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 08-NOV-2023, entry version 149.
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; 10116-ENSRNOP00000041885; -.
DR UCSC; RGD:2790; rat. [P16453-1]
DR AGR; RGD:2790; -.
DR RGD; 2790; Hdc.
DR eggNOG; KOG0628; Eukaryota.
DR InParanoid; P16453; -.
DR PhylomeDB; P16453; -.
DR BioCyc; MetaCyc:MONOMER-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: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: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 CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF68; HISTIDINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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
//
