UXS1_DANRE
ID UXS1_DANRE Reviewed; 418 AA.
AC Q6GMI9; Q8JHG1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=UDP-glucuronic acid decarboxylase 1;
DE EC=4.1.1.35;
DE AltName: Full=UDP-glucuronate decarboxylase 1;
DE Short=UXS-1;
GN Name=uxs1; ORFNames=zgc:91980;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=12006978; DOI=10.1038/ng896;
RA Golling G., Amsterdam A., Sun Z., Antonelli M., Maldonado E., Chen W.,
RA Burgess S., Haldi M., Artzt K., Farrington S., Lin S.-Y., Nissen R.M.,
RA Hopkins N.;
RT "Insertional mutagenesis in zebrafish rapidly identifies genes essential
RT for early vertebrate development.";
RL Nat. Genet. 31:135-140(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16759393; DOI=10.1186/1471-213x-6-28;
RA Nissen R.M., Amsterdam A., Hopkins N.;
RT "A zebrafish screen for craniofacial mutants identifies wdr68 as a highly
RT conserved gene required for endothelin-1 expression.";
RL BMC Dev. Biol. 6:28-28(2006).
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 (By similarity).
CC Essential during embryogenesis for craniofacial development.
CC {ECO:0000250, ECO:0000269|PubMed:12006978,
CC ECO:0000269|PubMed:16759393}.
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 -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
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 -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutants show cartilage defects due to impaired
CC chondrogenesis and have a reduced jaw size.
CC {ECO:0000269|PubMed:16759393}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. UDP-glucuronic acid decarboxylase subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH74058.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF506235; AAM34679.1; -; mRNA.
DR EMBL; BC074058; AAH74058.1; ALT_INIT; mRNA.
DR RefSeq; NP_775349.2; NM_173242.2.
DR AlphaFoldDB; Q6GMI9; -.
DR SMR; Q6GMI9; -.
DR STRING; 7955.ENSDARP00000072986; -.
DR PaxDb; Q6GMI9; -.
DR Ensembl; ENSDART00000078525; ENSDARP00000072986; ENSDARG00000056102.
DR GeneID; 192315; -.
DR KEGG; dre:192315; -.
DR CTD; 80146; -.
DR ZFIN; ZDB-GENE-020419-37; uxs1.
DR eggNOG; KOG1429; Eukaryota.
DR GeneTree; ENSGT00940000157868; -.
DR HOGENOM; CLU_007383_4_3_1; -.
DR InParanoid; Q6GMI9; -.
DR OMA; PKVKYLN; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q6GMI9; -.
DR TreeFam; TF105736; -.
DR UniPathway; UPA00796; UER00771.
DR PRO; PR:Q6GMI9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000056102; Expressed in intestine and 52 other tissues.
DR ExpressionAtlas; Q6GMI9; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IMP:ZFIN.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IMP:ZFIN.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:ZFIN.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IMP:ZFIN.
DR GO; GO:0001503; P:ossification; IMP:ZFIN.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:ZFIN.
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 2: Evidence at transcript level;
KW Decarboxylase; Developmental protein; Glycoprotein; Golgi apparatus; Lyase;
KW Membrane; NAD; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..418
FT /note="UDP-glucuronic acid decarboxylase 1"
FT /id="PRO_0000183273"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..418
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 397..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 117..142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229..233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 271..275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 288..295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 355..359
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 333..334
FT /note="AQ -> GS (in Ref. 1; AAM34679)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="P -> S (in Ref. 1; AAM34679)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="P -> T (in Ref. 1; AAM34679)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="K -> R (in Ref. 1; AAM34679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 47676 MW; A07B28880A7D7EC0 CRC64;
MMRMSWMVTV INRRMMKILI ALALIAYIAS VWGTYANMRS IQEHGEMKIE QRIDEAVGPL
REKIRELELS FTQKYPPVKF LSEKDRKRIL ITGGAGFVGS HLTDKLMMDG HEVTVVDNFF
TGRKRNVEHW IGHENFELIN HDVVEPLYIE VDQIYHLASP ASPPNYMYNP IKTLKTNTIG
TLNMLGLAKR VGARLLLAST SEVYGDPEVH PQNEDYWGHV NPIGPRACYD EGKRVAETMC
YAYMKQEGVE VRVARIFNTF GSRMHMNDGR VVSNFILQAL QGEALTVYGS GSQTRAFQYV
SDLVNGLVSL MNSNISSPVN LGNPEEHTIL EFAQLIKSLV ASRSHIQFLP EAQDDPQRRR
PDIRKAKLLL GWEPVVPLEE GLNKTIQYFS RELEHQANNQ YIPKPKAARM KKGRPRHN
