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P09057 (DCOR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ornithine decarboxylase

Short name=ODC
EC=4.1.1.17
Gene names
Name:Odc1
Synonyms:Odc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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_0000149894

Sites

Active site3601Proton donor; shared with dimeric partner By similarity

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
P09057 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: CEF9D268DDDE0DA6

FASTA46151,047
        10         20         30         40         50         60 
MGSFTKEEFD CHILDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDVLK KHLRWLKALP 

        70         80         90        100        110        120 
RVTPFYAVKC NDSRAIVSTL AAIGTGFDCA SKTEIQLVQG LGVPPERIIY ANPCKQVSQI 

       130        140        150        160        170        180 
KYAASNGVQM MTFDSEIELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLKTSRLL 

       190        200        210        220        230        240 
LERAKELNID VIGVSFHVGS GCTDPETFVQ AVSDARCVFD MGTEVGFSMY LLDIGGGFPG 

       250        260        270        280        290        300 
SEDTKLKFEE ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKTVWKEQ 

       310        320        330        340        350        360 
TGSDDEDESN EQTLMYYVND GVYGSFNCIL YDHAHVKALL QKRPKPDEKY YSSSIWGPTC 

       370        380        390        400        410        420 
DGLDRIVERC SLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPNIYYVMS RSMWQLMKQI 

       430        440        450        460 
QSHGFPPEVE EQDVGTLPMS CAQESGMDRH PAACASASIN V 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of rat ornithine decarboxylase cDNA."
van Kranen H.J., van de Zande L., van Kreijl C.F., Bisschop A., Wieringa B.
Gene 60:145-155(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of the rat ornithine decarboxylase gene."
van Steeg H., van Oostrom C.T.M., van Kranen H.J., van Kreijl C.F.
Nucleic Acids Res. 16:8173-8174(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Wistar.
Tissue: Liver.
[3]"Rat ornithine decarboxylase gene. Nucleotide sequence, potential regulatory elements, and comparison to the mouse gene."
Wen L., Huang J.K., Blackshear P.J.
J. Biol. Chem. 264:9016-9021(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: Fischer.
Tissue: Liver.
[4]"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].
Tissue: Testis.
[5]"The translation in vitro of rat ornithine decarboxylase mRNA is blocked by its 5' untranslated region in a polyamine-independent way."
Van Steeg H., Van Oostrom C.T.M., Hodemaekers H.M., Peters L., Thomas A.A.
Biochem. J. 274:521-526(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-37.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16982 mRNA. Translation: AAA41737.1.
X07944 Genomic DNA. Translation: CAA30765.1.
J04792 Genomic DNA. Translation: AAA66286.1. Sequence problems.
J04791 mRNA. Translation: AAA66164.1.
BC078882 mRNA. Translation: AAH78882.1.
IPIIPI00211162.
PIRDCRTO. A27361.
RefSeqNP_036747.1. NM_012615.2.
UniGeneRn.874.

3D structure databases

ProteinModelPortalP09057.
SMRP09057. Positions 7-421.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000007259.

PTM databases

PhosphoSiteP09057.

Proteomic databases

PaxDbP09057.
PRIDEP09057.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000007259; ENSRNOP00000007259; ENSRNOG00000005424.
GeneID24609.
KEGGrno:24609.

Organism-specific databases

CTD4953.
RGD3227. Odc1.

Phylogenomic databases

eggNOGCOG0019.
GeneTreeENSGT00390000011560.
HOGENOMHOG000274133.
HOVERGENHBG005456.
InParanoidP09057.
KOK01581.
OMAFSFYGPT.
OrthoDBEOG4ZGPC6.

Enzyme and pathway databases

SABIO-RKP09057.
UniPathwayUPA00535; UER00288.

Gene expression databases

GenevestigatorP09057.
GermOnlineENSRNOG00000005424. Rattus norvegicus.

Family and domain databases

Gene3D2.40.37.10. 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.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP09057.
ChEMBLCHEMBL3511.
NextBio603832.

Entry information

Entry nameDCOR_RAT
AccessionPrimary (citable) accession number: P09057
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: April 3, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families