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UXS1_PONAB
ID   UXS1_PONAB              Reviewed;         420 AA.
AC   Q5R885;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=UDP-glucuronic acid decarboxylase 1;
DE            EC=4.1.1.35;
DE   AltName: Full=UDP-glucuronate decarboxylase 1;
DE            Short=UGD;
DE            Short=UXS-1;
GN   Name=UXS1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000250}.
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   -!- SUBUNIT: Interacts with AKT1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
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; CR859869; CAH92025.1; -; mRNA.
DR   RefSeq; NP_001126176.1; NM_001132704.1.
DR   RefSeq; XP_009235107.1; XM_009236832.1.
DR   AlphaFoldDB; Q5R885; -.
DR   SMR; Q5R885; -.
DR   STRING; 9601.ENSPPYP00000013525; -.
DR   GeneID; 100173139; -.
DR   KEGG; pon:100173139; -.
DR   CTD; 80146; -.
DR   eggNOG; KOG1429; Eukaryota.
DR   HOGENOM; CLU_007383_4_3_1; -.
DR   InParanoid; Q5R885; -.
DR   OrthoDB; 848823at2759; -.
DR   UniPathway; UPA00796; UER00771.
DR   Proteomes; UP000001595; Unplaced.
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; IEA:InterPro.
DR   GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript 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_0000183271"
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"
SQ   SEQUENCE   420 AA;  47604 MW;  EC8DC0E1B1D02157 CRC64;
     MVSKALLRLV SAVNRRRMKL LLGIALLAYV ASVWGNFVNM RSIQENGELK IESKIEEMVE
     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 RIKKGRTRHN
 
 
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