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Q9JLA3 (UGGG1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Interacts with METTL23 By similarity. Ref.4

Subcellular location

Endoplasmic reticulum lumen. Endoplasmic reticulum-Golgi intermediate compartment Ref.6 PubMed 1840423.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242 Ref.2
Chain43 – 15511509UDP-glucose:glycoprotein glucosyltransferase 1
PRO_0000012273

Regions

Region1244 – 1551308Glucosyltransferase
Motif1548 – 15514Prevents secretion from ER Potential

Amino acid modifications

Modified residue12771Phosphoserine By similarity
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential
Glycosylation10151N-linked (GlcNAc...) Potential
Glycosylation12281N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis13581D → A: Inactive. Ref.2
Mutagenesis13601D → A: Inactive. Ref.2
Mutagenesis14531Q → A: Less than 2% activity retained. Ref.2
Mutagenesis14571N → A: Less than 15% activity retained. Ref.2
Sequence conflict121A → C in AAF67072. Ref.2
Sequence conflict441S → R AA sequence Ref.2
Sequence conflict324 – 3252QD → MV AA sequence Ref.2
Sequence conflict9691F → H AA sequence Ref.2
Sequence conflict11651L → K AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9JLA3 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: FD4A1B6BCCBF7738

FASTA1,551176,431
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF200359 mRNA. Translation: AAF67072.1. Different initiation.
RefSeqNP_598280.1. NM_133596.1.
XP_006244796.1. XM_006244734.1.
UniGeneRn.162227.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9JLA3. 3 interactions.
MINTMINT-4568455.
STRING10116.ENSRNOP00000020558.

Protein family/group databases

CAZyGT24. Glycosyltransferase Family 24.

Proteomic databases

PaxDbQ9JLA3.
PRIDEQ9JLA3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000020558; ENSRNOP00000020558; ENSRNOG00000014901.
GeneID171129.
KEGGrno:171129.
UCSCRGD:619710. rat.

Organism-specific databases

CTD56886.
RGD619710. Uggt1.

Phylogenomic databases

eggNOGNOG320899.
GeneTreeENSGT00390000004600.
HOGENOMHOG000184622.
HOVERGENHBG079469.
InParanoidQ9JLA3.
KOK11718.
OMARDYLDLT.
OrthoDBEOG75J0M7.
PhylomeDBQ9JLA3.
TreeFamTF300320.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ9JLA3.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view]
PANTHERPTHR11226. PTHR11226. 1 hit.
PfamPF06427. UDP-g_GGTase. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio621894.
PROQ9JLA3.

Entry information

Entry nameUGGG1_RAT
AccessionPrimary (citable) accession number: Q9JLA3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways