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P23738

- DCHS_MOUSE

UniProt

P23738 - DCHS_MOUSE

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Protein

Histidine decarboxylase

Gene

Hdc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the biosynthesis of histamine from histidine.By similarity

Catalytic activityi

L-histidine = histamine + CO2.

Cofactori

Pyridoxal phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881Substrate; via amide nitrogenBy similarity
Binding sitei201 – 2011SubstrateBy similarity

GO - Molecular functioni

  1. histidine decarboxylase activity Source: MGI
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. catecholamine biosynthetic process Source: UniProtKB-KW
  2. histamine biosynthetic process Source: MGI
  3. histidine catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00822; UER00786.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine decarboxylase (EC:4.1.1.22)
Short name:
HDC
Gene namesi
Name:Hdc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:96062. Hdc.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 662662Histidine decarboxylasePRO_0000146951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei312 – 3121N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiP23738.

PTM databases

PhosphoSiteiP23738.

Expressioni

Gene expression databases

BgeeiP23738.
CleanExiMM_HDC.
GenevestigatoriP23738.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028838.

Structurei

3D structure databases

ProteinModelPortaliP23738.
SMRiP23738. Positions 2-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00760000119205.
HOGENOMiHOG000121941.
HOVERGENiHBG000944.
InParanoidiP23738.
KOiK01590.
OMAiPICASEG.
OrthoDBiEOG75B851.
TreeFamiTF313863.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010977. Aromatic_deC.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
PRINTSiPR00800. YHDCRBOXLASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23738-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMEPCEYREY REYYRARGKE MVDYISQYLS TVRERQVTPN VQPGYLRAQL
60 70 80 90 100
PASAPEEPDS WDSIFGDIER VIMPGVVHWQ SPHMHAYYPA LTSWPSLLGD
110 120 130 140 150
MLADAINCLG FTWASSPACT ELEMNIMDWL AKMLGLPEYF LHHHPSSRGG
160 170 180 190 200
GVLQSTVSES TLIALLAARK NKILAMKACE PDANESSLNA RLVAYTSDQA
210 220 230 240 250
HSSVEKAGLI SLVKIRFLPV DDNFSLRGEA LQKAIEEDKQ QGLVPVFVCA
260 270 280 290 300
TLGTTGVCAF DRLSELGPIC ASEGLWLHVD AAYAGTAFLC PELRGFLEGI
310 320 330 340 350
EYADSFTFNP SKWMMVHFDC TGFWVKDKYK LQQTFSVNPI YLRHANSGAA
360 370 380 390 400
TDFMHWQIPL SRRFRSIKLW FVIRSFGVKN LQAHVRHGTE MAKYFESLVR
410 420 430 440 450
SDPSFEIPAK RHLGLVVFRL KGPNCLTESV LKEIAKAGQL FLIPATIQDK
460 470 480 490 500
LIIRFTVTSQ FTTKEDILRD WHLIQEAANL VLSQHCTSQP SPRAKNVIPP
510 520 530 540 550
PPGTRGLSLE SVSEGGDDPA QARKIIKQPG ASLARREGGS DLETMPDPFD
560 570 580 590 600
DCFSEEAPNT TKHKLSSFLF SYLSVQNRRK TTRSLSCNSV PMSAQKSLPA
610 620 630 640 650
DASLKNGGSF RARIFSGFPE QMMMMKKGAF KKLIKFYSVP SFPECSSQCA
660
RQLPCCPLEA MV
Length:662
Mass (Da):74,045
Last modified:July 27, 2011 - v2
Checksum:iF4CBC771DD437E77
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1771K → T in CAA40685. (PubMed:2125007)Curated
Sequence conflicti177 – 1771K → T AA sequence (PubMed:8268224)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57437 mRNA. Translation: CAA40685.1.
AF109137 mRNA. Translation: AAC95389.1.
AK088545 mRNA. Translation: BAC40415.1.
AK133455 mRNA. Translation: BAE21666.1.
AK150168 mRNA. Translation: BAE29356.1.
AK153104 mRNA. Translation: BAE31724.1.
AL844555 Genomic DNA. Translation: CAM18696.1.
CH466519 Genomic DNA. Translation: EDL28158.1.
S67000 Genomic DNA. Translation: AAB29093.1.
CCDSiCCDS16684.1.
PIRiS12989.
RefSeqiNP_032256.3. NM_008230.6.
UniGeneiMm.18603.

Genome annotation databases

EnsembliENSMUST00000028838; ENSMUSP00000028838; ENSMUSG00000027360.
GeneIDi15186.
KEGGimmu:15186.
UCSCiuc008mdr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57437 mRNA. Translation: CAA40685.1 .
AF109137 mRNA. Translation: AAC95389.1 .
AK088545 mRNA. Translation: BAC40415.1 .
AK133455 mRNA. Translation: BAE21666.1 .
AK150168 mRNA. Translation: BAE29356.1 .
AK153104 mRNA. Translation: BAE31724.1 .
AL844555 Genomic DNA. Translation: CAM18696.1 .
CH466519 Genomic DNA. Translation: EDL28158.1 .
S67000 Genomic DNA. Translation: AAB29093.1 .
CCDSi CCDS16684.1.
PIRi S12989.
RefSeqi NP_032256.3. NM_008230.6.
UniGenei Mm.18603.

3D structure databases

ProteinModelPortali P23738.
SMRi P23738. Positions 2-484.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000028838.

PTM databases

PhosphoSitei P23738.

Proteomic databases

PRIDEi P23738.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028838 ; ENSMUSP00000028838 ; ENSMUSG00000027360 .
GeneIDi 15186.
KEGGi mmu:15186.
UCSCi uc008mdr.1. mouse.

Organism-specific databases

CTDi 3067.
MGIi MGI:96062. Hdc.

Phylogenomic databases

eggNOGi COG0076.
GeneTreei ENSGT00760000119205.
HOGENOMi HOG000121941.
HOVERGENi HBG000944.
InParanoidi P23738.
KOi K01590.
OMAi PICASEG.
OrthoDBi EOG75B851.
TreeFami TF313863.

Enzyme and pathway databases

UniPathwayi UPA00822 ; UER00786 .

Miscellaneous databases

ChiTaRSi HDC. mouse.
NextBioi 287711.
PROi P23738.
SOURCEi Search...

Gene expression databases

Bgeei P23738.
CleanExi MM_HDC.
Genevestigatori P23738.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR010977. Aromatic_deC.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view ]
Pfami PF00282. Pyridoxal_deC. 1 hit.
[Graphical view ]
PRINTSi PR00800. YHDCRBOXLASE.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA-derived amino acid sequence of L-histidine decarboxylase from mouse mastocytoma P-815 cells."
    Yamamoto J., Yatsunami K., Ohmori E., Sugimoto Y., Fukui T., Katayama T., Ichikawa A.
    FEBS Lett. 276:214-218(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Hasegawa M., Foote S.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Liver.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Testis and Thymus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Enhanced expression of the mouse L-histidine decarboxylase gene with a combination of dexamethasone and 12-O-tetradecanoylphorbol-13-acetate."
    Ohgoh M., Yamamoto J., Kawata M., Yamamura I., Fukui T., Ichikawa A.
    Biochem. Biophys. Res. Commun. 196:1113-1119(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
  7. "Expression and characterization of recombinant mouse mastocytoma histidine decarboxylase."
    Yamamoto J., Fukui T., Suzuki K., Tanaka S., Yatsunami K., Ichikawa A.
    Biochim. Biophys. Acta 1216:431-440(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 173-186; 207-212; 378-406; 437-449 AND 495-512.
    Tissue: Mast cell.

Entry informationi

Entry nameiDCHS_MOUSE
AccessioniPrimary (citable) accession number: P23738
Secondary accession number(s): Q9QWU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3