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P00860 (DCOR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ornithine decarboxylase

Short name=ODC
EC=4.1.1.17
Gene names
Name:Odc1
Synonyms:Odc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Ornithine decarboxylase
PRO_0000149892

Sites

Active site3601Proton donor; shared with dimeric partner Ref.12 Ref.13

Amino acid modifications

Modified residue691N6-(pyridoxal phosphate)lysine
Modified residue3031Phosphoserine; by CK2

Experimental info

Mutagenesis3871G → A: Partial loss of activity. Ref.14
Mutagenesis3871G → 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 conflict1781R → W in AAA39846. Ref.10
Sequence conflict2061E → D in AAA51638. Ref.1
Sequence conflict2061E → D in AAA39845. Ref.2
Sequence conflict2061E → D in CAA30301. Ref.3
Sequence conflict2061E → D in AAA39849. Ref.4
Sequence conflict2061E → D in AAB27809. Ref.5
Sequence conflict3501Y → H in AAA39848. Ref.10

Secondary structure

......................................................................... 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00860 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: B581753F57AC0A30

FASTA46151,177
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION SER-303 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
CCDSCCDS25829.1.
PIRDCMSO. A01077.
I56477.
RefSeqNP_038642.2. NM_013614.2.
UniGeneMm.34102.
Mm.472891.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
7ODCX-ray1.60A1-424[»]
ProteinModelPortalP00860.
SMRP00860. Positions 2-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00860. 1 interaction.

Chemistry

ChEMBLCHEMBL2840.

PTM databases

PhosphoSiteP00860.

Proteomic databases

PRIDEP00860.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000171737; ENSMUSP00000128661; ENSMUSG00000011179.
GeneID18263.
KEGGmmu:18263.
UCSCuc007ncv.1. mouse.

Organism-specific databases

CTD4953.
MGIMGI:97402. Odc1.

Phylogenomic databases

eggNOGCOG0019.
GeneTreeENSGT00390000011560.
HOGENOMHOG000274133.
HOVERGENHBG005456.
InParanoidQ6PB87.
KOK01581.
OMATIHYVMS.
OrthoDBEOG73Z2T6.
TreeFamTF300760.

Enzyme and pathway databases

BRENDA4.1.1.17. 3474.
UniPathwayUPA00535; UER00288.

Gene expression databases

BgeeP00860.
CleanExMM_ODC1.
GenevestigatorP00860.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProIPR009006. 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.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00860.
NextBio293712.
PROP00860.
SOURCESearch...

Entry information

Entry nameDCOR_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot