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P23738

- DCHS_MOUSE

UniProt

P23738 - DCHS_MOUSE

Protein

Histidine decarboxylase

Gene

Hdc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    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.
    GeneTreeiENSGT00730000110825.
    HOGENOMiHOG000121941.
    HOVERGENiHBG000944.
    InParanoidiQ9QWU3.
    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

    MMEPCEYREY REYYRARGKE MVDYISQYLS TVRERQVTPN VQPGYLRAQL    50
    PASAPEEPDS WDSIFGDIER VIMPGVVHWQ SPHMHAYYPA LTSWPSLLGD 100
    MLADAINCLG FTWASSPACT ELEMNIMDWL AKMLGLPEYF LHHHPSSRGG 150
    GVLQSTVSES TLIALLAARK NKILAMKACE PDANESSLNA RLVAYTSDQA 200
    HSSVEKAGLI SLVKIRFLPV DDNFSLRGEA LQKAIEEDKQ QGLVPVFVCA 250
    TLGTTGVCAF DRLSELGPIC ASEGLWLHVD AAYAGTAFLC PELRGFLEGI 300
    EYADSFTFNP SKWMMVHFDC TGFWVKDKYK LQQTFSVNPI YLRHANSGAA 350
    TDFMHWQIPL SRRFRSIKLW FVIRSFGVKN LQAHVRHGTE MAKYFESLVR 400
    SDPSFEIPAK RHLGLVVFRL KGPNCLTESV LKEIAKAGQL FLIPATIQDK 450
    LIIRFTVTSQ FTTKEDILRD WHLIQEAANL VLSQHCTSQP SPRAKNVIPP 500
    PPGTRGLSLE SVSEGGDDPA QARKIIKQPG ASLARREGGS DLETMPDPFD 550
    DCFSEEAPNT TKHKLSSFLF SYLSVQNRRK TTRSLSCNSV PMSAQKSLPA 600
    DASLKNGGSF RARIFSGFPE QMMMMKKGAF KKLIKFYSVP SFPECSSQCA 650
    RQLPCCPLEA MV 662
    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 ENSGT00730000110825.
    HOGENOMi HOG000121941.
    HOVERGENi HBG000944.
    InParanoidi Q9QWU3.
    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

    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 1, 2014
    This is version 103 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