Ornithine decarboxylase - Homo sapiens (Human)

Hide | Top

Names and origin

Protein names

Recommended name:
    Ornithine decarboxylase
      Short name=ODC
    EC=4.1.1.17

Gene names

Name:

ODC1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity	L-ornithine = putrescine + CO(2).
Cofactor	Pyridoxal phosphate.
Enzyme regulation	Inhibited by S-nitrosylation.
Pathway	Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
Subunit structure	Homodimer.
Post-translational modification	S-Nitrosylation inhibits the enzyme. S-Nitrosylated in vitro on 4 cysteine residues.
Sequence similarities	Belongs to the Orn/Lys/Arg decarboxylase class-II family.

Hide | Top

Ontologies

Keywords
Biological process	Polyamine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
PTM	Phosphoprotein S-nitrosylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	polyamine biosynthetic process Non-traceable author statement. Source: UniProtKB
Cellular component	nucleus Inferred from direct assay. Source: HPA
Molecular function	ornithine decarboxylase activity Ref.11 Traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct	Notes
OAZ2	O95190	1	EBI-1044287,EBI-1051861

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 461

461

Ornithine decarboxylase

PRO_0000149891

Sites

Active site

360

1

Proton donor; shared with dimeric partner

Binding site

69

1

Pyridoxal phosphate (covalent)

Amino acid modifications

Modified residue

303

1

Phosphoserine; by CK2 By similarity

Modified residue

360

1

S-nitrosocysteine; in inhibited form Probable

Experimental info

Mutagenesis

360

1

C → A: 25% decrease of in vitro nitrosylation level

Secondary structure

1

.

461

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P11926-1 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 8CCB88CE80E823C5
Show »

FASTA

461

51,148

        10         20         30         40         50         60 
MNNFGNEEFD CHFLDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK KHLRWLKALP 

        70         80         90        100        110        120 
RVTPFYAVKC NDSKAIVKTL AATGTGFDCA SKTEIQLVQS LGVPPERIIY ANPCKQVSQI 

       130        140        150        160        170        180 
KYAANNGVQM MTFDSEVELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLRTSRLL 

       190        200        210        220        230        240 
LERAKELNID VVGVSFHVGS GCTDPETFVQ AISDARCVFD MGAEVGFSMY LLDIGGGFPG 

       250        260        270        280        290        300 
SEDVKLKFEE ITGVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKIVLKEQ 

       310        320        330        340        350        360 
TGSDDEDESS EQTFMYYVND GVYGSFNCIL YDHAHVKPLL QKRPKPDEKY YSSSIWGPTC 

       370        380        390        400        410        420 
DGLDRIVERC DLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPTIYYVMS GPAWQLMQQF 

       430        440        450        460 
QNPDFPPEVE EQDASTLPVS CAWESGMKRH RAACASASIN V

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA." Hickok N.J., Seppaenen P.J., Gunsalus G.L., Jaenne O.A. DNA 6:179-187(1987) [PubMed: 3595418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Jaenne O.A. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 415.
[3]	"Characterization and sequence analysis of the human ornithine decarboxylase gene." Fitzgerald M.C., Flanagan M.A. DNA 8:623-634(1989) [PubMed: 2693021] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Nucleotide sequence of the human ornithine decarboxylase gene." van Steeg H., van Oostrom C.T.M., Martens J.W.M., van Kreyl C.F., Schepens J., Wieringa B. Nucleic Acids Res. 17:8855-8856(1989) [PubMed: 2587220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Human ornithine decarboxylase-encoding loci: nucleotide sequence of the expressed gene and characterization of a pseudogene." Hickok N.J., Wahlfors J., Crozat A., Halmekytoe M., Alhonen L., Jaenne J., Jaenne O.A. Gene 93:257-263(1990) [PubMed: 2227439] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Isolation and expression of a human ornithine decarboxylase gene." Moshier J.A., Gilbert J.D., Skunca M., Dosescu J., Almodovar K.M., Luk G.D. J. Biol. Chem. 265:4884-4892(1990) [PubMed: 2318872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Multiple promoter elements govern expression of the human ornithine decarboxylase gene in colon carcinoma cells." Moshier J.A., Osborne D.L., Skunca M., Dosescu J., Gilbert J.D., Fitzgerald M.C., Polidori G., Wagner R.L., Friezner Degen S.J., Luk G.D., Flanagan M.A. Nucleic Acids Res. 20:2581-2590(1992) [PubMed: 1598217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	"Regulation of ornithine decarboxylase mRNA levels in human breast cancer cells: pattern of expression and involvement of core enhancer promoter element." Wright P.S., Cooper J.R., Cross-Doersen D.E., Miller J.A., Chmielewski P.A., Wagner R.L., Streng K.A., Flanagan M.A. Cell Growth Differ. 6:1097-1102(1995) [PubMed: 8519686] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[9]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[11]	"Expression of human chromosome 2 ornithine decarboxylase gene in ornithine decarboxylase-deficient Chinese hamster ovary cells." Hsieh J.T., Denning M.F., Heidel S.M., Verma A.K. Cancer Res. 50:2239-2244(1990) [PubMed: 2317811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
[12]	"Cell-cycle-dependent expression of human ornithine decarboxylase." Kaczmarek L., Calabretta B., Ferrari S., de Riel J.K. J. Cell. Physiol. 132:545-551(1987) [PubMed: 3308908] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 112-461.
[13]	"Nitric oxide inhibits ornithine decarboxylase by S-nitrosylation." Bauer P.M., Fukuto J.M., Buga G.M., Pegg A.E., Ignarro L.J. Biochem. Biophys. Res. Commun. 262:355-358(1999) [PubMed: 10462479] [Abstract] Cited for: S-NITROSYLATION.
[14]	"Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of cysteine 360 in the active site of the enzyme." Bauer P.M., Buga G.M., Fukuto J.M., Pegg A.E., Ignarro L.J. J. Biol. Chem. 276:34458-34464(2001) [PubMed: 11461922] [Abstract] Cited for: S-NITROSYLATION AT CYS-360, MUTAGENESIS OF CYS-360.
[15]	"Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding." Almrud J.J., Oliveira M.A., Kern A.D., Grishin N.V., Phillips M.A., Hackert M.L. J. Mol. Biol. 295:7-16(2000) [PubMed: 10623504] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+	Additional computationally mapped references.

Hide | Top

Web resources

Wikipedia

Ornithine decarboxylase entry

Hide | Top

Cross-references

Sequence databases

M16650 mRNA. Translation: AAA59966.2.
M31061 Genomic DNA. Translation: AAA60563.1.
X16277 Genomic DNA. Translation: CAA34353.1.
M33764 Genomic DNA. Translation: AAA60564.1.
M34158 Genomic DNA. Translation: AAA59969.1.
M81740 Genomic DNA. Translation: AAA59967.1.
X55362 mRNA. Translation: CAA39047.1.
AY841870 Genomic DNA. Translation: AAV88093.1.
BC025296 mRNA. Translation: AAH25296.1.
X53271 mRNA. Translation: CAA37369.1.
M20372 mRNA. Translation: AAA59968.1.

PIR

DCHUO. S06900.

RefSeq

NP_002530.1.

UniGene

Hs.467701