UXS1_RAT
ID UXS1_RAT Reviewed; 420 AA.
AC Q5PQX0; Q8K464;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=UDP-glucuronic acid decarboxylase 1;
DE EC=4.1.1.35 {ECO:0000269|PubMed:11877387};
DE AltName: Full=UDP-glucuronate decarboxylase 1;
DE Short=UGD;
DE Short=UXS-1;
GN Name=Uxs1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH AKT1, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11877387; DOI=10.1074/jbc.m109316200;
RA Moriarity J.L., Hurt K.J., Resnick A.C., Storm P.B., Laroy W.,
RA Schnaar R.L., Snyder S.H.;
RT "UDP-glucuronate decarboxylase, a key enzyme in proteoglycan synthesis.
RT Cloning, characterization, and localization.";
RL J. Biol. Chem. 277:16968-16975(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic
CC acid to UDP-xylose. Necessary for the biosynthesis of the core
CC tetrasaccharide in glycosaminoglycan biosynthesis.
CC {ECO:0000269|PubMed:11877387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + UDP-alpha-D-glucuronate = CO2 + UDP-alpha-D-xylose;
CC Xref=Rhea:RHEA:23916, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57632, ChEBI:CHEBI:58052; EC=4.1.1.35;
CC Evidence={ECO:0000269|PubMed:11877387};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23917;
CC Evidence={ECO:0000305|PubMed:11877387};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose
CC biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step
CC 1/1.
CC -!- SUBUNIT: Interacts with AKT1. {ECO:0000269|PubMed:11877387}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:11877387}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:11877387}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, spleen, lung,
CC testis, liver, skeletal muscle and kidney.
CC {ECO:0000269|PubMed:11877387}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. UDP-glucuronic acid decarboxylase subfamily. {ECO:0000305}.
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DR EMBL; AF482705; AAM45939.1; -; mRNA.
DR EMBL; BC086988; AAH86988.1; -; mRNA.
DR RefSeq; NP_647552.1; NM_139336.1.
DR AlphaFoldDB; Q5PQX0; -.
DR SMR; Q5PQX0; -.
DR BioGRID; 251537; 1.
DR STRING; 10116.ENSRNOP00000066044; -.
DR GlyGen; Q5PQX0; 1 site.
DR PaxDb; Q5PQX0; -.
DR GeneID; 246232; -.
DR KEGG; rno:246232; -.
DR CTD; 80146; -.
DR RGD; 628680; Uxs1.
DR VEuPathDB; HostDB:ENSRNOG00000045605; -.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_4_3_1; -.
DR InParanoid; Q5PQX0; -.
DR OMA; PKVKYLN; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q5PQX0; -.
DR BRENDA; 4.1.1.35; 5301.
DR UniPathway; UPA00796; UER00771.
DR PRO; PR:Q5PQX0; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000045605; Expressed in ovary and 20 other tissues.
DR Genevisible; Q5PQX0; RN.
DR GO; GO:1902494; C:catalytic complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0070403; F:NAD+ binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IDA:RGD.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:InterPro.
DR GO; GO:0033320; P:UDP-D-xylose biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR044516; UXS.
DR InterPro; IPR021761; UXS1_N.
DR PANTHER; PTHR43078; PTHR43078; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR Pfam; PF11803; UXS1_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; Decarboxylase; Glycoprotein; Golgi apparatus; Lyase; Membrane;
KW NAD; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..420
FT /note="UDP-glucuronic acid decarboxylase 1"
FT /id="PRO_0000183272"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..420
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 119..144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 273..277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 290..297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 357..361
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 55
FT /note="I -> T (in Ref. 1; AAM45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..116
FT /note="EVT -> DVS (in Ref. 1; AAM45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="Q -> E (in Ref. 1; AAM45939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 47539 MW; 1F0CF93BAF78C65B CRC64;
MVSKGLLRLV SSVNRRKMKL LLGIALFAYA ASVWGNFVNM RSIQENGELK IESKIEEIIE
PLREKIRDLE KSFTQKYPPV KFLSEKDRKR ILITGGAGFV GSHLTDKLMM DGHEVTVVDN
FFTGRKRNVE HWIGHENFEL INHDVVEPLY IEVDQIYHLA SPASPPNYMY NPIKTLKTNT
IGTLNMLGLA KRVGARLLLA STSEVYGDPE VHPQSEDYWG HVNPIGPRAC YDEGKRVAET
MCYAYMKQEG VEVRVARIFN TFGPRMHMND GRVVSNFILQ ALQGEPLTVY GSGSQTRAFQ
YVSDLVNGLV ALMNSNVSSP VNLGNPEEHT ILEFAQLIKN LVGSGSEIQF LSEAQDDPQK
RKPDIKKAKL MLGWEPVVPL EEGLNKAIHY FRKELEYQAN NQYIPKPKPA RVKKGRTRHS
