DCHS_HUMAN
ID DCHS_HUMAN Reviewed; 662 AA.
AC P19113; A1L4G0; B7ZM01;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Histidine decarboxylase;
DE Short=HDC;
DE EC=4.1.1.22;
GN Name=HDC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2216786; DOI=10.1093/nar/18.19.5891;
RA Yamauchi K., Ruriko S., Ohkawara Y., Tanno Y., Maeyama K., Watanabe T.,
RA Satoh K., Yoshizawa M., Shibahara S., Takishima T.;
RT "Nucleotide sequence of the cDNA encoding L-histidine decarboxylase derived
RT from human basophilic leukemia cell line, KU-812-F.";
RL Nucleic Acids Res. 18:5891-5891(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1768863; DOI=10.3109/10425179109020795;
RA Zahnow C.A., Yi H.F., McBride O.W., Joseph D.R.;
RT "Cloning of the cDNA encoding human histidine decarboxylase from an
RT erythroleukemia cell line and mapping of the gene locus to chromosome 15.";
RL DNA Seq. 1:395-400(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC TISSUE=Leukemia;
RX PubMed=1425659; DOI=10.1111/j.1432-1033.1992.tb17317.x;
RA Mamune-Sato R., Yamauchi K., Tanno Y., Ohkawara Y., Ohtsu H., Katayose D.,
RA Maeyama K., Watanabe T., Shibahara S., Takishima T.;
RT "Functional analysis of alternatively spliced transcripts of the human
RT histidine decarboxylase gene and its expression in human tissues and
RT basophilic leukemia cells.";
RL Eur. J. Biochem. 209:533-539(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8288622; DOI=10.1016/s0021-9258(17)42292-7;
RA Yatsunami K., Ohtsu H., Tsuchikawa M., Higuchi T., Ishibashi K., Shida A.,
RA Shima Y., Nakagawa S., Yamauchi K., Yamamoto M., Hayashi N., Watanabe T.,
RA Ichikawa A.;
RT "Structure of the L-histidine decarboxylase gene.";
RL J. Biol. Chem. 269:1554-1559(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP MET-31.
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-477 IN COMPLEX WITH HISTIDINE
RP METHYL ESTER AND PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, FUNCTION,
RP COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP LYS-305; TYR-334 AND SER-354.
RX PubMed=22767596; DOI=10.1074/jbc.m112.381897;
RA Komori H., Nitta Y., Ueno H., Higuchi Y.;
RT "Structural study reveals that Ser-354 determines substrate specificity on
RT human histidine decarboxylase.";
RL J. Biol. Chem. 287:29175-29183(2012).
RN [8]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-49 AND LYS-285.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Catalyzes the biosynthesis of histamine from histidine.
CC {ECO:0000269|PubMed:22767596}.
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 Evidence={ECO:0000269|PubMed:22767596};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:22767596};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for histidine {ECO:0000269|PubMed:22767596};
CC Vmax=1880 nmol/min/mg enzyme {ECO:0000269|PubMed:22767596};
CC -!- PATHWAY: Amine and polyamine biosynthesis; histamine biosynthesis;
CC histamine from L-histidine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22767596}.
CC -!- INTERACTION:
CC P19113; Q86UW9: DTX2; NbExp=6; IntAct=EBI-10200283, EBI-740376;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P19113-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P19113-2; Sequence=VSP_056296;
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; X54297; CAA38196.1; -; mRNA.
DR EMBL; M60445; AAC41698.1; -; mRNA.
DR EMBL; D16583; BAA04015.1; -; Genomic_DNA.
DR EMBL; AC009753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130527; AAI30528.1; -; mRNA.
DR EMBL; BC144173; AAI44174.1; -; mRNA.
DR CCDS; CCDS10134.1; -. [P19113-1]
DR CCDS; CCDS76754.1; -. [P19113-2]
DR PIR; A49882; A49882.
DR RefSeq; NP_001293075.1; NM_001306146.1. [P19113-2]
DR RefSeq; NP_002103.2; NM_002112.3. [P19113-1]
DR PDB; 4E1O; X-ray; 1.80 A; A/B/C/D/E/F=2-477.
DR PDB; 7EIW; X-ray; 2.10 A; A/B=2-477.
DR PDB; 7EIX; X-ray; 1.90 A; A/B=2-477.
DR PDB; 7EIY; X-ray; 2.20 A; A/B=2-477.
DR PDBsum; 4E1O; -.
DR PDBsum; 7EIW; -.
DR PDBsum; 7EIX; -.
DR PDBsum; 7EIY; -.
DR AlphaFoldDB; P19113; -.
DR SMR; P19113; -.
DR BioGRID; 109317; 3.
DR IntAct; P19113; 1.
DR STRING; 9606.ENSP00000267845; -.
DR ChEMBL; CHEMBL4523192; -.
DR DrugBank; DB00117; Histidine.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR CarbonylDB; P19113; -.
DR iPTMnet; P19113; -.
DR PhosphoSitePlus; P19113; -.
DR BioMuta; HDC; -.
DR DMDM; 1352220; -.
DR EPD; P19113; -.
DR MassIVE; P19113; -.
DR PaxDb; P19113; -.
DR PeptideAtlas; P19113; -.
DR PRIDE; P19113; -.
DR ProteomicsDB; 53634; -. [P19113-1]
DR ProteomicsDB; 7241; -.
DR Antibodypedia; 42596; 284 antibodies from 32 providers.
DR DNASU; 3067; -.
DR Ensembl; ENST00000267845.8; ENSP00000267845.3; ENSG00000140287.11. [P19113-1]
DR Ensembl; ENST00000543581.5; ENSP00000440252.1; ENSG00000140287.11. [P19113-2]
DR GeneID; 3067; -.
DR KEGG; hsa:3067; -.
DR MANE-Select; ENST00000267845.8; ENSP00000267845.3; NM_002112.4; NP_002103.2.
DR UCSC; uc001zxz.4; human. [P19113-1]
DR CTD; 3067; -.
DR DisGeNET; 3067; -.
DR GeneCards; HDC; -.
DR HGNC; HGNC:4855; HDC.
DR HPA; ENSG00000140287; Group enriched (brain, epididymis).
DR MalaCards; HDC; -.
DR MIM; 142704; gene.
DR neXtProt; NX_P19113; -.
DR OpenTargets; ENSG00000140287; -.
DR Orphanet; 856; NON RARE IN EUROPE: Tourette syndrome.
DR PharmGKB; PA29233; -.
DR VEuPathDB; HostDB:ENSG00000140287; -.
DR eggNOG; KOG0628; Eukaryota.
DR GeneTree; ENSGT00940000157938; -.
DR HOGENOM; CLU_011856_3_0_1; -.
DR InParanoid; P19113; -.
DR OMA; YKTPSRK; -.
DR OrthoDB; 856958at2759; -.
DR PhylomeDB; P19113; -.
DR TreeFam; TF313863; -.
DR BioCyc; MetaCyc:HS06697-MON; -.
DR BRENDA; 4.1.1.22; 2681.
DR PathwayCommons; P19113; -.
DR Reactome; R-HSA-70921; Histidine catabolism.
DR SABIO-RK; P19113; -.
DR SignaLink; P19113; -.
DR UniPathway; UPA00822; UER00786.
DR BioGRID-ORCS; 3067; 9 hits in 1071 CRISPR screens.
DR GeneWiki; Histidine_decarboxylase; -.
DR GenomeRNAi; 3067; -.
DR Pharos; P19113; Tbio.
DR PRO; PR:P19113; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P19113; protein.
DR Bgee; ENSG00000140287; Expressed in gall bladder and 124 other tissues.
DR ExpressionAtlas; P19113; baseline and differential.
DR Genevisible; P19113; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0004398; F:histidine decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0001694; P:histamine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006548; P:histidine catabolic process; IDA:UniProtKB.
DR GO; GO:0006547; P:histidine metabolic process; TAS:ProtInc.
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 3D-structure; Alternative splicing; Catecholamine biosynthesis;
KW Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..662
FT /note="Histidine decarboxylase"
FT /id="PRO_0000146950"
FT BINDING 81
FT /ligand="substrate"
FT BINDING 194
FT /ligand="substrate"
FT MOD_RES 305
FT /note="N6-(pyridoxal phosphate)lysine"
FT VAR_SEQ 348..380
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056296"
FT VARIANT 31
FT /note="T -> M (in dbSNP:rs17740607)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048873"
FT VARIANT 49
FT /note="E -> V (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036470"
FT VARIANT 285
FT /note="E -> K (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1353958864)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036471"
FT VARIANT 553
FT /note="F -> L (in dbSNP:rs16963486)"
FT /id="VAR_048874"
FT VARIANT 644
FT /note="E -> D (in dbSNP:rs2073440)"
FT /id="VAR_033846"
FT MUTAGEN 305
FT /note="K->G: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22767596"
FT MUTAGEN 334
FT /note="Y->F: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22767596"
FT MUTAGEN 354
FT /note="S->G: Strongly decreases affinity for histidine.
FT Strongly increases affinity for L-DOPA and confers enzyme
FT activity toward L-DOPA."
FT /evidence="ECO:0000269|PubMed:22767596"
FT CONFLICT 118
FT /note="N -> M (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="S -> Q (in Ref. 1; CAA38196 and 3; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="W -> M (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 4..23
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:4E1O"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:4E1O"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 150..172
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:4E1O"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 284..290
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:4E1O"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4E1O"
FT TURN 338..342
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 359..393
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 406..415
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 417..430
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:4E1O"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:4E1O"
FT HELIX 457..475
FT /evidence="ECO:0007829|PDB:4E1O"
SQ SEQUENCE 662 AA; 74141 MW; D7611CFAAD60F469 CRC64;
MMEPEEYRER GREMVDYICQ YLSTVRERRV TPDVQPGYLR AQLPESAPED PDSWDSIFGD
IERIIMPGVV HWQSPHMHAY YPALTSWPSL LGDMLADAIN CLGFTWASSP ACTELEMNVM
DWLAKMLGLP EHFLHHHPSS QGGGVLQSTV SESTLIALLA ARKNKILEMK TSEPDADESC
LNARLVAYAS DQAHSSVEKA GLISLVKMKF LPVDDNFSLR GEALQKAIEE DKQRGLVPVF
VCATLGTTGV CAFDCLSELG PICAREGLWL HIDAAYAGTA FLCPEFRGFL KGIEYADSFT
FNPSKWMMVH FDCTGFWVKD KYKLQQTFSV NPIYLRHANS GVATDFMHWQ IPLSRRFRSV
KLWFVIRSFG VKNLQAHVRH GTEMAKYFES LVRNDPSFEI PAKRHLGLVV FRLKGPNCLT
ENVLKEIAKA GRLFLIPATI QDKLIIRFTV TSQFTTRDDI LRDWNLIRDA ATLILSQHCT
SQPSPRVGNL ISQIRGARAW ACGTSLQSVS GAGDDPVQAR KIIKQPQRVG AGPMKRENGL
HLETLLDPVD DCFSEEAPDA TKHKLSSFLF SYLSVQTKKK TVRSLSCNSV PVSAQKPLPT
EASVKNGGSS RVRIFSRFPE DMMMLKKSAF KKLIKFYSVP SFPECSSQCG LQLPCCPLQA
MV
