P97807 (FUMH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fumarate hydratase, mitochondrial
Short name=Fumarase
EC=4.2.1.2

Alternative name(s):
EF-3

Gene names

Name:	Fh
Synonyms:	Fh1

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	507 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)

Catalytic activity	(S)-malate = fumarate + H2O.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subunit structure	Homotetramer By similarity.
Subcellular location	Isoform Mitochondrial: Mitochondrion. Isoform Cytoplasmic: Cytoplasm.
Post-translational modification	Isoform Cytoplasmic is acetylated at position 2 By similarity. Acetylation of Lys-474 is observed in liver mitochondria from fasted mice but not from fed mice.
Miscellaneous	There are 2 substrate binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity.
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative initiation
Domain	Transit peptide
Molecular function	Lyase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fumarate metabolic process Inferred from electronic annotation. Source: InterPro homeostasis of number of cells within a tissue Inferred from mutant phenotype PubMed 17418408. Source: MGI tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular_function	fumarate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform Mitochondrial (identifier: P97807-1)

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 Cytoplasmic (identifier: P97807-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: Missing.

Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2 (By similarity).

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 41	41	Mitochondrion By similarity
	Chain	42 – 507	466	Fumarate hydratase, mitochondrial		PRO_0000010323
Regions
	Region	173 – 176	4	B site By similarity
	Region	183 – 185	3	Substrate binding By similarity
Sites
	Binding site	144	1	Substrate By similarity
Amino acid modifications
	Modified residue	63	1	N6-acetyllysine Ref.6
	Modified residue	77	1	N6-acetyllysine By similarity
	Modified residue	112	1	N6-acetyllysine Ref.6
	Modified residue	289	1	N6-acetyllysine By similarity
	Modified residue	474	1	N6-acetyllysine Ref.6
Natural variations
	Alternative sequence	1 – 40	40	Missing in isoform Cytoplasmic.		VSP_018967
Experimental info
	Sequence conflict	183	1	S → N in AK002379. Ref.1
	Sequence conflict	236	1	A → T in AK002379. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mitochondrial [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 2F24F7B089608ABE	FASTA	507	54,357
	10 20 30 40 50 60 MYRALRLLAR SRRLLRVPSA GAAVSGEATT LPRCAPNVAR MASQNSFRVE FDTFGELKVP 70 80 90 100 110 120 TDKYYGAQTV RSTMNFKIGG ATERMPIPVI QAFGILKRAA AEVNQEYGLD PKIASAIMKA 130 140 150 160 170 180 ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV NEVISNRAIE MLGGELGSKK PVHPNDHVNK 190 200 210 220 230 240 SQSSNDTFPT AMHIAAAVEV HKVLLPGLQK LHDALSAKSK EFAQVIKIGR THTQDAVPLT 250 260 270 280 290 300 LGQEFSGYVQ QVQYAMVRIK AAMPRIYELA AGGTAVGTGL NTRIGFAEKV AAKVAALTGL 310 320 330 340 350 360 PFVTAPNKFE ALAAHDALVE LSGAMNTAAC SLMKIANDIR FLGSGPRSGL GELILPENEP 370 380 390 400 410 420 GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF ELNVFKPMMI KNVLHSARLL 430 440 450 460 470 480 GDASVSFTDN CVVGIQANTE RINKLMNESL MLVTALNPHI GYDKAAKIAK TAHKNGSTLK 490 500 ETAIELGYLT AEQFDEWVKP KDMLGPK
	Isoform Cytoplasmic [UniParc]. Checksum: 95ECA9B728E029AF	FASTA	467	50,053
	10 20 30 40 50 60 MASQNSFRVE FDTFGELKVP TDKYYGAQTV RSTMNFKIGG ATERMPIPVI QAFGILKRAA 70 80 90 100 110 120 AEVNQEYGLD PKIASAIMKA ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV NEVISNRAIE 130 140 150 160 170 180 MLGGELGSKK PVHPNDHVNK SQSSNDTFPT AMHIAAAVEV HKVLLPGLQK LHDALSAKSK 190 200 210 220 230 240 EFAQVIKIGR THTQDAVPLT LGQEFSGYVQ QVQYAMVRIK AAMPRIYELA AGGTAVGTGL 250 260 270 280 290 300 NTRIGFAEKV AAKVAALTGL PFVTAPNKFE ALAAHDALVE LSGAMNTAAC SLMKIANDIR 310 320 330 340 350 360 FLGSGPRSGL GELILPENEP GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF 370 380 390 400 410 420 ELNVFKPMMI KNVLHSARLL GDASVSFTDN CVVGIQANTE RINKLMNESL MLVTALNPHI 430 440 450 460 GYDKAAKIAK TAHKNGSTLK ETAIELGYLT AEQFDEWVKP KDMLGPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: Heart and Kidney.
[2]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"E2a-Pbx1 induces aberrant expression of tissue-specific and developmentally regulated genes when expressed in NIH 3T3 fibroblasts." Fu X., Kamps M.P. Mol. Cell. Biol. 17:1503-1512(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-282.
[5]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 49-71; 85-97; 99-112; 129-157; 181-210; 231-258; 266-283; 294-308; 348-368; 419-441; 445-464 AND 481-501, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[6]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-112 AND LYS-474, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK002379 mRNA. No translation available. AK147000 mRNA. Translation: BAE27597.1. CH466555 Genomic DNA. Translation: EDL13210.1. BC006048 mRNA. Translation: AAH06048.1. U72679 mRNA. Translation: AAB51039.1.
IPI	IPI00129928. IPI00759940.
RefSeq	NP_034339.2. NM_010209.2.
UniGene	Mm.41502.
3D structure databases
ProteinModelPortal	P97807.
SMR	P97807. Positions 46-507.
ModBase	Search...
Protein-protein interaction databases
IntAct	P97807. 3 interactions.
PTM databases
PhosphoSite	P97807.
2D gel databases
REPRODUCTION-2DPAGE	IPI00759940. P97807.
Proteomic databases
PaxDb	P97807.
PRIDE	P97807.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027810; ENSMUSP00000027810; ENSMUSG00000026526.
GeneID	14194.
KEGG	mmu:14194.
Organism-specific databases
CTD	14194.
MGI	MGI:95530. Fh1.
Phylogenomic databases
eggNOG	COG0114.
GeneTree	ENSGT00390000002779.
HOGENOM	HOG000061736.
HOVERGEN	HBG002183.
InParanoid	Q3UIA9.
KO	K01679.
OMA	KDTMGEV.
OrthoDB	EOG4F1X31.
Enzyme and pathway databases
UniPathway	UPA00223; UER01007.
Gene expression databases
ArrayExpress	P97807.
Bgee	P97807.
CleanEx	MM_FH1.
Genevestigator	P97807.
GermOnline	ENSMUSG00000026526. Mus musculus.
Family and domain databases
Gene3D	1.10.275.10. 1 hit.
InterPro	IPR005677. Fum_hydII. IPR024083. Fumarase/histidase_N. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. [Graphical view]
Pfam	PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00149. FUMRATELYASE.
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR00979. fumC_II. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	285416.
SOURCE	Search...

Entry information

Entry name

FUMH_MOUSE

Accession

Primary (citable) accession number: P97807
Secondary accession number(s): Q3UIA9, Q99JL0, Q9DCX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program