DCOR_HUMAN
ID DCOR_HUMAN Reviewed; 461 AA.
AC P11926; Q53TU3; Q6LDS9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17 {ECO:0000269|PubMed:17407445};
GN Name=ODC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3595418; DOI=10.1089/dna.1987.6.179;
RA Hickok N.J., Seppaenen P.J., Gunsalus G.L., Jaenne O.A.;
RT "Complete amino acid sequence of human ornithine decarboxylase deduced from
RT complementary DNA.";
RL DNA 6:179-187(1987).
RN [2]
RP SEQUENCE REVISION TO 415.
RA Jaenne O.A.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2693021; DOI=10.1089/dna.1.1989.8.623;
RA Fitzgerald M.C., Flanagan M.A.;
RT "Characterization and sequence analysis of the human ornithine
RT decarboxylase gene.";
RL DNA 8:623-634(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2587220; DOI=10.1093/nar/17.21.8855;
RA van Steeg H., van Oostrom C.T.M., Martens J.W.M., van Kreyl C.F.,
RA Schepens J., Wieringa B.;
RT "Nucleotide sequence of the human ornithine decarboxylase gene.";
RL Nucleic Acids Res. 17:8855-8856(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2227439; DOI=10.1016/0378-1119(90)90233-h;
RA Hickok N.J., Wahlfors J., Crozat A., Halmekytoe M., Alhonen L., Jaenne J.,
RA Jaenne O.A.;
RT "Human ornithine decarboxylase-encoding loci: nucleotide sequence of the
RT expressed gene and characterization of a pseudogene.";
RL Gene 93:257-263(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2318872; DOI=10.1016/s0021-9258(19)34057-8;
RA Moshier J.A., Gilbert J.D., Skunca M., Dosescu J., Almodovar K.M.,
RA Luk G.D.;
RT "Isolation and expression of a human ornithine decarboxylase gene.";
RL J. Biol. Chem. 265:4884-4892(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1598217; DOI=10.1093/nar/20.10.2581;
RA Moshier J.A., Osborne D.L., Skunca M., Dosescu J., Gilbert J.D.,
RA Fitzgerald M.C., Polidori G., Wagner R.L., Friezner Degen S.J., Luk G.D.,
RA Flanagan M.A.;
RT "Multiple promoter elements govern expression of the human ornithine
RT decarboxylase gene in colon carcinoma cells.";
RL Nucleic Acids Res. 20:2581-2590(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8519686;
RA Wright P.S., Cooper J.R., Cross-Doersen D.E., Miller J.A.,
RA Chmielewski P.A., Wagner R.L., Streng K.A., Flanagan M.A.;
RT "Regulation of ornithine decarboxylase mRNA levels in human breast cancer
RT cells: pattern of expression and involvement of core enhancer promoter
RT element.";
RL Cell Growth Differ. 6:1097-1102(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Esophagus, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
RX PubMed=2317811;
RA Hsieh J.T., Denning M.F., Heidel S.M., Verma A.K.;
RT "Expression of human chromosome 2 ornithine decarboxylase gene in ornithine
RT decarboxylase-deficient Chinese hamster ovary cells.";
RL Cancer Res. 50:2239-2244(1990).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 112-461.
RX PubMed=3308908; DOI=10.1002/jcp.1041320318;
RA Kaczmarek L., Calabretta B., Ferrari S., de Riel J.K.;
RT "Cell-cycle-dependent expression of human ornithine decarboxylase.";
RL J. Cell. Physiol. 132:545-551(1987).
RN [16]
RP S-NITROSYLATION.
RX PubMed=10462479; DOI=10.1006/bbrc.1999.1210;
RA Bauer P.M., Fukuto J.M., Buga G.M., Pegg A.E., Ignarro L.J.;
RT "Nitric oxide inhibits ornithine decarboxylase by S-nitrosylation.";
RL Biochem. Biophys. Res. Commun. 262:355-358(1999).
RN [17]
RP S-NITROSYLATION AT CYS-360, AND MUTAGENESIS OF CYS-360.
RX PubMed=11461922; DOI=10.1074/jbc.m105219200;
RA Bauer P.M., Buga G.M., Fukuto J.M., Pegg A.E., Ignarro L.J.;
RT "Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of
RT cysteine 360 in the active site of the enzyme.";
RL J. Biol. Chem. 276:34458-34464(2001).
RN [18]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT differential cellular gene expression in response to enterovirus 71
RT infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [19]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=17900240; DOI=10.1042/bj20071004;
RA Kanerva K., Makitie L.T., Pelander A., Heiskala M., Andersson L.C.;
RT "Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor
RT but not an arginine decarboxylase.";
RL Biochem. J. 409:187-192(2008).
RN [20] {ECO:0007744|PDB:1D7K}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 7-427, AND SUBUNIT.
RX PubMed=10623504; DOI=10.1006/jmbi.1999.3331;
RA Almrud J.J., Oliveira M.A., Kern A.D., Grishin N.V., Phillips M.A.,
RA Hackert M.L.;
RT "Crystal structure of human ornithine decarboxylase at 2.1 A resolution:
RT structural insights to antizyme binding.";
RL J. Mol. Biol. 295:7-16(2000).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH COFACTOR AND
RP SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17407445; DOI=10.1042/bj20070188;
RA Dufe V.T., Ingner D., Heby O., Khomutov A.R., Persson L., Al-Karadaghi S.;
RT "A structural insight into the inhibition of human and Leishmania donovani
RT ornithine decarboxylases by 1-amino-oxy-3-aminopropane.";
RL Biochem. J. 405:261-268(2007).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 2-421 IN COMPLEX WITH COFACTOR
RP AND OAZ1.
RX PubMed=26305948; DOI=10.1073/pnas.1508187112;
RA Wu H.Y., Chen S.F., Hsieh J.Y., Chou F., Wang Y.H., Lin W.T., Lee P.Y.,
RA Yu Y.J., Lin L.Y., Lin T.S., Lin C.L., Liu G.Y., Tzeng S.R., Hung H.C.,
RA Chan N.L.;
RT "Structural basis of antizyme-mediated regulation of polyamine
RT homeostasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11229-11234(2015).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH COFACTOR; OAZ1 AND
RP INHIBITOR.
RX PubMed=26443277; DOI=10.1038/srep14738;
RA Wu D., Kaan H.Y., Zheng X., Tang X., He Y., Vanessa Tan Q., Zhang N.,
RA Song H.;
RT "Structural basis of ornithine decarboxylase inactivation and accelerated
RT degradation by polyamine sensor antizyme1.";
RL Sci. Rep. 5:14738-14738(2015).
RN [24]
RP VARIANT BABS 448-LYS--VAL-461 DEL, INVOLVEMENT IN BABS, AND
RP CHARACTERIZATION OF VARIANT BABS 448-LYS--VAL-461 DEL.
RX PubMed=30239107; DOI=10.1002/ajmg.a.40523;
RA Bupp C.P., Schultz C.R., Uhl K.L., Rajasekaran S., Bachmann A.S.;
RT "Novel de novo pathogenic variant in the ODC1 gene in a girl with
RT developmental delay, alopecia, and dysmorphic features.";
RL Am. J. Med. Genet. A 176:2548-2553(2018).
RN [25]
RP VARIANT BABS 419-GLN--VAL-461 DEL, AND INVOLVEMENT IN BABS.
RX PubMed=30475435; DOI=10.1002/ajmg.a.60677;
RA Rodan L.H., Anyane-Yeboa K., Chong K., Klein Wassink-Ruiter J.S.,
RA Wilson A., Smith L., Kothare S.V., Rajabi F., Blaser S., Ni M.,
RA DeBerardinis R.J., Poduri A., Berry G.T.;
RT "Gain-of-function variants in the ODC1 gene cause a syndromic
RT neurodevelopmental disorder associated with macrocephaly, alopecia,
RT dysmorphic features, and neuroimaging abnormalities.";
RL Am. J. Med. Genet. A 176:2554-2560(2018).
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:0000269|PubMed:17900240}.
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:0000269|PubMed:17407445};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17407445, ECO:0000269|PubMed:26443277};
CC -!- ACTIVITY REGULATION: Inhibited by S-nitrosylation (PubMed:10462479,
CC PubMed:11461922). Inhibited by antizymes (AZs) OAZ1, OAZ2 and OAZ3 in
CC 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 (PubMed:17900240). Inhibited by 1-amino-oxy-3-
CC aminopropane (APA, an isosteric analog of putrescine)
CC (PubMed:17407445). Irreversibly inhibited by alpha-
CC difluoromethylornithine (DFMO) (PubMed:17407445).
CC {ECO:0000269|PubMed:10462479, ECO:0000269|PubMed:11461922,
CC ECO:0000269|PubMed:17407445, ECO:0000269|PubMed:17900240}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.08 mM for L-ornithine {ECO:0000269|PubMed:17407445};
CC Note=kcat is 3.3 sec(-1) with L-ornithine as substrate.
CC {ECO:0000269|PubMed:17407445};
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 (Probable).
CC Does not form a heterodimer with AZIN2 (By similarity).
CC {ECO:0000250|UniProtKB:P00860, ECO:0000305|PubMed:10623504}.
CC -!- INTERACTION:
CC P11926; Q9H8Y8: GORASP2; NbExp=11; IntAct=EBI-1044287, EBI-739467;
CC P11926; Q92993: KAT5; NbExp=6; IntAct=EBI-1044287, EBI-399080;
CC P11926; Q9UMX2: OAZ3; NbExp=5; IntAct=EBI-1044287, EBI-10281601;
CC P11926; Q9UMX2-2: OAZ3; NbExp=3; IntAct=EBI-1044287, EBI-12049527;
CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC infection (at protein level). {ECO:0000269|PubMed:16548883}.
CC -!- PTM: S-Nitrosylation inhibits the enzyme. S-Nitrosylated in vitro on 4
CC cysteine residues. {ECO:0000269|PubMed:10462479,
CC ECO:0000269|PubMed:11461922}.
CC -!- DISEASE: Bachmann-Bupp syndrome (BABS) [MIM:619075]: An autosomal
CC dominant disorder characterized by global developmental delay,
CC alopecia, absolute or relative macrocephaly, and facial dysmorphism.
CC Neuroimaging shows white matter abnormalities, prominent Virchow-Robin
CC spaces, periventricular cysts, and abnormalities of the corpus
CC callosum. {ECO:0000269|PubMed:30239107, ECO:0000269|PubMed:30475435}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry. BABS is due to truncating variants that lead to a gain
CC of function. This phenomenon apparently results from truncation
CC proximal to or involving the C-terminal region of ODC1 protein, distal
CC enough to allow escape from nonsense-mediated decay. A gain of function
CC is corroborated by elevated plasma levels of N-acetylputrescine, with
CC otherwise normal polyamine levels, in affected individuals.
CC {ECO:0000269|PubMed:30475435}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/odc1/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ornithine decarboxylase entry;
CC URL="https://en.wikipedia.org/wiki/Ornithine_decarboxylase";
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DR EMBL; M16650; AAA59966.2; -; mRNA.
DR EMBL; M31061; AAA60563.1; -; Genomic_DNA.
DR EMBL; X16277; CAA34353.1; -; Genomic_DNA.
DR EMBL; M33764; AAA60564.1; -; Genomic_DNA.
DR EMBL; M34158; AAA59969.1; -; Genomic_DNA.
DR EMBL; M81740; AAA59967.1; -; Genomic_DNA.
DR EMBL; X55362; CAA39047.1; -; mRNA.
DR EMBL; AK292352; BAF85041.1; -; mRNA.
DR EMBL; AK312766; BAG35632.1; -; mRNA.
DR EMBL; AY841870; AAV88093.1; -; Genomic_DNA.
DR EMBL; AC007249; AAY15034.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00958.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00959.1; -; Genomic_DNA.
DR EMBL; BC025296; AAH25296.1; -; mRNA.
DR EMBL; X53271; CAA37369.1; -; mRNA.
DR EMBL; M20372; AAA59968.1; -; mRNA.
DR CCDS; CCDS1672.1; -.
DR PIR; S06900; DCHUO.
DR RefSeq; NP_001274118.1; NM_001287189.1.
DR RefSeq; NP_001274119.1; NM_001287190.1.
DR RefSeq; NP_002530.1; NM_002539.2.
DR PDB; 1D7K; X-ray; 2.10 A; A/B=7-427.
DR PDB; 2ON3; X-ray; 3.00 A; A/B=1-461.
DR PDB; 2OO0; X-ray; 1.90 A; A/B=1-461.
DR PDB; 4ZGY; X-ray; 2.63 A; A=2-421.
DR PDB; 5BWA; X-ray; 3.20 A; A=1-461.
DR PDB; 7S3F; X-ray; 2.49 A; A/B=1-424.
DR PDB; 7S3G; X-ray; 1.66 A; A/B=1-424.
DR PDBsum; 1D7K; -.
DR PDBsum; 2ON3; -.
DR PDBsum; 2OO0; -.
DR PDBsum; 4ZGY; -.
DR PDBsum; 5BWA; -.
DR PDBsum; 7S3F; -.
DR PDBsum; 7S3G; -.
DR AlphaFoldDB; P11926; -.
DR SMR; P11926; -.
DR BioGRID; 111007; 22.
DR CORUM; P11926; -.
DR IntAct; P11926; 17.
DR MINT; P11926; -.
DR STRING; 9606.ENSP00000234111; -.
DR BindingDB; P11926; -.
DR ChEMBL; CHEMBL1869; -.
DR DrugBank; DB06243; Eflornithine.
DR DrugBank; DB04263; Geneticin.
DR DrugBank; DB03856; L-Eflornithine.
DR DrugBank; DB04083; N(6)-(pyridoxal phosphate)-L-lysine.
DR DrugBank; DB02824; N-Pyridoxyl-Glycine-5-Monophosphate.
DR DrugBank; DB01917; Putrescine.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugBank; DB02209; Pyridoxine phosphate.
DR DrugBank; DB00127; Spermine.
DR DrugCentral; P11926; -.
DR GuidetoPHARMACOLOGY; 1276; -.
DR iPTMnet; P11926; -.
DR PhosphoSitePlus; P11926; -.
DR BioMuta; ODC1; -.
DR DMDM; 118377; -.
DR EPD; P11926; -.
DR jPOST; P11926; -.
DR MassIVE; P11926; -.
DR PaxDb; P11926; -.
DR PeptideAtlas; P11926; -.
DR PRIDE; P11926; -.
DR ProteomicsDB; 52813; -.
DR Antibodypedia; 781; 905 antibodies from 34 providers.
DR CPTC; P11926; 3 antibodies.
DR DNASU; 4953; -.
DR Ensembl; ENST00000234111.9; ENSP00000234111.4; ENSG00000115758.13.
DR Ensembl; ENST00000405333.5; ENSP00000385333.1; ENSG00000115758.13.
DR GeneID; 4953; -.
DR KEGG; hsa:4953; -.
DR MANE-Select; ENST00000234111.9; ENSP00000234111.4; NM_002539.3; NP_002530.1.
DR UCSC; uc002rao.3; human.
DR CTD; 4953; -.
DR DisGeNET; 4953; -.
DR GeneCards; ODC1; -.
DR HGNC; HGNC:8109; ODC1.
DR HPA; ENSG00000115758; Low tissue specificity.
DR MalaCards; ODC1; -.
DR MIM; 165640; gene.
DR MIM; 619075; phenotype.
DR neXtProt; NX_P11926; -.
DR OpenTargets; ENSG00000115758; -.
DR Orphanet; 544488; Global developmental delay-alopecia-macrocephaly-facial dysmorphism-structural brain anomalies syndrome.
DR PharmGKB; PA31897; -.
DR VEuPathDB; HostDB:ENSG00000115758; -.
DR eggNOG; KOG0622; Eukaryota.
DR GeneTree; ENSGT00950000182995; -.
DR HOGENOM; CLU_026444_1_1_1; -.
DR InParanoid; P11926; -.
DR OMA; YCRSMAS; -.
DR OrthoDB; 725914at2759; -.
DR PhylomeDB; P11926; -.
DR TreeFam; TF300760; -.
DR BioCyc; MetaCyc:HS03935-MON; -.
DR BRENDA; 4.1.1.17; 2681.
DR PathwayCommons; P11926; -.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-351202; Metabolism of polyamines.
DR SABIO-RK; P11926; -.
DR SignaLink; P11926; -.
DR SIGNOR; P11926; -.
DR UniPathway; UPA00535; UER00288.
DR BioGRID-ORCS; 4953; 21 hits in 1088 CRISPR screens.
DR ChiTaRS; ODC1; human.
DR EvolutionaryTrace; P11926; -.
DR GeneWiki; ODC1; -.
DR GenomeRNAi; 4953; -.
DR Pharos; P11926; Tclin.
DR PRO; PR:P11926; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P11926; protein.
DR Bgee; ENSG00000115758; Expressed in secondary oocyte and 205 other tissues.
DR ExpressionAtlas; P11926; baseline and differential.
DR Genevisible; P11926; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IDA:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0006595; P:polyamine metabolic process; TAS:Reactome.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
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; IEP:UniProtKB.
DR DisProt; DP02673; -.
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 3D-structure; Decarboxylase; Disease variant; Hypotrichosis; Lyase;
KW Phosphoprotein; Polyamine biosynthesis; Pyridoxal phosphate;
KW Reference proteome; S-nitrosylation.
FT CHAIN 1..461
FT /note="Ornithine decarboxylase"
FT /id="PRO_0000149891"
FT ACT_SITE 360
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000305|PubMed:10623504"
FT BINDING 200
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17407445,
FT ECO:0007744|PDB:2OO0"
FT BINDING 237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17407445,
FT ECO:0007744|PDB:2OO0"
FT BINDING 274..277
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17407445,
FT ECO:0000269|PubMed:26305948, ECO:0000269|PubMed:26443277,
FT ECO:0007744|PDB:2OO0"
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:0000269|PubMed:17407445,
FT ECO:0000269|PubMed:26305948, ECO:0000269|PubMed:26443277,
FT ECO:0007744|PDB:2OO0"
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:0000269|PubMed:26305948,
FT ECO:0000305|PubMed:17407445"
FT MOD_RES 303
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 360
FT /note="S-nitrosocysteine; in inhibited form"
FT /evidence="ECO:0000305|PubMed:11461922"
FT VARIANT 419..461
FT /note="Missing (in BABS)"
FT /evidence="ECO:0000269|PubMed:30475435"
FT /id="VAR_085000"
FT VARIANT 448..461
FT /note="Missing (in BABS; gain-of-function variant resulting
FT in increased putrescine biosynthesis as indicated by higher
FT amount of putrescine in patient red blood cells compared to
FT controls; increased ODC1 protein levels in patient red
FT blood cells)"
FT /evidence="ECO:0000269|PubMed:30239107"
FT /id="VAR_085001"
FT MUTAGEN 360
FT /note="C->A: 25% decrease of in vitro nitrosylation level."
FT /evidence="ECO:0000269|PubMed:11461922"
FT HELIX 1..5
FT /evidence="ECO:0007829|PDB:2OO0"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:7S3G"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2OO0"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:2OO0"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 206..225
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 248..262
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 284..297
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:7S3G"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:2OO0"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 365..373
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:7S3G"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:7S3G"
FT HELIX 411..421
FT /evidence="ECO:0007829|PDB:7S3G"
SQ SEQUENCE 461 AA; 51148 MW; 8CCB88CE80E823C5 CRC64;
MNNFGNEEFD CHFLDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK KHLRWLKALP
RVTPFYAVKC NDSKAIVKTL AATGTGFDCA SKTEIQLVQS LGVPPERIIY ANPCKQVSQI
KYAANNGVQM MTFDSEVELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLRTSRLL
LERAKELNID VVGVSFHVGS GCTDPETFVQ AISDARCVFD MGAEVGFSMY LLDIGGGFPG
SEDVKLKFEE ITGVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKIVLKEQ
TGSDDEDESS EQTFMYYVND GVYGSFNCIL YDHAHVKPLL QKRPKPDEKY YSSSIWGPTC
DGLDRIVERC DLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPTIYYVMS GPAWQLMQQF
QNPDFPPEVE EQDASTLPVS CAWESGMKRH RAACASASIN V
