Reviewed, UniProtKB/Swiss-Prot P00860 (DCOR_MOUSE)

Names and origin

Protein names

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

Gene names

Name:	Odc1
Synonyms:	Odc

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

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

General annotation (Comments)

Catalytic activity	L-ornithine = putrescine + CO(2).
Cofactor	Pyridoxal phosphate.
Pathway	Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the Orn/Lys/Arg decarboxylase class-II family.

Ontologies

Keywords
Biological process	Polyamine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	kidney development Inferred from mutant phenotype. Source: MGI polyamine biosynthetic process Inferred from electronic annotation. Source: InterPro positive regulation of cell proliferation Inferred from mutant phenotype. Source: MGI
Cellular component	cytosol Inferred from direct assay. Source: MGI
Molecular function	ornithine decarboxylase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 461

461

Ornithine decarboxylase

PRO_0000149892

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

Experimental info

Mutagenesis

387

1

G → A: Partial loss of activity

Mutagenesis

387

1

G → C, D, E, F, H, I, K, L, M, N, P, Q, R, S, T, V, W or Y: Loss of activity

Sequence conflict

178

1

R → W in AAA39846. Ref.6

Sequence conflict

206

1

D → E in AAA39846. Ref.6

Sequence conflict

350

1

Y → H in AAA39848. Ref.6

Secondary structure

1

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461

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Beta strand

9 – 14

6

Helix

20 – 28

9

Beta strand

40 – 44

5

Helix

45 – 58

14

Beta strand

62 – 67

6

Helix

68 – 70

3

Helix

74 – 83

10

Beta strand

86 – 89

4

Helix

92 – 100

9

Helix

105 – 107

3

Beta strand

108 – 110

3

Helix

117 – 125

9

Beta strand

130 – 133

4

Helix

136 – 145

10

Beta strand

150 – 155

6

Helix

174 – 186

13

Beta strand

190 – 195

6

Helix

206 – 225

20

Beta strand

231 – 233

3

Beta strand

241 – 246

6

Helix

248 – 262

15

Helix

265 – 267

3

Beta strand

270 – 273

4

Helix

277 – 280

4

Helix

281 – 283

3

Beta strand

284 – 296

13

Beta strand

313 – 319

7

Turn

322 – 326

5

Helix

327 – 331

5

Beta strand

339 – 342

4

Beta strand

350 – 356

7

Beta strand

358 – 360

3

Beta strand

365 – 373

9

Beta strand

380 – 383

4

Beta strand

388 – 390

3

Helix

391 – 393

3

Helix

397 – 399

3

Beta strand

404 – 410

7

Helix

411 – 417

7

Sequences

	Sequence		Length	Mass (Da)
	P00860-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: DEF1753FA2AC0A30	FASTA	461	51,163
	10 20 30 40 50 60 MSSFTKDEFD CHILDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK KHLRWLKALP 70 80 90 100 110 120 RVTPFYAVKC NDSRAIVSTL AAIGTGFDCA SKTEIQLVQG LGVPAERVIY ANPCKQVSQI 130 140 150 160 170 180 KYAASNGVQM MTFDSEIELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLKTSRLL 190 200 210 220 230 240 LERAKELNID VIGVSFHVGS GCTDPDTFVQ AVSDARCVFD MATEVGFSMH LLDIGGGFPG 250 260 270 280 290 300 SEDTKLKFEE ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKTVWKEQ 310 320 330 340 350 360 PGSDDEDESN EQTFMYYVND GVYGSFNCIL YDHAHVKALL QKRPKPDEKY YSSSIWGPTC 370 380 390 400 410 420 DGLDRIVERC NLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPNIYYVMS RPMWQLMKQI 430 440 450 460 QSHGFPPEVE EQDDGTLPMS CAQESGMDRH PAACASARIN V

References

[1]	"Nucleotide sequence of murine ornithine decarboxylase mRNA." Kahana C., Nathans D. Proc. Natl. Acad. Sci. U.S.A. 82:1673-1677(1985) [PubMed: 3856848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Nucleotide sequence of the mouse ornithine decarboxylase gene." Coffino P., Chen E.L. Nucleic Acids Res. 16:2731-2731(1988) [PubMed: 3362685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c.
[3]	"Mouse ornithine decarboxylase. Complete amino acid sequence deduced from cDNA." Gupta M., Coffino P. J. Biol. Chem. 260:2941-2944(1985) [PubMed: 2982844] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Isolation and characterization of the mouse ornithine decarboxylase gene." Katz A., Kahana C. J. Biol. Chem. 263:7604-7609(1988) [PubMed: 3372502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Domains within the mammalian ornithine decarboxylase messenger RNA have evolved independently and episodically." Johannes G.J., Berger F.G. J. Mol. Evol. 36:555-567(1993) [PubMed: 8350350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[6]	"Two ornithine decarboxylase mRNA species in mouse kidney arise from size heterogeneity at their 3' termini." Hickok N.J., Seppaenen P.J., Kontula K.K., Jaenne P.A., Bardin C.W., Jaenne O.A. Proc. Natl. Acad. Sci. U.S.A. 83:594-598(1986) [PubMed: 3456155] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-461.
[7]	"Mouse ornithine decarboxylase is phosphorylated by casein kinase-II at a predominant single location (serine 303)." Rosenberg-Hasson Y., Strumpf D., Kahana C. Eur. J. Biochem. 197:419-424(1991) [PubMed: 2026163] [Abstract] Cited for: PHOSPHORYLATION BY CKII.
[8]	"Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites." Poulin R., Lu L., Ackermann B., Bey P., Pegg A.E. J. Biol. Chem. 267:150-158(1992) [PubMed: 1730582] [Abstract] Cited for: ACTIVE SITE, PYRIDOXAL PHOSPHATE AT LYS-69.
[9]	"Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants." Tobias K.E., Kahana C. Biochemistry 32:5842-5847(1993) [PubMed: 8504104] [Abstract] Cited for: ACTIVE SITE.
[10]	"Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers." Tobias K.E., Mamroud-Kidron E., Kahana C. Eur. J. Biochem. 218:245-250(1993) [PubMed: 8243470] [Abstract] Cited for: MUTAGENESIS OF GLY-387.
[11]	"Structure of mammalian ornithine decarboxylase at 1.6-A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases." Kern A.D., Oliveira M.A., Coffino P., Hackert M.L. Structure 7:567-581(1999) [PubMed: 10378276] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M20617 mRNA. Translation: AAA51638.1.
M10624 mRNA. Translation: AAA39845.1.
X07392 Genomic DNA. Translation: CAA30301.1.
J03733 Genomic DNA. Translation: AAA39849.1.
S64539 mRNA. Translation: AAB27809.1.
M12330 mRNA. Translation: AAA39846.1.
M12331 mRNA. Translation: AAA39848.1.

PIR

DCMSO. A01077.
I56477.

UniGene

Mm.34102
Mm.437048

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
7ODC	X-ray	1.60	A	1-424	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P00860.

PTM databases

PhosphoSite

P00860.

Genome annotation databases

Ensembl

ENSMUSG00000011179. Mus musculus. [Contig view]

Organism-specific databases

MGI

MGI:97402. Odc1.

Phylogenomic databases

HOGENOM

P00860.

HOVERGEN

P00860.

Gene expression databases

ArrayExpress

P00860.

CleanEx

MM_ODC1.

GermOnline

ENSMUSG00000011179. Mus musculus.

Family and domain databases

InterPro

IPR000183. De-COase2.
IPR002433. Orn_de-COase.
[Graphical view]

Pfam

PF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]

PRINTS

PR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.

PROSITE

PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

DCOR_MOUSE

Accession

Primary (citable) accession number: P00860
Secondary accession number(s): Q61997, Q61998

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 25, 2008
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)