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Q9JLA3

- UGGG1_RAT

UniProt

Q9JLA3 - UGGG1_RAT

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Protein
UDP-glucose:glycoprotein glucosyltransferase 1
Gene
Uggt1, Gt, Ugcgl1, Uggt, Ugt1, Ugtr
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

Calcium.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)1 Publication

pH dependencei

Optimum pH is 7.6-8.0.1 Publication

Pathwayi

GO - Molecular functioni

  1. UDP-glucose:glycoprotein glucosyltransferase activity Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. unfolded protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: UniProtKB
  2. UDP-glucosylation Source: GOC
  3. protein folding Source: RGD
  4. protein glycosylation Source: UniProtKB-UniPathway
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, Uggt, Ugt1, Ugtr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi619710. Uggt1.

Subcellular locationi

Endoplasmic reticulum lumen. Endoplasmic reticulum-Golgi intermediate compartment 2 Publications

GO - Cellular componenti

  1. endoplasmic reticulum Source: RGD
  2. endoplasmic reticulum lumen Source: UniProtKB
  3. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
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 Publication
Add
BLAST
Chaini43 – 15511509UDP-glucose:glycoprotein glucosyltransferase 1
PRO_0000012273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi269 – 2691N-linked (GlcNAc...) Reviewed prediction
Glycosylationi536 – 5361N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1015 – 10151N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1228 – 12281N-linked (GlcNAc...) Reviewed prediction
Modified residuei1277 – 12771Phosphoserine By 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.1 Publication

Protein-protein interaction databases

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

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1548 – 15514Prevents secretion from ER Reviewed prediction

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

MCSRGDANAA GAAAARRVTG LCYNMGLLIA LALLCLFSLA EANSKAITTS     50
LTTKWFSAPL LLEASEFLAE DSQEKFWSFV EASQNIGSSD QHDTDRSYYD 100
AILEAAFRFL SPLQQNLLKF CLSLRSYSAS IQAFQQIAVD EPPPEGCKSF 150
LSVHGKQTCD LGTLESLLLT APDRPKPLLF KGDHRYPSSN PESPVVIFYS 200
EIGHEEFSNI HHQLISKSNE GKINYVFRHY ISNPRKEPVH LSGYGVELAI 250
KSTEYKAKDD TQVKGTEVNT TVIGENDPID EVQGFLFGKL RELYPSLEGQ 300
LKEFRKHLVE STNEMAPLKV WQLQDLSFQT AARILAAPVE LALVVMKDIS 350
QNFPTKARAI TKTAVSAQLR AEVEENQKYF KGTIGLQPGD SALFINGLHI 400
DLDTQDIFSL FDTLRNEARV MEGLHRLGIE GLSLHNILKL NIQPSETDYA 450
VDIRSPAISW VNNLEVDSRY NSWPSSLQEL LRPTFPGVIR QIRKNLHNMV 500
FIVDPVHETT AELVSIAEMF LSNHIPLRIG FIFVVNDSED VDGMQDAGVA 550
VLRAYNYVGQ EVDGYHAFQT LTQIYNKVRT GEKVKVEHVV SVLEKKYPYV 600
EVNSILGIDS AYDQNRKEAR GYYEQTGVGP LPVVLFNGMP FEKEQLDPDE 650
LETITMHKIL ETTTFFQRAV YLGELSHDQD VVEYIMNQPN VVPRINSRIL 700
TAKREYLDLT ASNNFYVDDF ARFSALDSRG KTAAIANSMN YLTKKGMSSK 750
EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD AIKHQKTSNN VRISMINNPS 800
REISDSSTPV SRAIWAALQT QTSNSAKNFI TKMVKEETAE ALAAGVDIGE 850
FSVGGMDVSL FKEVFESSRM DFILSHALYC RDVLKLKKGQ RVVISNGRII 900
GPLEDSELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV 950
DALLSAQPKG EARIEYQFFE DKHSAIKLKP KEGETYYDVV AVVDPVTREA 1000
QRLAPLLLVL AQLINMSLRV FMNCQSKLSD MPLKSFYRYV LEPEISFTAD 1050
NSFAKGPIAK FLDMPQSPLF TLNLNTPESW MVESVRTPYD LDNIYLEEVD 1100
SIVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP TTVDTIVMAN 1150
LGYFQLKANP GAWILRLRKG RSDDIYRIYS HDGTDSPPDA NDVVVILNNF 1200
KSKIIKVKVQ KKADMANEDL LSDGTNENES GFWDSFKWGF SGQKTEEVKQ 1250
DKDDIINIFS VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK 1300
EFIPYMAKKY NFQYELVQYK WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV 1350
VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY GYTPFCDSRR EMDGYRFWKS 1400
GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG LSQDPNSLSN 1450
LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE 1500
PKLEAAVRIV PEWQDYDQEI KQLQTLFQEE KELGTLHEEE TQEGSQKHEE 1550
L 1551
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121A → C in AAF67072. 1 Publication
Sequence conflicti44 – 441S → R AA sequence 1 Publication
Sequence conflicti324 – 3252QD → MV AA sequence 1 Publication
Sequence conflicti969 – 9691F → H AA sequence 1 Publication
Sequence conflicti1165 – 11651L → K AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF200359 mRNA. Translation: AAF67072.1. Different initiation.
RefSeqiNP_598280.1. NM_133596.1.
XP_006244796.1. XM_006244734.1.
UniGeneiRn.162227.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF200359 mRNA. Translation: AAF67072.1 . Different initiation.
RefSeqi NP_598280.1. NM_133596.1.
XP_006244796.1. XM_006244734.1.
UniGenei Rn.162227.

3D structure databases

ModBasei 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-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.

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: September 3, 2014
This is version 93 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

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