalytic domain is assumed to mediate recognition of proteins with partial folding defects.
Sequence similarities	Belongs to the glycosyltransferase 8 family. Ref.2
Biophysicochemical properties	Kinetic parameters: KM=44 µM for UDP-glucose (in the presence of 0.5 µM denatured acid phosphatase) Ref.2 Ref.5 Vmax=34 pmol/h/mg enzyme toward UDP-glucose (in the presence of 0.5 µM denatured acid phosphatase) Ref.2 pH dependence: Optimum pH is 7.6-8.0. Ref.5
Sequence caution	The sequence AAF67072.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	'de novo' posttranslational protein folding Traceable author statement Ref.2. Source: UniProtKB protein glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum lumen Inferred from direct assay Ref.6. Source: UniProtKB endoplasmic reticulum-Golgi intermediate compartment Inferred from direct assay Ref.6. Source: UniProtKB
Molecular function	UDP-glucose:glycoprotein glucosyltransferase activity Inferred from direct assay Ref.2. Source: UniProtKB unfolded protein binding Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 42	42	Ref.2
	Chain	43 – 1551	1509	UDP-glucose:glycoprotein glucosyltransferase 1		PRO_0000012273
Regions
	Region	1244 – 1551	308	Glucosyltransferase
	Motif	1548 – 1551	4	Prevents secretion from ER Potential
Amino acid modifications
	Modified residue	738	1	Phosphoserine By similarity
	Modified residue	741	1	Phosphotyrosine By similarity
	Modified residue	748	1	Phosphoserine By similarity
	Glycosylation	269	1	N-linked (GlcNAc...) Potential
	Glycosylation	536	1	N-linked (GlcNAc...) Potential
	Glycosylation	1015	1	N-linked (GlcNAc...) Potential
	Glycosylation	1228	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	1358	1	D → A: Inactive. Ref.2
	Mutagenesis	1360	1	D → A: Inactive. Ref.2
	Mutagenesis	1453	1	Q → A: Less than 2% activity retained. Ref.2
	Mutagenesis	1457	1	N → A: Less than 15% activity retained. Ref.2
	Sequence conflict	12	1	A → C in AAF67072. Ref.2
	Sequence conflict	44	1	S → R AA sequence Ref.2
	Sequence conflict	324 – 325	2	QD → MV AA sequence Ref.2
	Sequence conflict	969	1	F → H AA sequence Ref.2
	Sequence conflict	1165	1	L → K AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9JLA3 [UniParc]. Last modified March 3, 2009. Version 2. Checksum: FD4A1B6BCCBF7738	FASTA	1,551	176,431
	10 20 30 40 50 60 MCSRGDANAA GAAAARRVTG LCYNMGLLIA LALLCLFSLA EANSKAITTS LTTKWFSAPL 70 80 90 100 110 120 LLEASEFLAE DSQEKFWSFV EASQNIGSSD QHDTDRSYYD AILEAAFRFL SPLQQNLLKF 130 140 150 160 170 180 CLSLRSYSAS IQAFQQIAVD EPPPEGCKSF LSVHGKQTCD LGTLESLLLT APDRPKPLLF 190 200 210 220 230 240 KGDHRYPSSN PESPVVIFYS EIGHEEFSNI HHQLISKSNE GKINYVFRHY ISNPRKEPVH 250 260 270 280 290 300 LSGYGVELAI KSTEYKAKDD TQVKGTEVNT TVIGENDPID EVQGFLFGKL RELYPSLEGQ 310 320 330 340 350 360 LKEFRKHLVE STNEMAPLKV WQLQDLSFQT AARILAAPVE LALVVMKDIS QNFPTKARAI 370 380 390 400 410 420 TKTAVSAQLR AEVEENQKYF KGTIGLQPGD SALFINGLHI DLDTQDIFSL FDTLRNEARV 430 440 450 460 470 480 MEGLHRLGIE GLSLHNILKL NIQPSETDYA VDIRSPAISW VNNLEVDSRY NSWPSSLQEL 490 500 510 520 530 540 LRPTFPGVIR QIRKNLHNMV FIVDPVHETT AELVSIAEMF LSNHIPLRIG FIFVVNDSED 550 560 570 580 590 600 VDGMQDAGVA VLRAYNYVGQ EVDGYHAFQT LTQIYNKVRT GEKVKVEHVV SVLEKKYPYV 610 620 630 640 650 660 EVNSILGIDS AYDQNRKEAR GYYEQTGVGP LPVVLFNGMP FEKEQLDPDE LETITMHKIL 670 680 690 700 710 720 ETTTFFQRAV YLGELSHDQD VVEYIMNQPN VVPRINSRIL TAKREYLDLT ASNNFYVDDF 730 740 750 760 770 780 ARFSALDSRG KTAAIANSMN YLTKKGMSSK EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD 790 800 810 820 830 840 AIKHQKTSNN VRISMINNPS REISDSSTPV SRAIWAALQT QTSNSAKNFI TKMVKEETAE 850 860 870 880 890 900 ALAAGVDIGE FSVGGMDVSL FKEVFESSRM DFILSHALYC RDVLKLKKGQ RVVISNGRII 910 920 930 940 950 960 GPLEDSELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV DALLSAQPKG 970 980 990 1000 1010 1020 EARIEYQFFE DKHSAIKLKP KEGETYYDVV AVVDPVTREA QRLAPLLLVL AQLINMSLRV 1030 1040 1050 1060 1070 1080 FMNCQSKLSD MPLKSFYRYV LEPEISFTAD NSFAKGPIAK FLDMPQSPLF TLNLNTPESW 1090 1100 1110 1120 1130 1140 MVESVRTPYD LDNIYLEEVD SIVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP 1150 1160 1170 1180 1190 1200 TTVDTIVMAN LGYFQLKANP GAWILRLRKG RSDDIYRIYS HDGTDSPPDA NDVVVILNNF 1210 1220 1230 1240 1250 1260 KSKIIKVKVQ KKADMANEDL LSDGTNENES GFWDSFKWGF SGQKTEEVKQ DKDDIINIFS 1270 1280 1290 1300 1310 1320 VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK EFIPYMAKKY NFQYELVQYK 1330 1340 1350 1360 1370 1380 WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY 1390 1400 1410 1420 1430 1440 GYTPFCDSRR EMDGYRFWKS GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG 1450 1460 1470 1480 1490 1500 LSQDPNSLSN LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE 1510 1520 1530 1540 1550 PKLEAAVRIV PEWQDYDQEI KQLQTLFQEE KELGTLHEEE TQEGSQKHEE L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed: 15057822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"Cloning and characterization of mammalian UDP-glucose glycoprotein:glucosyltransferase and the development of a specific substrate for this enzyme." Tessier D.C., Dignard D., Zapun A., Radominska-Pandya A., Parodi A.J., Bergeron J.J.M., Thomas D.Y. Glycobiology 10:403-412(2000) [PubMed: 10764828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-1551, PROTEIN SEQUENCE OF 43-59; 223-237; 256-267; 293-302; 307-315; 320-328; 440-456; 732-744; 764-776; 779-783; 950-958; 968-972; 1035-1056; 1158-1165; 1170-1179; 1239-1244; 1301-1308; 1314-1319; 1354-1368 AND 1400-1411, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-1358; ASP-1360; GLN-1453 AND ASN-1457. Strain: Sprague-Dawley. Tissue: Liver.
[3]	Lubec G., Kang S.U., Lubec S. Submitted (SEP-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 46-54; 950-959; 1028-1034 AND 1273-1283, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain.
[4]	"Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells." Korotkov K.V., Kumaraswamy E., Zhou Y., Hatfield D.L., Gladyshev V.N. J. Biol. Chem. 276:15330-15336(2001) [PubMed: 11278576] [Abstract] Cited for: PROTEIN SEQUENCE OF 55-75; 554-577; 668-691 AND 890-910, INTERACTION WITH SEP15.
[5]	"Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase." Trombetta S.E., Parodi A.J. J. Biol. Chem. 267:9236-9240(1992) [PubMed: 1533626] [Abstract] Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[6]	"Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control." Zuber C., Fan J.-Y., Guhl B., Parodi A., Fessler J.H., Parker C., Roth J. Proc. Natl. Acad. Sci. U.S.A. 98:10710-10715(2001) [PubMed: 11535823] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation." Taylor S.C., Ferguson A.D., Bergeron J.J.M., Thomas D.Y. Nat. Struct. Mol. Biol. 11:128-134(2004) [PubMed: 14730348] [Abstract] Cited for: FUNCTION.
[8]	"Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT." Ritter C., Quirin K., Kowarik M., Helenius A. EMBO J. 24:1730-1738(2005) [PubMed: 15861139] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF200359 mRNA. Translation: AAF67072.1. Different initiation.
IPI	IPI00205519.
RefSeq	NP_598280.1. NM_133596.1.
UniGene	Rn.162227.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9JLA3. 1 interaction.
STRING	Q9JLA3.
Protein family/group databases
CAZy	GT24. Glycosyltransferase Family 24.
Proteomic databases
PRIDE	Q9JLA3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000020558; ENSRNOP00000020558; ENSRNOG00000014901.
GeneID	171129.
KEGG	rno:171129.
UCSC	NM_133596. rat.
Organism-specific databases
CTD	56886.
RGD	619710. Uggt1.
Phylogenomic databases
eggNOG	roNOG07773.
GeneTree	ENSGT00390000004600.
HOVERGEN	HBG079469.
InParanoid	Q9JLA3.
OrthoDB	EOG46WZ7H.
Gene expression databases
ArrayExpress	Q9JLA3.
Genevestigator	Q9JLA3.
GermOnline	ENSRNOG00000014901. Rattus norvegicus.
Family and domain databases
InterPro	IPR009448. UDP-g_GGtrans. [Graphical view]
KO	K11718.
PANTHER	PTHR11226. UDP-g_GGtrans. 1 hit.
Pfam	PF06427. UDP-g_GGTase. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	621894.

Entry information

Entry name

UGGG1_RAT

Accession

Primary (citable) accession number: Q9JLA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	March 3, 2009
Last modified:	December 14, 2011
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program