P35492 (HUTH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidine ammonia-lyase
Short name=Histidase
EC=4.3.1.3

Gene names

Name:	Hal
Synonyms:	Hsd, Huth

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 › Mus

Protein attributes

Sequence length	657 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-histidine = urocanate + NH3.
Pathway	Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
Post-translational modification	Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly By similarity.
Involvement in disease	Note=Defects in Hal are the cause of histidinemia (His).
Sequence similarities	Belongs to the PAL/histidase family.

Ontologies

Keywords
Biological process	Histidine metabolism
Disease	Disease mutation
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro histidine catabolic process Inferred from direct assay Ref.1. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro soluble fraction Inferred from direct assay Ref.1. Source: MGI
Molecular function	histidine ammonia-lyase activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 657	657	Histidine ammonia-lyase		PRO_0000161059
Amino acid modifications
	Modified residue	254	1	2,3-didehydroalanine (Ser) By similarity
	Modified residue	631	1	Phosphoserine Ref.5
	Modified residue	635	1	Phosphoserine Ref.5 Ref.6
	Modified residue	648	1	Phosphoserine Ref.4 Ref.5
	Cross-link	253 ↔ 255		5-imidazolinone (Ala-Gly) By similarity
Natural variations
	Natural variant	322	1	R → Q in His; reduced stability. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P35492 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 03402C348686C22D	FASTA	657	72,258
	10 20 30 40 50 60 MPRYTVHVRG EWLAVPCQDG KLTVGWLGRE AVRRYMKNKP DNGGFTSVDE VQFLVHRCKG 70 80 90 100 110 120 LGLLDNEDEL EVALEDNEFV EVVIEGDVMS PDFIPSQPEG VFLYSKYREP EKYIALDGDS 130 140 150 160 170 180 LSTEDLVNLG KGRYKIKLTS IAEKKVQQSR EVIDSIIKER TVVYGITTGF GKFARTVIPA 190 200 210 220 230 240 NKLQELQVNL VRSHSSGVGK PLSPERCRML LALRINVLAK GYSGISLETL KQVIEAFNAS 250 260 270 280 290 300 CLSYVPEKGT VGASGDLAPL SHLALGLIGE GKMWSPKSGW ADAKYVLEAH GLKPIVLKPK 310 320 330 340 350 360 EGLALINGTQ MITSLGCEAL ERASAIARQA DIVAALTLEV LKGTTKAFDT DIHAVRPHRG 370 380 390 400 410 420 QIEVAFRFRS LLDSDHHPSE IAESHRFCDR VQDAYTLRCC PQVHGVVNDT IAFVKDIITT 430 440 450 460 470 480 ELNSATDNPM VFASRGETIS GGNFHGEYPA KALDYLAIGV HELAAISERR IERLCNPSLS 490 500 510 520 530 540 ELPAFLVAEG GLNSGFMIAH CTAAALVSES KALCHPSSVD SLSTSAATED HVSMGGWAAR 550 560 570 580 590 600 KALRVVEHVE QVLAIELLAA CQGIEFLRPL KTTTPLEKVY DLVRSVVRPW IKDRFMAPDI 610 620 630 640 650 EAAHRLLLDQ KVWEVAAPYI EKYRMEHIPE SRPLSPTAFS LESLRKNSAT IPESDDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of the mutation in murine histidinemia (his) and genetic mapping of the murine histidase locus (Hal) on chromosome 10." Taylor R.G., Grieco D., Clarke G.A., McInnes R.R., Taylor B.A. Genomics 16:231-240(1993) [PubMed: 8486363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS GLN-322. Strain: C57BL/6J. Tissue: Liver.
[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]. Strain: C57BL/6J. Tissue: Skin.
[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]. Strain: FVB/N. Tissue: Liver.
[4]	"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: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-635 AND SER-648, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L07645 mRNA. Translation: AAA37777.1. AK014518 mRNA. Translation: BAB29407.1. BC057637 mRNA. Translation: AAH57637.1.
IPI	IPI00118625.
PIR	A46128.
RefSeq	NP_034531.1. NM_010401.3.
UniGene	Mm.13000.
3D structure databases
ProteinModelPortal	P35492.
SMR	P35492. Positions 3-85, 112-619.
ModBase	Search...
Protein-protein interaction databases
STRING	P35492.
PTM databases
PhosphoSite	P35492.
Proteomic databases
PRIDE	P35492.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000129421; ENSMUSP00000123336; ENSMUSG00000020017.
GeneID	15109.
KEGG	mmu:15109.
NMPDR	fig|10090.3.peg.14273.
Organism-specific databases
CTD	3034.
MGI	MGI:96010. Hal.
Phylogenomic databases
eggNOG	roNOG12953.
GeneTree	ENSGT00390000009047.
HOGENOM	HBG510887.
HOVERGEN	HBG004509.
InParanoid	P35492.
OMA	QKGQIDS.
Gene expression databases
ArrayExpress	P35492.
Bgee	P35492.
CleanEx	MM_HAL.
Genevestigator	P35492.
GermOnline	ENSMUSG00000020017. Mus musculus.
Family and domain databases
InterPro	IPR005921. HutH. IPR008948. L-Aspartase-like. IPR024083. L-Aspartase-like_N. IPR001106. Phe/His_NH3-lyase. IPR022313. Phe/His_NH3-lyase_AS. [Graphical view]
Gene3D	G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KO	K01745.
Pfam	PF00221. PAL. 1 hit. [Graphical view]
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR01225. HutH. 1 hit.
PROSITE	PS00488. PAL_HISTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	287506.
SOURCE	Search...

Entry information

Entry name

HUTH_MOUSE

Accession

Primary (citable) accession number: P35492

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 16, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program