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Protein

UDP-glucuronic acid decarboxylase 1

Gene

Uxs1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis (By similarity).By similarity

Catalytic activityi

UDP-D-glucuronate = UDP-D-xylose + CO2.

Cofactori

NAD+By similarity

Pathwayi: UDP-alpha-D-xylose biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-alpha-D-xylose from UDP-alpha-D-glucuronate.
Proteins known to be involved in this subpathway in this organism are:
  1. UDP-glucuronic acid decarboxylase 1 (Uxs1)
This subpathway is part of the pathway UDP-alpha-D-xylose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-alpha-D-xylose from UDP-alpha-D-glucuronate, the pathway UDP-alpha-D-xylose biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei228 – 2281SubstrateBy similarity
Active sitei231 – 2311Proton acceptorBy similarity
Binding sitei260 – 2601SubstrateBy similarity
Binding sitei272 – 2721NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi119 – 14426NADBy similarityAdd
BLAST
Nucleotide bindingi231 – 2355NADBy similarity
Nucleotide bindingi273 – 2775SubstrateBy similarity
Nucleotide bindingi290 – 2978SubstrateBy similarity
Nucleotide bindingi357 – 3615SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00796; UER00771.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucuronic acid decarboxylase 1 (EC:4.1.1.35)
Alternative name(s):
UDP-glucuronate decarboxylase 1
Short name:
UGD
Short name:
UXS-1
Gene namesi
Name:Uxs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1915133. Uxs1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence analysisAdd
BLAST
Transmembranei20 – 4021Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini41 – 420380LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420UDP-glucuronic acid decarboxylase 1PRO_0000183270Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941PhosphothreonineBy similarity
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ91XL3.
MaxQBiQ91XL3.
PaxDbiQ91XL3.
PRIDEiQ91XL3.

PTM databases

iPTMnetiQ91XL3.
PhosphoSiteiQ91XL3.

Expressioni

Gene expression databases

BgeeiQ91XL3.
CleanExiMM_UXS1.
ExpressionAtlasiQ91XL3. baseline and differential.
GenevisibleiQ91XL3. MM.

Interactioni

Subunit structurei

Interacts with AKT1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000119939.

Structurei

3D structure databases

ProteinModelPortaliQ91XL3.
SMRiQ91XL3. Positions 88-399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1429. Eukaryota.
COG0451. LUCA.
GeneTreeiENSGT00530000063128.
HOVERGENiHBG094144.
InParanoidiQ91XL3.
KOiK08678.
OMAiTISYFRN.
OrthoDBiEOG73FQMK.
PhylomeDBiQ91XL3.
TreeFamiTF105736.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR021761. UXS1_N.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
PF11803. UXS1_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91XL3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSKGLLRLV SSVNRRRMKL LLGIALFAYA ASVWGNFVNM RSIQENGELK
60 70 80 90 100
IESKIEEIVE PLREKIRDLE KSFTQKYPPV KFLSEKDRKR ILITGGAGFV
110 120 130 140 150
GSHLTDKLMM DGHEVTVVDN FFTGRKRNVE HWIGHENFEL INHDVVEPLY
160 170 180 190 200
IEVDQIYHLA SPASPPNYMY NPIKTLKTNT IGTLNMLGLA KRVGARLLLA
210 220 230 240 250
STSEVYGDPE VHPQSEDYWG HVNPIGPRAC YDEGKRVAET MCYAYMKQEG
260 270 280 290 300
VEVRVARIFN TFGPRMHMND GRVVSNFILQ ALQGEPLTVY GSGSQTRAFQ
310 320 330 340 350
YVSDLVNGLV ALMNSNVSSP VNLGNPEEHT ILEFAQLIKN LVGSGSEIQF
360 370 380 390 400
LSEAQDDPQK RKPDIKKAKL MLGWEPVVPL EEGLNKAIHY FRKELEYQAN
410 420
NQYIPKPKPA RVKKGRTRHS
Length:420
Mass (Da):47,553
Last modified:December 1, 2001 - v1
Checksum:iDB188E2780309AE4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571R → G in BAE31165 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF399958 mRNA. Translation: AAK85410.1.
AK075806 mRNA. Translation: BAC35974.1.
AK152376 mRNA. Translation: BAE31165.1.
BC037049 mRNA. Translation: AAH37049.1.
CCDSiCCDS35551.1.
RefSeqiNP_080706.1. NM_026430.3.
UniGeneiMm.387202.

Genome annotation databases

EnsembliENSMUST00000126008; ENSMUSP00000119939; ENSMUSG00000057363.
GeneIDi67883.
KEGGimmu:67883.
UCSCiuc007avq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF399958 mRNA. Translation: AAK85410.1.
AK075806 mRNA. Translation: BAC35974.1.
AK152376 mRNA. Translation: BAE31165.1.
BC037049 mRNA. Translation: AAH37049.1.
CCDSiCCDS35551.1.
RefSeqiNP_080706.1. NM_026430.3.
UniGeneiMm.387202.

3D structure databases

ProteinModelPortaliQ91XL3.
SMRiQ91XL3. Positions 88-399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000119939.

PTM databases

iPTMnetiQ91XL3.
PhosphoSiteiQ91XL3.

Proteomic databases

EPDiQ91XL3.
MaxQBiQ91XL3.
PaxDbiQ91XL3.
PRIDEiQ91XL3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000126008; ENSMUSP00000119939; ENSMUSG00000057363.
GeneIDi67883.
KEGGimmu:67883.
UCSCiuc007avq.1. mouse.

Organism-specific databases

CTDi80146.
MGIiMGI:1915133. Uxs1.

Phylogenomic databases

eggNOGiKOG1429. Eukaryota.
COG0451. LUCA.
GeneTreeiENSGT00530000063128.
HOVERGENiHBG094144.
InParanoidiQ91XL3.
KOiK08678.
OMAiTISYFRN.
OrthoDBiEOG73FQMK.
PhylomeDBiQ91XL3.
TreeFamiTF105736.

Enzyme and pathway databases

UniPathwayiUPA00796; UER00771.

Miscellaneous databases

PROiQ91XL3.
SOURCEiSearch...

Gene expression databases

BgeeiQ91XL3.
CleanExiMM_UXS1.
ExpressionAtlasiQ91XL3. baseline and differential.
GenevisibleiQ91XL3. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR021761. UXS1_N.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
PF11803. UXS1_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "UDP-glucuronic acid decarboxylase, the first committed step in glycosaminoglycan synthesis."
    Olson S.K., Esko J.D.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: LAF1.
    Tissue: Mastocytoma.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow macrophage and Pancreas.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiUXS1_MOUSE
AccessioniPrimary (citable) accession number: Q91XL3
Secondary accession number(s): Q3U854
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.