LOCUS       NP_647552                420 aa            linear   ROD 24-JUN-2024
DEFINITION  UDP-glucuronic acid decarboxylase 1 [Rattus norvegicus].
ACCESSION   NP_647552
VERSION     NP_647552.2
DBSOURCE    REFSEQ: accession NM_139336.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Polizzi,S.J., Walsh,R.M. Jr., Le Magueres,P., Criswell,A.R. and
            Wood,Z.A.
  TITLE     Human UDP-alpha-d-xylose synthase forms a catalytically important
            tetramer that has not been observed in crystal structures
  JOURNAL   Biochemistry 52 (22), 3888-3898 (2013)
   PUBMED   23656592
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Polizzi,S.J., Walsh,R.M. Jr., Peeples,W.B., Lim,J.M., Wells,L. and
            Wood,Z.A.
  TITLE     Human UDP-alpha-D-xylose synthase and Escherichia coli ArnA
            conserve a conformational shunt that controls whether xylose or
            4-keto-xylose is produced
  JOURNAL   Biochemistry 51 (44), 8844-8855 (2012)
   PUBMED   23072385
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Moriarity,J.L., Hurt,K.J., Resnick,A.C., Storm,P.B., Laroy,W.,
            Schnaar,R.L. and Snyder,S.H.
  TITLE     UDP-glucuronate decarboxylase, a key enzyme in proteoglycan
            synthesis: cloning, characterization, and localization
  JOURNAL   J Biol Chem 277 (19), 16968-16975 (2002)
   PUBMED   11877387
  REMARK    GeneRIF: UDP-glucuronate decarboxylase, a key enzyme in
            proteoglycan synthesis: cloning, characterization, and
            localization.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Nov 27, 2020 this sequence version replaced NP_647552.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF482705.1, BC086988.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..420
                     /product="UDP-glucuronic acid decarboxylase 1"
                     /EC_number="4.1.1.35"
                     /note="UXS-1"
                     /calculated_mol_wt=47408
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q8NBZ7; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX0.1)"
     Region          4..78
                     /region_name="UXS1_N"
                     /note="UDP-glucuronate decarboxylase N-terminal;
                     pfam11803"
                     /db_xref="CDD:463356"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQX0.1)"
     Region          89..392
                     /region_name="UGD_SDR_e"
                     /note="UDP-glucuronate decarboxylase (UGD) and related
                     proteins, extended (e) SDRs; cd05230"
                     /db_xref="CDD:187541"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8NBZ7; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX0.1)"
     Site            order(95,97..100,119..124,143..145,159..163,178,200..202,
                     231,235,258..261,272)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187541"
     Site            order(148..149,184..185,188..189,191..192,245)
                     /site_type="other"
                     /note="putative substrate binding site 2 [chemical
                     binding]"
                     /db_xref="CDD:187541"
     Site            order(165,228,260,271..273,276..277,288..290,295,297,331,
                     357,361)
                     /site_type="other"
                     /note="putative substrate binding site 1 [chemical
                     binding]"
                     /db_xref="CDD:187541"
     Site            order(179,202,231,235)
                     /site_type="active"
                     /db_xref="CDD:187541"
     Site            316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX0.1)"
     CDS             1..420
                     /gene="Uxs1"
                     /gene_synonym="UGD"
                     /coded_by="NM_139336.2:46..1308"
                     /db_xref="GeneID:246232"
                     /db_xref="RGD:628680"
ORIGIN      
        1 mvskgllrlv ssvnrrkmkl llgialfaya asvwgnfvnm rsiqengelk ieskieeiie
       61 plrekirdle ksftqkyppv kflsekdrkr ilitggagfv gshltdklmm dghevtvvdn
      121 fftgrkrnve hwighenfel inhdvveply ievdqiyhla spasppnymy npiktlktnt
      181 igtlnmlgla krvgarllla stsevygdpe vhpqsedywg hvnpigprac ydegkrvaet
      241 mcyaymkqeg vevrvarifn tfgprmhmnd grvvsnfilq alqgepltvy gsgsqtrafq
      301 yvsdlvnglv almnsnvssp vnlgnpeeht ilefaqlikn lvgsgseiqf lseaqddpqk
      361 rkpdikkakl mlgwepvvpl eeglnkaihy frkeleyqan nqyipkpkpa rvkkgrtrhs
//
