Reviewed, UniProtKB/Swiss-Prot P19113 (DCHS_HUMAN)

Names and origin

Protein names

Recommended name:
    Histidine decarboxylase
      Short name=HDC
    EC=4.1.1.22

Gene names

Name:

HDC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	662 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	L-histidine = histamine + CO2.
Cofactor	Pyridoxal phosphate.
Pathway	Amine and polyamine biosynthesis; histamine biosynthesis; histamine from L-histidine: step 1/1.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the group II decarboxylase family.

Ontologies

Keywords
Biological process	Catecholamine biosynthesis
Coding sequence diversity	Polymorphism
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Gene Ontology (GO)
Biological process	catecholamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW histidine metabolic process Traceable author statement. Source: ProtInc
Molecular function	histidine decarboxylase activity Traceable author statement. Source: ProtInc pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 662	662	Histidine decarboxylase		PRO_0000146950
Amino acid modifications
	Modified residue	305	1	N6-(pyridoxal phosphate)lysine Potential
Natural variations
	Natural variant	31	1	T → M: dbSNP rs17740607. Ref.5		VAR_048873
	Natural variant	49	1	E → V in a colorectal cancer sample; somatic mutation. Ref.6		VAR_036470
	Natural variant	285	1	E → K in a colorectal cancer sample; somatic mutation. Ref.6		VAR_036471
	Natural variant	553	1	F → L: dbSNP rs16963486.		VAR_048874
	Natural variant	644	1	E → D: dbSNP rs2073440.		VAR_033846
Experimental info
	Sequence conflict	118	1	N → M Ref.3
	Sequence conflict	148	1	S → Q Ref.1
	Sequence conflict	148	1	S → Q Ref.3
	Sequence conflict	500	1	W → M Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P19113-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: D7611CFAAD60F469	FASTA	662	74,141
	10 20 30 40 50 60 MMEPEEYRER GREMVDYICQ YLSTVRERRV TPDVQPGYLR AQLPESAPED PDSWDSIFGD 70 80 90 100 110 120 IERIIMPGVV HWQSPHMHAY YPALTSWPSL LGDMLADAIN CLGFTWASSP ACTELEMNVM 130 140 150 160 170 180 DWLAKMLGLP EHFLHHHPSS QGGGVLQSTV SESTLIALLA ARKNKILEMK TSEPDADESC 190 200 210 220 230 240 LNARLVAYAS DQAHSSVEKA GLISLVKMKF LPVDDNFSLR GEALQKAIEE DKQRGLVPVF 250 260 270 280 290 300 VCATLGTTGV CAFDCLSELG PICAREGLWL HIDAAYAGTA FLCPEFRGFL KGIEYADSFT 310 320 330 340 350 360 FNPSKWMMVH FDCTGFWVKD KYKLQQTFSV NPIYLRHANS GVATDFMHWQ IPLSRRFRSV 370 380 390 400 410 420 KLWFVIRSFG VKNLQAHVRH GTEMAKYFES LVRNDPSFEI PAKRHLGLVV FRLKGPNCLT 430 440 450 460 470 480 ENVLKEIAKA GRLFLIPATI QDKLIIRFTV TSQFTTRDDI LRDWNLIRDA ATLILSQHCT 490 500 510 520 530 540 SQPSPRVGNL ISQIRGARAW ACGTSLQSVS GAGDDPVQAR KIIKQPQRVG AGPMKRENGL 550 560 570 580 590 600 HLETLLDPVD DCFSEEAPDA TKHKLSSFLF SYLSVQTKKK TVRSLSCNSV PVSAQKPLPT 610 620 630 640 650 660 EASVKNGGSS RVRIFSRFPE DMMMLKKSAF KKLIKFYSVP SFPECSSQCG LQLPCCPLQA MV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the cDNA encoding L-histidine decarboxylase derived from human basophilic leukemia cell line, KU-812-F." Yamauchi K., Ruriko S., Ohkawara Y., Tanno Y., Maeyama K., Watanabe T., Satoh K., Yoshizawa M., Shibahara S., Takishima T. Nucleic Acids Res. 18:5891-5891(1990) [PubMed: 2216786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of the cDNA encoding human histidine decarboxylase from an erythroleukemia cell line and mapping of the gene locus to chromosome 15." Zahnow C.A., Yi H.F., McBride O.W., Joseph D.R. DNA Seq. 1:395-400(1991) [PubMed: 1768863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells." Mamune-Sato R., Yamauchi K., Tanno Y., Ohkawara Y., Ohtsu H., Katayose D., Maeyama K., Watanabe T., Shibahara S., Takishima T. Eur. J. Biochem. 209:533-539(1992) [PubMed: 1425659] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING. Tissue: Leukemia.
[4]	"Structure of the L-histidine decarboxylase gene." Yatsunami K., Ohtsu H., Tsuchikawa M., Higuchi T., Ishibashi K., Shida A., Shima Y., Nakagawa S., Yamauchi K., Yamamoto M., Hayashi N., Watanabe T., Ichikawa A. J. Biol. Chem. 269:1554-1559(1994) [PubMed: 8288622] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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], VARIANT MET-31.
[6]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-49 AND LYS-285.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X54297 mRNA. Translation: CAA38196.1. M60445 mRNA. Translation: AAC41698.1. D16583 Genomic DNA. Translation: BAA04015.1. BC130527 mRNA. Translation: AAI30528.1.
IPI	IPI00290368.
PIR	A49882.
RefSeq	NP_002103.2.
UniGene	Hs.1481
3D structure databases
HSSP	HSSP built from PDB template 1JS3 based on UniProtKB P80041.
ModBase	Search...
Proteomic databases
PRIDE	P19113.
Genome annotation databases
Ensembl	ENSG00000140287. Homo sapiens. [Contig view]
GeneID	3067.
KEGG	hsa:3067.
NMPDR	fig|9606.3.peg.10696.
Organism-specific databases
GeneCards	GC15M048321.
H-InvDB	HIX0012231.
HGNC	HGNC:4855. HDC.
MIM	142704. gene.
PharmGKB	PA29233.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P19113.
HOVERGEN	P19113.
OMA	P19113. LHHHPSS.
Enzyme and pathway databases
BRENDA	4.1.1.22. 247.
Gene expression databases
ArrayExpress	P19113.
Bgee	P19113.
CleanEx	HS_HDC.
GermOnline	ENSG00000140287. Homo sapiens.
Family and domain databases
InterPro	IPR010977. Aromatic_deC. IPR002129. PyrdxlP-dep_de-COase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
PANTHER	PTHR11999. Pyridoxal_deC. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
PRINTS	PR00800. YHDCRBOXLASE.
PROSITE	PS00392. DDC_GAD_HDC_YDC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00117. L-Histidine. DB00114. Pyridoxal Phosphate.
NextBio	12133.
SOURCE	Search...

Entry information

Entry name

DCHS_HUMAN

Accession

Primary (citable) accession number: P19113
Secondary accession number(s): A1L4G0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)