HUTH_MOUSE
ID HUTH_MOUSE Reviewed; 657 AA.
AC P35492;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Histidine ammonia-lyase;
DE Short=Histidase;
DE EC=4.3.1.3;
GN Name=Hal; Synonyms=Hsd, Huth;
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 [MRNA], AND VARIANT HIS GLN-322.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=8486363; DOI=10.1006/geno.1993.1164;
RA Taylor R.G., Grieco D., Clarke G.A., McInnes R.R., Taylor B.A.;
RT "Identification of the mutation in murine histidinemia (his) and genetic
RT mapping of the murine histidase locus (Hal) on chromosome 10.";
RL Genomics 16:231-240(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-396 AND SER-648, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-396 AND THR-637, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Pancreas;
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine = NH4(+) + trans-urocanate; Xref=Rhea:RHEA:21232,
CC ChEBI:CHEBI:17771, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595; EC=4.3.1.3;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10122};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Ala-Ser-Gly. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Hal are the cause of histidinemia (His).
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR EMBL; L07645; AAA37777.1; -; mRNA.
DR EMBL; AK014518; BAB29407.1; -; mRNA.
DR EMBL; BC057637; AAH57637.1; -; mRNA.
DR CCDS; CCDS36036.1; -.
DR PIR; A46128; A46128.
DR RefSeq; NP_034531.1; NM_010401.4.
DR AlphaFoldDB; P35492; -.
DR SMR; P35492; -.
DR BioGRID; 200203; 12.
DR STRING; 10090.ENSMUSP00000123336; -.
DR iPTMnet; P35492; -.
DR PhosphoSitePlus; P35492; -.
DR jPOST; P35492; -.
DR MaxQB; P35492; -.
DR PaxDb; P35492; -.
DR PRIDE; P35492; -.
DR ProteomicsDB; 273324; -.
DR Antibodypedia; 30149; 156 antibodies from 26 providers.
DR DNASU; 15109; -.
DR Ensembl; ENSMUST00000129421; ENSMUSP00000123336; ENSMUSG00000020017.
DR GeneID; 15109; -.
DR KEGG; mmu:15109; -.
DR UCSC; uc007gus.1; mouse.
DR CTD; 3034; -.
DR MGI; MGI:96010; Hal.
DR VEuPathDB; HostDB:ENSMUSG00000020017; -.
DR eggNOG; KOG0222; Eukaryota.
DR GeneTree; ENSGT00390000009047; -.
DR HOGENOM; CLU_014801_4_0_1; -.
DR InParanoid; P35492; -.
DR OMA; CAPQVAG; -.
DR OrthoDB; 923557at2759; -.
DR PhylomeDB; P35492; -.
DR TreeFam; TF313824; -.
DR Reactome; R-MMU-70921; Histidine catabolism.
DR UniPathway; UPA00379; UER00549.
DR BioGRID-ORCS; 15109; 1 hit in 73 CRISPR screens.
DR PRO; PR:P35492; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P35492; protein.
DR Bgee; ENSMUSG00000020017; Expressed in skin of external ear and 77 other tissues.
DR ExpressionAtlas; P35492; baseline and differential.
DR Genevisible; P35492; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; IDA:MGI.
DR GO; GO:0006548; P:histidine catabolic process; IDA:MGI.
DR GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR CDD; cd00332; PAL-HAL; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR InterPro; IPR001106; Aromatic_Lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR005921; HutH.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR021922; Par3/HAL_N.
DR InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR Pfam; PF12053; Par3_HAL_N_term; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR01225; hutH; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 1: Evidence at protein level;
KW Disease variant; Histidine metabolism; Lyase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..657
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000161059"
FT MOD_RES 254
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21213"
FT MOD_RES 637
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CROSSLNK 253..255
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250"
FT VARIANT 322
FT /note="R -> Q (in His; reduced stability)"
FT /evidence="ECO:0000269|PubMed:8486363"
SQ SEQUENCE 657 AA; 72258 MW; 03402C348686C22D CRC64;
MPRYTVHVRG EWLAVPCQDG KLTVGWLGRE AVRRYMKNKP DNGGFTSVDE VQFLVHRCKG
LGLLDNEDEL EVALEDNEFV EVVIEGDVMS PDFIPSQPEG VFLYSKYREP EKYIALDGDS
LSTEDLVNLG KGRYKIKLTS IAEKKVQQSR EVIDSIIKER TVVYGITTGF GKFARTVIPA
NKLQELQVNL VRSHSSGVGK PLSPERCRML LALRINVLAK GYSGISLETL KQVIEAFNAS
CLSYVPEKGT VGASGDLAPL SHLALGLIGE GKMWSPKSGW ADAKYVLEAH GLKPIVLKPK
EGLALINGTQ MITSLGCEAL ERASAIARQA DIVAALTLEV LKGTTKAFDT DIHAVRPHRG
QIEVAFRFRS LLDSDHHPSE IAESHRFCDR VQDAYTLRCC PQVHGVVNDT IAFVKDIITT
ELNSATDNPM VFASRGETIS GGNFHGEYPA KALDYLAIGV HELAAISERR IERLCNPSLS
ELPAFLVAEG GLNSGFMIAH CTAAALVSES KALCHPSSVD SLSTSAATED HVSMGGWAAR
KALRVVEHVE QVLAIELLAA CQGIEFLRPL KTTTPLEKVY DLVRSVVRPW IKDRFMAPDI
EAAHRLLLDQ KVWEVAAPYI EKYRMEHIPE SRPLSPTAFS LESLRKNSAT IPESDDL
