UXS1_MOUSE
ID UXS1_MOUSE Reviewed; 420 AA.
AC Q91XL3; Q3U854;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=LAF1; TISSUE=Mastocytoma;
RA Olson S.K., Esko J.D.;
RT "UDP-glucuronic acid decarboxylase, the first committed step in
RT glycosaminoglycan synthesis.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AF399958; AAK85410.1; -; mRNA.
DR EMBL; AK075806; BAC35974.1; -; mRNA.
DR EMBL; AK152376; BAE31165.1; -; mRNA.
DR EMBL; BC037049; AAH37049.1; -; mRNA.
DR CCDS; CCDS35551.1; -.
DR RefSeq; NP_080706.1; NM_026430.3.
DR AlphaFoldDB; Q91XL3; -.
DR SMR; Q91XL3; -.
DR BioGRID; 212507; 3.
DR STRING; 10090.ENSMUSP00000119939; -.
DR GlyGen; Q91XL3; 1 site.
DR iPTMnet; Q91XL3; -.
DR PhosphoSitePlus; Q91XL3; -.
DR EPD; Q91XL3; -.
DR MaxQB; Q91XL3; -.
DR PaxDb; Q91XL3; -.
DR PeptideAtlas; Q91XL3; -.
DR PRIDE; Q91XL3; -.
DR ProteomicsDB; 300206; -.
DR Antibodypedia; 1921; 125 antibodies from 19 providers.
DR DNASU; 67883; -.
DR Ensembl; ENSMUST00000126008; ENSMUSP00000119939; ENSMUSG00000057363.
DR GeneID; 67883; -.
DR KEGG; mmu:67883; -.
DR UCSC; uc007avq.1; mouse.
DR CTD; 80146; -.
DR MGI; MGI:1915133; Uxs1.
DR VEuPathDB; HostDB:ENSMUSG00000057363; -.
DR eggNOG; KOG1429; Eukaryota.
DR GeneTree; ENSGT00940000157868; -.
DR HOGENOM; CLU_007383_4_3_1; -.
DR InParanoid; Q91XL3; -.
DR OMA; PKVKYLN; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q91XL3; -.
DR TreeFam; TF105736; -.
DR UniPathway; UPA00796; UER00771.
DR BioGRID-ORCS; 67883; 12 hits in 71 CRISPR screens.
DR ChiTaRS; Uxs1; mouse.
DR PRO; PR:Q91XL3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91XL3; protein.
DR Bgee; ENSMUSG00000057363; Expressed in indifferent gonad and 250 other tissues.
DR ExpressionAtlas; Q91XL3; baseline and differential.
DR Genevisible; Q91XL3; MM.
DR GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070403; F:NAD+ binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; ISO:MGI.
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_0000183270"
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 257
FT /note="R -> G (in Ref. 2; BAE31165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 47553 MW; DB188E2780309AE4 CRC64;
MVSKGLLRLV SSVNRRRMKL LLGIALFAYA ASVWGNFVNM RSIQENGELK IESKIEEIVE
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
