Reviewed, UniProtKB/Swiss-Prot Q9JLZ3 (AUHM_MOUSE)

Names and origin

Protein names

Recommended name:
    Methylglutaconyl-CoA hydratase, mitochondrial
    EC=4.2.1.18
Alternative name(s):
    AU-specific RNA-binding enoyl-CoA hydratase
      Short name=AU-binding enoyl-CoA hydratase
      Short name=muAUH

Gene names

Name:

Auh

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA. Has very low enoyl-CoA hydratase activity. Was originally identified as RNA-binding protein that binds in vitro to clustered 5'-AUUUA-3' motifs By similarity. Ref.1
Catalytic activity	(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H2O.
Pathway	Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 3/3.
Subunit structure	Homohexamer By similarity.
Subcellular location	Mitochondrion Ref.1.
Tissue specificity	Detected in heart, brain, liver, spleen, skeletal muscle and kidney. Ref.1
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
Biological process	Branched-chain amino acid catabolism
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	RNA-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological process	branched chain family amino acid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Ref.1 Traceable author statement. Source: MGI
Cellular component	mitochondrion Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	enoyl-CoA hydratase activity Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB mRNA 3'-UTR binding Inferred from sequence or structural similarity. Source: UniProtKB methylglutaconyl-CoA hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9JLZ3-1)

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.

Isoform 2 (identifier: Q9JLZ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     115-157: GADLKERAKM...VPTIAAIDGL → VSFQLKADIQ...PDSRCSPQIW
     159-314: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9JLZ3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     144-144: A → V
     145-314: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 42	42	Mitochondrion By similarity
	Chain	43 – 314	272	Methylglutaconyl-CoA hydratase, mitochondrial		PRO_0000007416
Regions
	Region	80 – 94	15	RNA-binding By similarity
Natural variations
	Alternative sequence	115 – 157	43	GADLK…AIDGL → VSFQLKADIQLCFQFAPFWW PLQSHSSQKPEVTPDSRCSP QIW in isoform 2.		VSP_008337
	Alternative sequence	144	1	A → V in isoform 3.		VSP_008338
	Alternative sequence	145 – 314	170	Missing in isoform 3.		VSP_008339
	Alternative sequence	159 – 314	156	Missing in isoform 2.		VSP_008340
Experimental info
	Sequence conflict	15 – 16	2	GR → VG in BAB23078. Ref.2
	Sequence conflict	15 – 16	2	GR → VG in BAB31947. Ref.2
	Sequence conflict	15 – 16	2	GR → VG in AAH49597. Ref.3
	Sequence conflict	22	1	A → P in BAB23078. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 974694EAC28FA157	FASTA	314	33,395
	10 20 30 40 50 60 MAAAAPGALG ALRTGRVRLV AACCARLGPA AWARGTAPRR GYSSEVKTED ELRVRHLEEE 70 80 90 100 110 120 NRGIVVLGIN RAYGKNALSK NLLKMLSKAV DALKSDKKVR TIIIRSEVPG IFCAGADLKE 130 140 150 160 170 180 RAKMHSSEVG PFVSKIRSVI NDIANLPVPT IAAIDGLALG GGLELALACD IRVAASSAKM 190 200 210 220 230 240 GLVETKLAII PGGGGTQRLP RAIGMSLAKE LIFSARVLDG QEAKAVGLIS HVLEQNQEGD 250 260 270 280 290 300 AAYRKALDLA REFLPQGPVA MRVAKLAINQ GMEVDLVTGL AIEEACYAQT ISTKDRLEGL 310 LAFKEKRPPR YKGE
	Isoform 2. Checksum: 0C3F5C54554FA5F6	FASTA	158	17,360
	10 20 30 40 50 60 MAAAAPGALG ALRTGRVRLV AACCARLGPA AWARGTAPRR GYSSEVKTED ELRVRHLEEE 70 80 90 100 110 120 NRGIVVLGIN RAYGKNALSK NLLKMLSKAV DALKSDKKVR TIIIRSEVPG IFCAVSFQLK 130 140 150 ADIQLCFQFA PFWWPLQSHS SQKPEVTPDS RCSPQIWA
	Isoform 3. Checksum: 85F50AD406A6A012	FASTA	144	15,508
	10 20 30 40 50 60 MAAAAPGALG ALRTGRVRLV AACCARLGPA AWARGTAPRR GYSSEVKTED ELRVRHLEEE 70 80 90 100 110 120 NRGIVVLGIN RAYGKNALSK NLLKMLSKAV DALKSDKKVR TIIIRSEVPG IFCAGADLKE 130 140 RAKMHSSEVG PFVSKIRSVI NDIV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterisation and mitochondrial localisation of AUH, an AU-specific RNA-binding enoyl-CoA hydratase." Brennan L.E., Nakagawa J., Egger D., Bienz K., Moroni C. Gene 228:85-91(1999) [PubMed: 10072761] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: BALB/c. Tissue: Brain.
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Strain: C57BL/6J. Tissue: Embryo.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain and Salivary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF118386 mRNA. Translation: AAF28835.1. AK003929 mRNA. Translation: BAB23078.1. AK019978 mRNA. Translation: BAB31947.1. BC026525 mRNA. Translation: AAH26525.1. BC049597 mRNA. Translation: AAH49597.1.
IPI	IPI00124900. IPI00357510. IPI00357511.
RefSeq	NP_057918.2.
UniGene	Mm.252034
3D structure databases
SMR	Q9JLZ3. Positions 49-314.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JLZ3.
PTM databases
PhosphoSite	Q9JLZ3.
Proteomic databases
PRIDE	Q9JLZ3.
Genome annotation databases
Ensembl	ENSMUST00000021913; ENSMUSP00000021913; ENSMUSG00000021460; Mus musculus. [Genome view] ENSMUST00000110031; ENSMUSP00000105658; ENSMUSG00000021460; Mus musculus. [Genome view]
GeneID	11992.
KEGG	mmu:11992.
UCSC	uc007qnd.1. mouse. uc007qng.1. mouse.
Organism-specific databases
CTD	11992.
MGI	MGI:1338011. Auh.
Phylogenomic databases
HOGENOM	HBG748731.
HOVERGEN	Q9JLZ3.
InParanoid	Q9JLZ3.
Enzyme and pathway databases
BRENDA	4.2.1.18. 244.
Gene expression databases
ArrayExpress	Q9JLZ3.
Bgee	Q9JLZ3.
CleanEx	MM_AUH.
Genevestigator	Q9JLZ3.
GermOnline	ENSMUSG00000021460. Mus musculus.
Family and domain databases
InterPro	IPR001753. Crotonase_core. IPR018376. Enoyl-CoA_hyd/isom_CS. [Graphical view]
Pfam	PF00378. ECH. 1 hit. [Graphical view]
PROSITE	PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	280169.
SOURCE	Search...

Entry information

Entry name

AUHM_MOUSE

Accession

Primary (citable) accession number: Q9JLZ3
Secondary accession number(s): Q80YD7 , Q8QZS0, Q9CY78, Q9D155

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	October 1, 2000
Last modified:	December 15, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)