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Q9JLA3

- UGGG1_RAT

UniProt

Q9JLA3 - UGGG1_RAT

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
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (03 Mar 2009)
      Previous versions | rss
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    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)2 Publications

    pH dependencei

    Optimum pH is 7.6-8.0.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. UDP-glucose:glycoprotein glucosyltransferase activity Source: UniProtKB
    3. 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

    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

    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

    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.

    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:
    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...
    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

    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: October 1, 2014
    This is version 94 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