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P00860

- DCOR_MOUSE

UniProt

P00860 - DCOR_MOUSE

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Protein

Ornithine decarboxylase

Gene

Odc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Key enzyme of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine.2 Publications

Catalytic activityi

L-ornithine = putrescine + CO2.

Cofactori

Pyridoxal phosphate.

Enzyme regulationi

Inhibited by S-nitrosylation. Inhibited by antizyme OAZ1, OAZ2 and OAZ3 (By similarity).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei360 – 3601Proton donor; shared with dimeric partner2 Publications

GO - Molecular functioni

  1. ornithine decarboxylase activity Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. kidney development Source: MGI
  2. positive regulation of cell proliferation Source: MGI
  3. putrescine biosynthetic process from ornithine Source: UniProtKB
  4. regulation of protein catabolic process Source: UniProtKB
  5. response to virus Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi4.1.1.17. 3474.
UniPathwayiUPA00535; UER00288.

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine decarboxylase (EC:4.1.1.17)
Short name:
ODC
Gene namesi
Name:Odc1
Synonyms:Odc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:97402. Odc1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: MGI
  3. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi387 – 3871G → A: Partial loss of activity. 1 Publication
Mutagenesisi387 – 3871G → C, D, E, F, H, I, K, L, M, N, P, Q, R, S, T, V, W or Y: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Ornithine decarboxylasePRO_0000149892Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691N6-(pyridoxal phosphate)lysine
Modified residuei303 – 3031Phosphoserine; by CK21 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00860.
PRIDEiP00860.

PTM databases

PhosphoSiteiP00860.

Expressioni

Tissue specificityi

Expressed during testis development in the outer part of the seminiferous tubules.1 Publication

Gene expression databases

BgeeiP00860.
CleanExiMM_ODC1.
GenevestigatoriP00860.

Interactioni

Subunit structurei

Monomer. Homodimer. Does not form an heterodimer with AZIN2.1 Publication

Protein-protein interaction databases

IntActiP00860. 1 interaction.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64
Beta strandi9 – 146
Helixi20 – 289
Beta strandi40 – 445
Helixi45 – 5814
Beta strandi62 – 676
Helixi68 – 703
Helixi74 – 8310
Beta strandi86 – 894
Helixi92 – 1009
Helixi105 – 1073
Beta strandi108 – 1103
Helixi117 – 1259
Beta strandi130 – 1334
Helixi136 – 14510
Beta strandi150 – 1556
Helixi174 – 18613
Beta strandi190 – 1956
Helixi206 – 22520
Beta strandi231 – 2333
Beta strandi241 – 2466
Helixi248 – 26215
Helixi265 – 2673
Beta strandi270 – 2734
Helixi277 – 2804
Helixi281 – 2833
Beta strandi284 – 29613
Beta strandi313 – 3197
Turni322 – 3265
Helixi327 – 3315
Beta strandi339 – 3424
Beta strandi350 – 3567
Beta strandi358 – 3603
Beta strandi365 – 3739
Beta strandi380 – 3834
Beta strandi388 – 3903
Helixi391 – 3933
Helixi397 – 3993
Beta strandi404 – 4107
Helixi411 – 4177

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
7ODCX-ray1.60A1-424[»]
ProteinModelPortaliP00860.
SMRiP00860. Positions 2-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00860.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0019.
GeneTreeiENSGT00390000011560.
HOGENOMiHOG000274133.
HOVERGENiHBG005456.
InParanoidiP00860.
KOiK01581.
OMAiTIHYVMS.
OrthoDBiEOG73Z2T6.
TreeFamiTF300760.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. 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]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00860-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSFTKDEFD CHILDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK
60 70 80 90 100
KHLRWLKALP RVTPFYAVKC NDSRAIVSTL AAIGTGFDCA SKTEIQLVQG
110 120 130 140 150
LGVPAERVIY ANPCKQVSQI KYAASNGVQM MTFDSEIELM KVARAHPKAK
160 170 180 190 200
LVLRIATDDS KAVCRLSVKF GATLKTSRLL LERAKELNID VIGVSFHVGS
210 220 230 240 250
GCTDPETFVQ AVSDARCVFD MATEVGFSMH LLDIGGGFPG SEDTKLKFEE
260 270 280 290 300
ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKTVWKEQ
310 320 330 340 350
PGSDDEDESN EQTFMYYVND GVYGSFNCIL YDHAHVKALL QKRPKPDEKY
360 370 380 390 400
YSSSIWGPTC DGLDRIVERC NLPEMHVGDW MLFENMGAYT VAAASTFNGF
410 420 430 440 450
QRPNIYYVMS RPMWQLMKQI QSHGFPPEVE EQDDGTLPMS CAQESGMDRH
460
PAACASARIN V
Length:461
Mass (Da):51,177
Last modified:July 27, 2011 - v2
Checksum:iB581753F57AC0A30
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781R → W in AAA39846. (PubMed:3456155)Curated
Sequence conflicti206 – 2061E → D in AAA51638. (PubMed:2982844)Curated
Sequence conflicti206 – 2061E → D in AAA39845. (PubMed:3856848)Curated
Sequence conflicti206 – 2061E → D in CAA30301. (PubMed:3362685)Curated
Sequence conflicti206 – 2061E → D in AAA39849. (PubMed:3372502)Curated
Sequence conflicti206 – 2061E → D in AAB27809. (PubMed:8350350)Curated
Sequence conflicti350 – 3501Y → H in AAA39848. (PubMed:3456155)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS25829.1.
PIRiA01077. DCMSO.
I56477.
RefSeqiNP_038642.2. NM_013614.2.
UniGeneiMm.34102.
Mm.472891.

Genome annotation databases

EnsembliENSMUST00000171737; ENSMUSP00000128661; ENSMUSG00000011179.
GeneIDi18263.
KEGGimmu:18263.
UCSCiuc007ncv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS25829.1.
PIRi A01077. DCMSO.
I56477.
RefSeqi NP_038642.2. NM_013614.2.
UniGenei Mm.34102.
Mm.472891.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
7ODC X-ray 1.60 A 1-424 [» ]
ProteinModelPortali P00860.
SMRi P00860. Positions 2-418.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00860. 1 interaction.

Chemistry

ChEMBLi CHEMBL2840.

PTM databases

PhosphoSitei P00860.

Proteomic databases

MaxQBi P00860.
PRIDEi P00860.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000171737 ; ENSMUSP00000128661 ; ENSMUSG00000011179 .
GeneIDi 18263.
KEGGi mmu:18263.
UCSCi uc007ncv.1. mouse.

Organism-specific databases

CTDi 4953.
MGIi MGI:97402. Odc1.

Phylogenomic databases

eggNOGi COG0019.
GeneTreei ENSGT00390000011560.
HOGENOMi HOG000274133.
HOVERGENi HBG005456.
InParanoidi P00860.
KOi K01581.
OMAi TIHYVMS.
OrthoDBi EOG73Z2T6.
TreeFami TF300760.

Enzyme and pathway databases

UniPathwayi UPA00535 ; UER00288 .
BRENDAi 4.1.1.17. 3474.

Miscellaneous databases

EvolutionaryTracei P00860.
NextBioi 293712.
PROi P00860.
SOURCEi Search...

Gene expression databases

Bgeei P00860.
CleanExi MM_ODC1.
Genevestigatori P00860.

Family and domain databases

Gene3Di 2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProi 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.
IPR029066. PLP-binding_barrel.
[Graphical view ]
Pfami PF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view ]
PRINTSi PR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMi SSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEi PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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 AT 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. "Expression of antizyme inhibitor 2 in male haploid germinal cells suggests a role in spermiogenesis."
    Lopez-Contreras A.J., Ramos-Molina B., Martinez-de-la-Torre M., Penafiel-Verdu C., Puelles L., Cremades A., Penafiel R.
    Int. J. Biochem. Cell Biol. 41:1070-1078(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  16. "Structural and degradative aspects of ornithine decarboxylase antizyme inhibitor 2."
    Ramos-Molina B., Lambertos A., Lopez-Contreras A.J., Kasprzak J.M., Czerwoniec A., Bujnicki J.M., Cremades A., Penafiel R.
    FEBS Open Bio 4:510-521(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  17. "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).

Entry informationi

Entry nameiDCOR_MOUSE
AccessioniPrimary (citable) accession number: P00860
Secondary accession number(s): Q61997, Q61998, Q6PB87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3