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Q9JLA3

- UGGG1_RAT

UniProt

Q9JLA3 - UGGG1_RAT

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Protein

UDP-glucose:glycoprotein glucosyltransferase 1

Gene

Uggt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Cofactori

Ca2+1 Publication

Kineticsi

  1. KM=44 µM for UDP-glucose (in the presence of 0.5 µM denatured acid phosphatase)2 Publications

Vmax=34 pmol/h/mg enzyme toward UDP-glucose (in the presence of 0.5 µM denatured acid phosphatase)2 Publications

pH dependencei

Optimum pH is 7.6-8.0.2 Publications

Pathwayi

GO - Molecular functioni

  1. UDP-glucose:glycoprotein glucosyltransferase activity Source: UniProtKB
  2. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: UniProtKB
  2. protein folding Source: RGD
  3. protein glycosylation Source: UniProtKB-UniPathway
  4. UDP-glucosylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_196403. ER Quality Control Compartment (ERQC).
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT24. Glycosyltransferase Family 24.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucose:glycoprotein glucosyltransferase 1 (EC:2.4.1.-)
Short name:
UGT1
Short name:
rUGT1
Alternative name(s):
UDP--Glc:glycoprotein glucosyltransferase
UDP-glucose ceramide glucosyltransferase-like 1
Gene namesi
Name:Uggt1
Synonyms:Gt, Ugcgl1, UggtImported, Ugt1, Ugtr1 Publication
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi619710. Uggt1.

Subcellular locationi

Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation. Endoplasmic reticulum-Golgi intermediate compartment 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: RGD
  2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  3. endoplasmic reticulum lumen Source: UniProtKB
  4. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1358 – 13581D → A: Inactive. 1 Publication
Mutagenesisi1360 – 13601D → A: Inactive. 1 Publication
Mutagenesisi1453 – 14531Q → A: Less than 2% activity retained. 1 Publication
Mutagenesisi1457 – 14571N → A: Less than 15% activity retained. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 42421 PublicationAdd
BLAST
Chaini43 – 15511509UDP-glucose:glycoprotein glucosyltransferase 1PRO_0000012273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1015 – 10151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1228 – 12281N-linked (GlcNAc...)Sequence Analysis
Modified residuei1277 – 12771PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9JLA3.
PRIDEiQ9JLA3.

Expressioni

Gene expression databases

GenevestigatoriQ9JLA3.

Interactioni

Subunit structurei

Monomer as well as in a tight complex with SEP15. Interacts with METTL23 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ9JLA3. 3 interactions.
MINTiMINT-4568455.
STRINGi10116.ENSRNOP00000020558.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1244 – 1551308GlucosyltransferaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1548 – 15514Prevents secretion from ERPROSITE-ProRule annotation

Domaini

N-terminal non-catalytic domain is assumed to mediate recognition of proteins with partial folding defects.

Sequence similaritiesi

Belongs to the glycosyltransferase 8 family.1 Publication

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG320899.
GeneTreeiENSGT00390000004600.
HOGENOMiHOG000184622.
HOVERGENiHBG079469.
InParanoidiQ9JLA3.
KOiK11718.
OMAiRDYLDLT.
OrthoDBiEOG75J0M7.
PhylomeDBiQ9JLA3.
TreeFamiTF300320.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view]
PANTHERiPTHR11226. PTHR11226. 1 hit.
PfamiPF06427. UDP-g_GGTase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9JLA3-1 [UniParc]FASTAAdd to Basket

« Hide

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

L
Length:1,551
Mass (Da):176,431
Last modified:March 3, 2009 - v2
Checksum:iFD4A1B6BCCBF7738
GO

Sequence cautioni

The sequence AAF67072.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121A → C in AAF67072. (PubMed:10764828)Curated
Sequence conflicti44 – 441S → R AA sequence (PubMed:10764828)Curated
Sequence conflicti324 – 3252QD → MV AA sequence (PubMed:10764828)Curated
Sequence conflicti969 – 9691F → H AA sequence (PubMed:10764828)Curated
Sequence conflicti1165 – 11651L → K AA sequence (PubMed:10764828)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF200359 mRNA. Translation: AAF67072.1. Different initiation.
RefSeqiNP_598280.1. NM_133596.1.
XP_006244796.1. XM_006244734.2.
UniGeneiRn.162227.

Genome annotation databases

EnsembliENSRNOT00000020558; ENSRNOP00000020558; ENSRNOG00000014901.
GeneIDi171129.
KEGGirno:171129.
UCSCiRGD:619710. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF200359 mRNA. Translation: AAF67072.1 . Different initiation.
RefSeqi NP_598280.1. NM_133596.1.
XP_006244796.1. XM_006244734.2.
UniGenei Rn.162227.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9JLA3. 3 interactions.
MINTi MINT-4568455.
STRINGi 10116.ENSRNOP00000020558.

Protein family/group databases

CAZyi GT24. Glycosyltransferase Family 24.

Proteomic databases

PaxDbi Q9JLA3.
PRIDEi Q9JLA3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000020558 ; ENSRNOP00000020558 ; ENSRNOG00000014901 .
GeneIDi 171129.
KEGGi rno:171129.
UCSCi RGD:619710. rat.

Organism-specific databases

CTDi 56886.
RGDi 619710. Uggt1.

Phylogenomic databases

eggNOGi NOG320899.
GeneTreei ENSGT00390000004600.
HOGENOMi HOG000184622.
HOVERGENi HBG079469.
InParanoidi Q9JLA3.
KOi K11718.
OMAi RDYLDLT.
OrthoDBi EOG75J0M7.
PhylomeDBi Q9JLA3.
TreeFami TF300320.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_196403. ER Quality Control Compartment (ERQC).

Miscellaneous databases

NextBioi 621894.
PROi Q9JLA3.

Gene expression databases

Genevestigatori Q9JLA3.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view ]
PANTHERi PTHR11226. PTHR11226. 1 hit.
Pfami PF06427. UDP-g_GGTase. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [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-DawleyImported.
    Tissue: LiverImported.
  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.

Entry informationi

Entry nameiUGGG1_RAT
AccessioniPrimary (citable) accession number: Q9JLA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 3, 2009
Last modified: November 26, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3