ID   DCOR_RAT                Reviewed;         461 AA.
AC   P09057;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Ornithine decarboxylase;
DE            Short=ODC;
DE            EC=4.1.1.17;
GN   Name=Odc1; Synonyms=Odc;
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].
RX   PubMed=3443298; DOI=10.1016/0378-1119(87)90222-8;
RA   van Kranen H.J., van de Zande L., van Kreijl C.F., Bisschop A.,
RA   Wieringa B.;
RT   "Cloning and nucleotide sequence of rat ornithine decarboxylase cDNA.";
RL   Gene 60:145-155(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=3419906; DOI=10.1093/nar/16.16.8173;
RA   van Steeg H., van Oostrom C.T.M., van Kranen H.J., van Kreijl C.F.;
RT   "Nucleotide sequence of the rat ornithine decarboxylase gene.";
RL   Nucleic Acids Res. 16:8173-8174(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Fischer; TISSUE=Liver;
RX   PubMed=2722815; DOI=10.1016/s0021-9258(18)81896-8;
RA   Wen L., Huang J.K., Blackshear P.J.;
RT   "Rat ornithine decarboxylase gene. Nucleotide sequence, potential
RT   regulatory elements, and comparison to the mouse gene.";
RL   J. Biol. Chem. 264:9016-9021(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-37.
RX   PubMed=2006916; DOI=10.1042/bj2740521;
RA   Van Steeg H., Van Oostrom C.T.M., Hodemaekers H.M., Peters L., Thomas A.A.;
RT   "The translation in vitro of rat ornithine decarboxylase mRNA is blocked by
RT   its 5' untranslated region in a polyamine-independent way.";
RL   Biochem. J. 274:521-526(1991).
CC   -!- FUNCTION: Catalyzes the first and rate-limiting step of polyamine
CC       biosynthesis that converts ornithine into putrescine, which is the
CC       precursor for the polyamines, spermidine and spermine. Polyamines are
CC       essential for cell proliferation and are implicated in cellular
CC       processes, ranging from DNA replication to apoptosis.
CC       {ECO:0000250|UniProtKB:P11926}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:326268; EC=4.1.1.17;
CC         Evidence={ECO:0000250|UniProtKB:P11926};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P11926};
CC   -!- ACTIVITY REGULATION: Inhibited by antizymes (AZs) OAZ1, OAZ2 and OAZ3
CC       in response to polyamine levels. AZs inhibit the assembly of the
CC       functional homodimer by binding to ODC monomers. Additionally, OAZ1
CC       targets ODC monomers for ubiquitin-independent proteolytic destruction
CC       by the 26S proteasome. {ECO:0000250|UniProtKB:P11926}.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC   -!- SUBUNIT: Homodimer. Only the dimer is catalytically active, as the
CC       active sites are constructed of residues from both monomers.
CC       {ECO:0000250|UniProtKB:P00860}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000305}.
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DR   EMBL; M16982; AAA41737.1; -; mRNA.
DR   EMBL; X07944; CAA30765.1; -; Genomic_DNA.
DR   EMBL; J04792; AAA66286.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; J04791; AAA66164.1; -; mRNA.
DR   EMBL; BC078882; AAH78882.1; -; mRNA.
DR   PIR; A27361; DCRTO.
DR   RefSeq; NP_001289012.1; NM_001302083.1.
DR   RefSeq; NP_036747.1; NM_012615.3.
DR   RefSeq; XP_006239969.1; XM_006239907.3.
DR   RefSeq; XP_006239970.1; XM_006239908.3.
DR   RefSeq; XP_017449519.1; XM_017594030.1.
DR   AlphaFoldDB; P09057; -.
DR   SMR; P09057; -.
DR   STRING; 10116.ENSRNOP00000007259; -.
DR   BindingDB; P09057; -.
DR   ChEMBL; CHEMBL3511; -.
DR   DrugCentral; P09057; -.
DR   iPTMnet; P09057; -.
DR   PhosphoSitePlus; P09057; -.
DR   PaxDb; P09057; -.
DR   Ensembl; ENSRNOT00000007259; ENSRNOP00000007259; ENSRNOG00000005424.
DR   GeneID; 24609; -.
DR   KEGG; rno:24609; -.
DR   CTD; 4953; -.
DR   RGD; 3227; Odc1.
DR   eggNOG; KOG0622; Eukaryota.
DR   GeneTree; ENSGT00950000182995; -.
DR   InParanoid; P09057; -.
DR   OMA; YCRSMAS; -.
DR   OrthoDB; 725914at2759; -.
DR   PhylomeDB; P09057; -.
DR   TreeFam; TF300760; -.
DR   BRENDA; 4.1.1.17; 5301.
DR   Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-RNO-351202; Metabolism of polyamines.
DR   SABIO-RK; P09057; -.
DR   UniPathway; UPA00535; UER00288.
DR   PRO; PR:P09057; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000005424; Expressed in kidney and 20 other tissues.
DR   ExpressionAtlas; P09057; baseline and differential.
DR   Genevisible; P09057; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IDA:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; ISO:RGD.
DR   GO; GO:0006595; P:polyamine metabolic process; IDA:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0009446; P:putrescine biosynthetic process; IDA:RGD.
DR   GO; GO:0033387; P:putrescine biosynthetic process from ornithine; ISS:UniProtKB.
DR   GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; ISO:RGD.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022657; De-COase2_CS.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR002433; Orn_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR11482; PTHR11482; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   PRINTS; PR01182; ORNDCRBXLASE.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Direct protein sequencing; Lyase; Phosphoprotein;
KW   Polyamine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   S-nitrosylation.
FT   CHAIN           1..461
FT                   /note="Ornithine decarboxylase"
FT                   /id="PRO_0000149894"
FT   ACT_SITE        360
FT                   /note="Proton donor; shared with dimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         200
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         237
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         274..277
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         331..332
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P07805"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P07805"
FT   BINDING         389
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   SITE            197
FT                   /note="Stacks against the aromatic ring of pyridoxal
FT                   phosphate and stabilizes reaction intermediates"
FT                   /evidence="ECO:0000250|UniProtKB:P00860"
FT   MOD_RES         69
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   MOD_RES         303
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P00860"
FT   MOD_RES         360
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
SQ   SEQUENCE   461 AA;  51047 MW;  CEF9D268DDDE0DA6 CRC64;
     MGSFTKEEFD CHILDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDVLK KHLRWLKALP
     RVTPFYAVKC NDSRAIVSTL AAIGTGFDCA SKTEIQLVQG LGVPPERIIY ANPCKQVSQI
     KYAASNGVQM MTFDSEIELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLKTSRLL
     LERAKELNID VIGVSFHVGS GCTDPETFVQ AVSDARCVFD MGTEVGFSMY LLDIGGGFPG
     SEDTKLKFEE ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKTVWKEQ
     TGSDDEDESN EQTLMYYVND GVYGSFNCIL YDHAHVKALL QKRPKPDEKY YSSSIWGPTC
     DGLDRIVERC SLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPNIYYVMS RSMWQLMKQI
     QSHGFPPEVE EQDVGTLPMS CAQESGMDRH PAACASASIN V