DCHS_MOUSE
ID DCHS_MOUSE Reviewed; 662 AA.
AC P23738; Q9QWU3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Histidine decarboxylase;
DE Short=HDC;
DE EC=4.1.1.22;
GN Name=Hdc;
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].
RX PubMed=2125007; DOI=10.1016/0014-5793(90)80545-t;
RA Yamamoto J., Yatsunami K., Ohmori E., Sugimoto Y., Fukui T., Katayama T.,
RA Ichikawa A.;
RT "cDNA-derived amino acid sequence of L-histidine decarboxylase from mouse
RT mastocytoma P-815 cells.";
RL FEBS Lett. 276:214-218(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Hasegawa M., Foote S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Testis, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RX PubMed=8250869; DOI=10.1006/bbrc.1993.2366;
RA Ohgoh M., Yamamoto J., Kawata M., Yamamura I., Fukui T., Ichikawa A.;
RT "Enhanced expression of the mouse L-histidine decarboxylase gene with a
RT combination of dexamethasone and 12-O-tetradecanoylphorbol-13-acetate.";
RL Biochem. Biophys. Res. Commun. 196:1113-1119(1993).
RN [7]
RP PROTEIN SEQUENCE OF 173-186; 207-212; 378-406; 437-449 AND 495-512.
RC TISSUE=Mast cell;
RX PubMed=8268224; DOI=10.1016/0167-4781(93)90011-2;
RA Yamamoto J., Fukui T., Suzuki K., Tanaka S., Yatsunami K., Ichikawa A.;
RT "Expression and characterization of recombinant mouse mastocytoma histidine
RT decarboxylase.";
RL Biochim. Biophys. Acta 1216:431-440(1993).
CC -!- FUNCTION: Catalyzes the biosynthesis of histamine from histidine.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-histidine = CO2 + histamine; Xref=Rhea:RHEA:20840,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57595,
CC ChEBI:CHEBI:58432; EC=4.1.1.22;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amine and polyamine biosynthesis; histamine biosynthesis;
CC histamine from L-histidine: step 1/1.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; X57437; CAA40685.1; -; mRNA.
DR EMBL; AF109137; AAC95389.1; -; mRNA.
DR EMBL; AK088545; BAC40415.1; -; mRNA.
DR EMBL; AK133455; BAE21666.1; -; mRNA.
DR EMBL; AK150168; BAE29356.1; -; mRNA.
DR EMBL; AK153104; BAE31724.1; -; mRNA.
DR EMBL; AL844555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28158.1; -; Genomic_DNA.
DR EMBL; S67000; AAB29093.1; -; Genomic_DNA.
DR CCDS; CCDS16684.1; -.
DR PIR; S12989; S12989.
DR RefSeq; NP_032256.3; NM_008230.6.
DR AlphaFoldDB; P23738; -.
DR SMR; P23738; -.
DR BioGRID; 200264; 1.
DR STRING; 10090.ENSMUSP00000028838; -.
DR PhosphoSitePlus; P23738; -.
DR PaxDb; P23738; -.
DR PRIDE; P23738; -.
DR ProteomicsDB; 279837; -.
DR Antibodypedia; 42596; 284 antibodies from 32 providers.
DR DNASU; 15186; -.
DR Ensembl; ENSMUST00000028838; ENSMUSP00000028838; ENSMUSG00000027360.
DR GeneID; 15186; -.
DR KEGG; mmu:15186; -.
DR UCSC; uc008mdr.2; mouse.
DR CTD; 3067; -.
DR MGI; MGI:96062; Hdc.
DR VEuPathDB; HostDB:ENSMUSG00000027360; -.
DR eggNOG; KOG0628; Eukaryota.
DR GeneTree; ENSGT00940000157938; -.
DR HOGENOM; CLU_011856_3_0_1; -.
DR InParanoid; P23738; -.
DR OMA; YKTPSRK; -.
DR OrthoDB; 856958at2759; -.
DR PhylomeDB; P23738; -.
DR TreeFam; TF313863; -.
DR BRENDA; 4.1.1.22; 3474.
DR Reactome; R-MMU-70921; Histidine catabolism.
DR SABIO-RK; P23738; -.
DR UniPathway; UPA00822; UER00786.
DR BioGRID-ORCS; 15186; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Hdc; mouse.
DR PRO; PR:P23738; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P23738; protein.
DR Bgee; ENSMUSG00000027360; Expressed in granulocyte and 145 other tissues.
DR Genevisible; P23738; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0004398; F:histidine decarboxylase activity; IMP:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
DR GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0001694; P:histamine biosynthetic process; IMP:MGI.
DR GO; GO:0001692; P:histamine metabolic process; ISO:MGI.
DR GO; GO:0006548; P:histidine catabolic process; IMP:MGI.
DR GO; GO:0006547; P:histidine metabolic process; ISO:MGI.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW Catecholamine biosynthesis; Decarboxylase; Direct protein sequencing;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..662
FT /note="Histidine decarboxylase"
FT /id="PRO_0000146951"
FT REGION 489..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 312
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 177
FT /note="K -> T (in Ref. 1; CAA40685 and 7; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 74045 MW; F4CBC771DD437E77 CRC64;
MMEPCEYREY REYYRARGKE MVDYISQYLS TVRERQVTPN VQPGYLRAQL PASAPEEPDS
WDSIFGDIER VIMPGVVHWQ SPHMHAYYPA LTSWPSLLGD MLADAINCLG FTWASSPACT
ELEMNIMDWL AKMLGLPEYF LHHHPSSRGG GVLQSTVSES TLIALLAARK NKILAMKACE
PDANESSLNA RLVAYTSDQA HSSVEKAGLI SLVKIRFLPV DDNFSLRGEA LQKAIEEDKQ
QGLVPVFVCA TLGTTGVCAF DRLSELGPIC ASEGLWLHVD AAYAGTAFLC PELRGFLEGI
EYADSFTFNP SKWMMVHFDC TGFWVKDKYK LQQTFSVNPI YLRHANSGAA TDFMHWQIPL
SRRFRSIKLW FVIRSFGVKN LQAHVRHGTE MAKYFESLVR SDPSFEIPAK RHLGLVVFRL
KGPNCLTESV LKEIAKAGQL FLIPATIQDK LIIRFTVTSQ FTTKEDILRD WHLIQEAANL
VLSQHCTSQP SPRAKNVIPP PPGTRGLSLE SVSEGGDDPA QARKIIKQPG ASLARREGGS
DLETMPDPFD DCFSEEAPNT TKHKLSSFLF SYLSVQNRRK TTRSLSCNSV PMSAQKSLPA
DASLKNGGSF RARIFSGFPE QMMMMKKGAF KKLIKFYSVP SFPECSSQCA RQLPCCPLEA
MV
