ID   DCHS_RAT                Reviewed;         656 AA.
AC   P16453; Q63029;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Histidine decarboxylase;
DE            Short=HDC;
DE            EC=4.1.1.22;
GN   Name=Hdc;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Fetal liver;
RX   PubMed=2300558; DOI=10.1073/pnas.87.2.733;
RA   Joseph D.R., Sullivan P.M., Wang Y.-M., Kozak C., Fenstermacher D.A.,
RA   Behrendsen M.E., Zahnow C.A.;
RT   "Characterization and expression of the complementary DNA encoding rat
RT   histidine decarboxylase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:733-737(1990).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=2402512; DOI=10.1073/pnas.87.18.7346-b;
RA   Joseph D.R., Sullivan P.M., Wang Y.-M., Kozak C., Fenstermacher D.A.,
RA   Behrendsen M.E., Zahnow C.A.;
RT   "Characterization and expression of the complementary DNA encoding rat
RT   histidine decarboxylase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:7346-7346(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 240-656.
RC   STRAIN=Sprague-Dawley; TISSUE=Fetal liver;
RX   PubMed=1702422; DOI=10.1016/s0021-9258(18)52414-5;
RA   Sullivan P.M., Petrusz P., Szpirer C., Joseph D.R.;
RT   "Alternative processing of androgen-binding protein RNA transcripts in
RT   fetal rat liver. Identification of a transcript formed by trans splicing.";
RL   J. Biol. Chem. 266:143-154(1991).
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   -!- ACTIVITY REGULATION: Phosphorylation of brain HDC by cAMP-dependent
CC       protein kinase leads to enzyme inactivation.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; histamine biosynthesis;
CC       histamine from L-histidine: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms may be produced.;
CC       Name=1;
CC         IsoId=P16453-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Brain, glandular regions of the stomach, mast cells
CC       and fetal liver.
CC   -!- PTM: May be post-translationally processed.
CC   -!- MISCELLANEOUS: A putative trans-splicing which involves HDC and SHBG
CC       gene regions produces a fusion protein expressed in fetal liver.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA63476.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M29591; AAA41326.1; -; mRNA.
DR   EMBL; M38759; AAA63476.1; ALT_INIT; mRNA.
DR   PIR; A34890; A34890.
DR   PIR; A39030; A39030.
DR   AlphaFoldDB; P16453; -.
DR   SMR; P16453; -.
DR   STRING; 10116.ENSRNOP00000041885; -.
DR   BindingDB; P16453; -.
DR   ChEMBL; CHEMBL3243911; -.
DR   PhosphoSitePlus; P16453; -.
DR   PaxDb; P16453; -.
DR   UCSC; RGD:2790; rat. [P16453-1]
DR   RGD; 2790; Hdc.
DR   eggNOG; KOG0628; Eukaryota.
DR   InParanoid; P16453; -.
DR   PhylomeDB; P16453; -.
DR   BioCyc; MetaCyc:MON-14635; -.
DR   Reactome; R-RNO-70921; Histidine catabolism.
DR   SABIO-RK; P16453; -.
DR   UniPathway; UPA00822; UER00786.
DR   PRO; PR:P16453; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0016597; F:amino acid binding; IDA:RGD.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0004398; F:histidine decarboxylase activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:RGD.
DR   GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0001694; P:histamine biosynthetic process; ISO:RGD.
DR   GO; GO:0001692; P:histamine metabolic process; IDA:RGD.
DR   GO; GO:0006548; P:histidine catabolic process; ISO:RGD.
DR   GO; GO:0006547; P:histidine metabolic process; IDA:RGD.
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   2: Evidence at transcript level;
KW   Alternative splicing; Catecholamine biosynthesis; Decarboxylase; Lyase;
KW   Phosphoprotein; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..656
FT                   /note="Histidine decarboxylase"
FT                   /id="PRO_0000146952"
FT   REGION          481..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         308
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         343
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         362
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   VARIANT         8
FT                   /note="H -> R"
FT   VARIANT         28
FT                   /note="V -> L"
FT   VARIANT         286
FT                   /note="R -> C"
SQ   SEQUENCE   656 AA;  73636 MW;  F21BB2B8D1A480F3 CRC64;
     MMEPSEYHEY QARGKEMVDY ICQYLSTVRE RQVTPNVKPG YLRAQIPSSA PEEPDSWDSI
     FGDIEQIIMP GVVHWQSPHM HAYYPALTSW PSLLGDMLAD AINCLGFTWA SSPACTELEM
     NIMDWLAKML GLPDFFLHHH PSSQGGGVLQ RTVSESTLIA LLAARKNKIL EMKAHEPNAD
     ESSLNARLVA YASDQAHSSV EKAGLISLVK IKFLPVDDNF SLRGEALQKA IEEDKQQGLV
     PVFVCATLGT TGVCAFDKLS ELGPICAREG LWLHVDAAYA GTAFLRPELR GFLKGIEYAD
     SFTFNPSKWM MVHFDCTGFW VKDKYKLQQT FSVNPIYLRH ANSGVATDFM HWQIPLSRRF
     RSIKLWFVIR SFGVKNLQAH VRHGTDMAKY FESLVRSDPV FEIPAERHLG LVVFRLKGPN
     CLTESVLKEI AKTGQVFLIP ATIQDKLIIR FTVTSQFTTK DDILRDWNLI REAANLVLSQ
     HCTSQPSPRA KNLIPPPVTR DSKDLTNGLS LESVNEGGDD PVQVRKIFRL PGDSLETTMD
     PFDDCFSEEA SDTTKHKLSS FLFSYLSVQN KKKTMRSLSC NSMPMSAQKS PPPDASVKHG
     GFFRARIFSG FPEEMMMMKK GGFKKLIKFY SVPSFPECSS QCGTLQLPCC PLQAMV