P70691 (UD12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-glucuronosyltransferase 1-2
Short name=UDPGT 1-2
Short name=UGT1*2
Short name=UGT1-02
Short name=UGT1.2
EC=2.4.1.17

Alternative name(s):
Bilirubin-specific UDPGT
UDP-glucuronosyltransferase 1A2
Short name=UGT1A2

Gene names

Name:	Ugt1a2
Synonyms:	Ugt1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.
Catalytic activity	UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside.
Subcellular location	Microsome By similarity. Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.
Tissue specificity	Expressed in kidney. Ref.2
Sequence similarities	Belongs to the UDP-glycosyltransferase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	glucuronosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. The different isozymes have a different N-terminal domain and a common C-terminal domain of 245 residues.

Isoform 1 (identifier: P70691-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 533	506	UDP-glucuronosyltransferase 1-2		PRO_0000036012
Regions
	Transmembrane	491 – 511	21	Helical; Potential
Amino acid modifications
	Modified residue	282	1	Phosphothreonine Ref.6
	Glycosylation	141	1	N-linked (GlcNAc...) Potential
	Glycosylation	295	1	N-linked (GlcNAc...) Potential
	Glycosylation	433	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	143	1	S → G in AAP48594. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: FB458439525550FA	FASTA	533	60,285
	10 20 30 40 50 60 MDTGLCVPLR GISGLLLLLC ALPWAEGAKV LVLPMEGSQW LSMRDVVREL HARGHQTVVL 70 80 90 100 110 120 ASEVTVHIKG EDFFTLKTYA FPYTKEEYQQ EILSDIEKTF KTQHFVKAFF ETTASIRNFF 130 140 150 160 170 180 DLYSNSCIAL LHNKMLIQQL NSSFFDVILT DPIFPCGAVL AKYLQIPAVF ILRSLSCGIE 190 200 210 220 230 240 YEATQCPNPS SYIPNLLTRL SDHMDFLQRV QNMLYYLVLK YICRLSITPY ESLASELLQR 250 260 270 280 290 300 EVSLVEVLSH ASVWLFRGDF VLDYPRPIMP NMVFIGGINC VTKKPLSQEF EAYVNASGEH 310 320 330 340 350 360 GIVVFSLGSM VSEIPEKKAM EIAEALGRIP QTVLWRYTGT RPSNLAKNTI LVKWLPQNDL 370 380 390 400 410 420 LGHPKTRAFI THSGSHGIYE GICNGVPMVM MPLFGDQMDN AKRMETRGAG VTLNVLEMTA 430 440 450 460 470 480 DDLENALKTV INNKSYKENI MRLSSLHKDR PIEPLDLAVF WVEYVMRHKG APHLRPAAHD 490 500 510 520 530 LTWYQYHSLD VIGFLLAIVL TVVFIVFKCC AYGCRKCFGG KGRVKKSHKS KTH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of cDNAs for mouse phenol and bilirubin UDP-glucuronosyltransferases and mapping of the mouse gene for phenol UDP-glucuronosyltransferase (Ugtla1) to chromosome 1 by restriction fragment length variations." Koiwai O., Hasada K., Yasui Y., Sakai Y., Sato H., Watanabe T. Biochem. Genet. 33:111-122(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[2]	"Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation." Zhang T., Haws P., Wu Q. Genome Res. 14:79-89(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Liver.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-282, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D87866 mRNA. Translation: BAA13482.1. AY227195 mRNA. Translation: AAP48594.1. AK002629 mRNA. Translation: BAB22243.1. CH466520 Genomic DNA. Translation: EDL40122.1. BC138676 mRNA. Translation: AAI38677.1. BC145969 mRNA. Translation: AAI45970.1.
IPI	IPI00111936.
RefSeq	NP_038729.1. NM_013701.3.
UniGene	Mm.300095.
3D structure databases
ProteinModelPortal	P70691.
SMR	P70691. Positions 284-444.
ModBase	Search...
Protein family/group databases
CAZy	GT1. Glycosyltransferase Family 1.
PTM databases
PhosphoSite	P70691.
Proteomic databases
PRIDE	P70691.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000049289; ENSMUSP00000037258; ENSMUSG00000090171.
GeneID	22236.
KEGG	mmu:22236.
Organism-specific databases
CTD	22236.
MGI	MGI:3576049. Ugt1a2.
Phylogenomic databases
GeneTree	ENSGT00640000091365.
HOGENOM	HOG000220832.
HOVERGEN	HBG004033.
KO	K00699.
OMA	FMERIET.
Gene expression databases
ArrayExpress	P70691.
Bgee	P70691.
Genevestigator	P70691.
GermOnline	ENSMUSG00000054545. Mus musculus.
Family and domain databases
InterPro	IPR002213. UDP_glucos_trans. [Graphical view]
PANTHER	PTHR11926. PTHR11926. 1 hit.
Pfam	PF00201. UDPGT. 1 hit. [Graphical view]
PROSITE	PS00375. UDPGT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	302289.
SOURCE	Search...

Entry information

Entry name

UD12_MOUSE

Accession

Primary (citable) accession number: P70691
Secondary accession number(s): Q545X2, Q6XL49

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program