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UD2A3_MOUSE
ID   UD2A3_MOUSE             Reviewed;         534 AA.
AC   Q8BWQ1; Q8R129; Q9D811;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=UDP-glucuronosyltransferase 2A3;
DE            Short=UDPGT 2A3;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=Ugt2a3;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Small intestine;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=17050650; DOI=10.1124/dmd.106.012070;
RA   Buckley D.B., Klaassen C.D.;
RT   "Tissue- and gender-specific mRNA expression of UDP-
RT   glucuronosyltransferases (UGTs) in mice.";
RL   Drug Metab. Dispos. 35:121-127(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
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).
RN   [5]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-135, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: UDP-glucuronosyltransferases catalyze phase II
CC       biotransformation reactions in which lipophilic substrates are
CC       conjugated with glucuronic acid to increase water solubility and
CC       enhance excretion. They are of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC         beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver, with lower levels in
CC       duodenum and jejunum. {ECO:0000269|PubMed:17050650}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AK008601; BAB25770.1; -; mRNA.
DR   EMBL; AK050327; BAC34191.1; -; mRNA.
DR   EMBL; BC025795; AAH25795.1; -; mRNA.
DR   CCDS; CCDS19387.1; -.
DR   RefSeq; NP_082370.2; NM_028094.3.
DR   AlphaFoldDB; Q8BWQ1; -.
DR   SMR; Q8BWQ1; -.
DR   BioGRID; 215148; 1.
DR   STRING; 10090.ENSMUSP00000031195; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyGen; Q8BWQ1; 2 sites.
DR   iPTMnet; Q8BWQ1; -.
DR   PhosphoSitePlus; Q8BWQ1; -.
DR   SwissPalm; Q8BWQ1; -.
DR   jPOST; Q8BWQ1; -.
DR   MaxQB; Q8BWQ1; -.
DR   PaxDb; Q8BWQ1; -.
DR   PeptideAtlas; Q8BWQ1; -.
DR   PRIDE; Q8BWQ1; -.
DR   ProteomicsDB; 297801; -.
DR   Antibodypedia; 24205; 130 antibodies from 19 providers.
DR   DNASU; 72094; -.
DR   Ensembl; ENSMUST00000031195; ENSMUSP00000031195; ENSMUSG00000035780.
DR   GeneID; 72094; -.
DR   KEGG; mmu:72094; -.
DR   UCSC; uc008xyh.2; mouse.
DR   CTD; 79799; -.
DR   MGI; MGI:1919344; Ugt2a3.
DR   VEuPathDB; HostDB:ENSMUSG00000035780; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000162432; -.
DR   HOGENOM; CLU_012949_0_2_1; -.
DR   InParanoid; Q8BWQ1; -.
DR   OMA; MVGVPIF; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; Q8BWQ1; -.
DR   TreeFam; TF315472; -.
DR   BioGRID-ORCS; 72094; 3 hits in 70 CRISPR screens.
DR   ChiTaRS; Ugt2a3; mouse.
DR   PRO; PR:Q8BWQ1; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8BWQ1; protein.
DR   Bgee; ENSMUSG00000035780; Expressed in left lobe of liver and 40 other tissues.
DR   Genevisible; Q8BWQ1; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; ISO:MGI.
DR   GO; GO:0052695; P:cellular glucuronidation; ISO:MGI.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..534
FT                   /note="UDP-glucuronosyltransferase 2A3"
FT                   /id="PRO_0000299147"
FT   TOPO_DOM        19..493
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        494..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        515..534
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         135
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        252
FT                   /note="K -> E (in Ref. 1; BAB25770)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="P -> S (in Ref. 2; AAH25795)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        346
FT                   /note="T -> I (in Ref. 1; BAB25770)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   534 AA;  61119 MW;  3BF4F591395B1620 CRC64;
     MVSEKCVAAF FLLQLCWAGC GFCSKVLVWP CDMSHWLNLK TILEELGARG HEVTVLKYPS
     IIIDQSKRIP LHFENIPLLY EIETAENRLN EIANLAVNVI PNLSLWEAAK TLQDFFLQVT
     GDFESICRSV LYNQKFMDKL RDAQYDVVVI DPVVPCGELV AEVLQIPFVY TLRFSMGYYM
     EKHCGQLPIP LSYVPVVMSE LTDNMTFTER VKNMMFSLLF EYWLQQYDFA FWDQFYSETL
     GRPTTFCKTV GKADIWLIRT YWDVEFPRPY LPNFEFVGGL HCKPAKPLPK EMEEFVQSSG
     EHGVVVFSLG SMVKNLTEEK ANLIASVLAQ IPQKVLWRYS GKKPATLGSN TRLFNWIPQN
     DLLGHPKTKA FITHGGTNGI YEAIYHGVPM VGVPMLGDQP HNIAHMEAKG AALKVSISTM
     TSTDLLSAVR AVINEPSYKE NAMRLSRIHH DQPVKPLDRA VFWIEFVMRH KGAKHLRVAA
     HDLSWFQYHS LDVIGFLLLC VVTLTFIITK FCLFVCQKLY MKESKKMGNR KKKN
 
 
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