P00860 (DCOR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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 › Mus

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-ornithine = putrescine + CO2.
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 Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	kidney development Inferred from mutant phenotype. Source: MGI polyamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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 Ref.12 Ref.13

Amino acid modifications

Modified residue

69

1

N6-(pyridoxal phosphate)lysine

Modified residue

303

1

Phosphoserine; by CK2

Experimental info

Mutagenesis

387

1

G → A: Partial loss of activity. Ref.14

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. Ref.14

Sequence conflict

178

1

R → W in AAA39846. Ref.10

Sequence conflict

206

1

E → D in AAA51638. Ref.1

Sequence conflict

206

1

E → D in AAA39845. Ref.2

Sequence conflict

206

1

E → D in CAA30301. Ref.3

Sequence conflict

206

1

E → D in AAA39849. Ref.4

Sequence conflict

206

1

E → D in AAB27809. Ref.5

Sequence conflict

350

1

Y → H in AAA39848. Ref.10

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 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: B581753F57AC0A30	FASTA	461	51,177
	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 GCTDPETFVQ 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"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].
[3]	"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.
[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 [MRNA].
[6]	Yu Y., Luo X. Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Kunming.
[7]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Egg.
[8]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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]. Strain: C57BL/6. Tissue: Brain and Embryo.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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

EMBL
GenBank
DDBJ

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.
EU684749 mRNA. Translation: ACD81645.1.
AK139610 mRNA. Translation: BAE24082.1.
CH466582 Genomic DNA. Translation: EDK98494.1.
BC059826 mRNA. Translation: AAH59826.1.
BC083122 mRNA. Translation: AAH83122.1.
M12330 mRNA. Translation: AAA39846.1.
M12331 mRNA. Translation: AAA39848.1.

IPI

IPI00135743.

PIR

DCMSO. A01077.
I56477.

RefSeq

NP_038642.2. NM_013614.2.

UniGene

Mm.34102.
Mm.472891.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P00860.

SMR

P00860. Positions 2-418.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00860. 1 interaction.

STRING

P00860.

PTM databases

PhosphoSite

P00860.

Proteomic databases

PRIDE

P00860.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000171737; ENSMUSP00000128661; ENSMUSG00000011179.

GeneID

18263.

KEGG

mmu:18263.

NMPDR

fig|10090.3.peg.25991.

Organism-specific databases

CTD

4953.

MGI

MGI:97402. Odc1.

Phylogenomic databases

eggNOG

roNOG04260.

HOGENOM

HBG672375.

HOVERGEN

HBG005456.

InParanoid

P00860.

OrthoDB

EOG4ZGPC6.

PhylomeDB

P00860.

Enzyme and pathway databases

BRENDA

4.1.1.17. 3474.

Gene expression databases

ArrayExpress

P00860.

Bgee

P00860.

CleanEx

MM_ODC1.

Genevestigator

P00860.

GermOnline

ENSMUSG00000011179. Mus musculus.

Family and domain databases

InterPro

IPR009006. Ala_racemase/Decarboxylase_C.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR002433. Orn_de-COase.
[Graphical view]

Gene3D

G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 1 hit.

KO

K01581.

Pfam

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

PRINTS

PR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.

SUPFAM

SSF50621. Racem_decarbox_C. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

DCOR_MOUSE

Accession

Primary (citable) accession number: P00860
Secondary accession number(s): Q61997, Q61998, Q6PB87

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program