P11926 (DCOR_HUMAN) 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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.
Enzyme regulation	Inhibited by S-nitrosylation.
Pathway	Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
Subunit structure	Homodimer.
Induction	Down-regulated in response to enterovirus 71 (EV71) infection (at protein level). Ref.18
Post-translational modification	S-Nitrosylation inhibits the enzyme. S-Nitrosylated in vitro on 4 cysteine residues.
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 S-nitrosylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	kidney development Inferred from electronic annotation. Source: Compara polyamine biosynthetic process Non-traceable author statement. Source: UniProtKB positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara putrescine biosynthetic process from ornithine Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of cellular amino acid metabolic process Traceable author statement. Source: Reactome response to virus Inferred from expression pattern Ref.18. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ornithine decarboxylase activity Traceable author statement Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
OAZ2	O95190	1	EBI-1044287,EBI-1051861

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 461

461

Ornithine decarboxylase

PRO_0000149891

Sites

Active site

360

1

Proton donor; shared with dimeric partner

Amino acid modifications

Modified residue

69

1

N6-(pyridoxal phosphate)lysine

Modified residue

303

1

Phosphoserine; by CK2 By similarity

Modified residue

360

1

S-nitrosocysteine; in inhibited form Probable

Experimental info

Mutagenesis

360

1

C → A: 25% decrease of in vitro nitrosylation level. Ref.17

Secondary structure

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461

Helix Strand Turn

Details...

Helix

1 – 5

5

Turn

6 – 8

3

Beta strand

11 – 14

4

Helix

20 – 30

11

Turn

31 – 33

3

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

Beta strand

162 – 164

3

Turn

167 – 169

3

Helix

174 – 186

13

Beta strand

190 – 195

6

Helix

206 – 225

20

Beta strand

231 – 233

3

Beta strand

240 – 246

7

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 – 324

3

Helix

325 – 327

3

Helix

328 – 331

4

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 – 420

10

Sequences

	Sequence		Length	Mass (Da)
	P11926 [UniParc]. Last modified April 1, 1990. Version 2. Checksum: 8CCB88CE80E823C5	FASTA	461	51,148
	10 20 30 40 50 60 MNNFGNEEFD CHFLDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK KHLRWLKALP 70 80 90 100 110 120 RVTPFYAVKC NDSKAIVKTL AATGTGFDCA SKTEIQLVQS LGVPPERIIY ANPCKQVSQI 130 140 150 160 170 180 KYAANNGVQM MTFDSEVELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLRTSRLL 190 200 210 220 230 240 LERAKELNID VVGVSFHVGS GCTDPETFVQ AISDARCVFD MGAEVGFSMY LLDIGGGFPG 250 260 270 280 290 300 SEDVKLKFEE ITGVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKIVLKEQ 310 320 330 340 350 360 TGSDDEDESS EQTFMYYVND GVYGSFNCIL YDHAHVKPLL QKRPKPDEKY YSSSIWGPTC 370 380 390 400 410 420 DGLDRIVERC DLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPTIYYVMS GPAWQLMQQF 430 440 450 460 QNPDFPPEVE EQDASTLPVS CAWESGMKRH RAACASASIN V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA." Hickok N.J., Seppaenen P.J., Gunsalus G.L., Jaenne O.A. DNA 6:179-187(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Jaenne O.A. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 415.
[3]	"Characterization and sequence analysis of the human ornithine decarboxylase gene." Fitzgerald M.C., Flanagan M.A. DNA 8:623-634(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Nucleotide sequence of the human ornithine decarboxylase gene." van Steeg H., van Oostrom C.T.M., Martens J.W.M., van Kreyl C.F., Schepens J., Wieringa B. Nucleic Acids Res. 17:8855-8856(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Human ornithine decarboxylase-encoding loci: nucleotide sequence of the expressed gene and characterization of a pseudogene." Hickok N.J., Wahlfors J., Crozat A., Halmekytoe M., Alhonen L., Jaenne J., Jaenne O.A. Gene 93:257-263(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Isolation and expression of a human ornithine decarboxylase gene." Moshier J.A., Gilbert J.D., Skunca M., Dosescu J., Almodovar K.M., Luk G.D. J. Biol. Chem. 265:4884-4892(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Multiple promoter elements govern expression of the human ornithine decarboxylase gene in colon carcinoma cells." Moshier J.A., Osborne D.L., Skunca M., Dosescu J., Gilbert J.D., Fitzgerald M.C., Polidori G., Wagner R.L., Friezner Degen S.J., Luk G.D., Flanagan M.A. Nucleic Acids Res. 20:2581-2590(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	"Regulation of ornithine decarboxylase mRNA levels in human breast cancer cells: pattern of expression and involvement of core enhancer promoter element." Wright P.S., Cooper J.R., Cross-Doersen D.E., Miller J.A., Chmielewski P.A., Wagner R.L., Streng K.A., Flanagan M.A. Cell Growth Differ. 6:1097-1102(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Esophagus and Testis.
[10]	NIEHS SNPs program Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	"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: Lymph.
[14]	"Expression of human chromosome 2 ornithine decarboxylase gene in ornithine decarboxylase-deficient Chinese hamster ovary cells." Hsieh J.T., Denning M.F., Heidel S.M., Verma A.K. Cancer Res. 50:2239-2244(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
[15]	"Cell-cycle-dependent expression of human ornithine decarboxylase." Kaczmarek L., Calabretta B., Ferrari S., de Riel J.K. J. Cell. Physiol. 132:545-551(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 112-461.
[16]	"Nitric oxide inhibits ornithine decarboxylase by S-nitrosylation." Bauer P.M., Fukuto J.M., Buga G.M., Pegg A.E., Ignarro L.J. Biochem. Biophys. Res. Commun. 262:355-358(1999) [PubMed] [Europe PMC] [Abstract] Cited for: S-NITROSYLATION.
[17]	"Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of cysteine 360 in the active site of the enzyme." Bauer P.M., Buga G.M., Fukuto J.M., Pegg A.E., Ignarro L.J. J. Biol. Chem. 276:34458-34464(2001) [PubMed] [Europe PMC] [Abstract] Cited for: S-NITROSYLATION AT CYS-360, MUTAGENESIS OF CYS-360.
[18]	"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection." Leong W.F., Chow V.T. Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, MASS SPECTROMETRY.
[19]	"Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding." Almrud J.J., Oliveira M.A., Kern A.D., Grishin N.V., Phillips M.A., Hackert M.L. J. Mol. Biol. 295:7-16(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Wikipedia

Ornithine decarboxylase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16650 mRNA. Translation: AAA59966.2.
M31061 Genomic DNA. Translation: AAA60563.1.
X16277 Genomic DNA. Translation: CAA34353.1.
M33764 Genomic DNA. Translation: AAA60564.1.
M34158 Genomic DNA. Translation: AAA59969.1.
M81740 Genomic DNA. Translation: AAA59967.1.
X55362 mRNA. Translation: CAA39047.1.
AK292352 mRNA. Translation: BAF85041.1.
AK312766 mRNA. Translation: BAG35632.1.
AY841870 Genomic DNA. Translation: AAV88093.1.
AC007249 Genomic DNA. Translation: AAY15034.1.
CH471053 Genomic DNA. Translation: EAX00958.1.
CH471053 Genomic DNA. Translation: EAX00959.1.
BC025296 mRNA. Translation: AAH25296.1.
X53271 mRNA. Translation: CAA37369.1.
M20372 mRNA. Translation: AAA59968.1.

IPI

IPI00008497.

PIR

DCHUO. S06900.

RefSeq

NP_002530.1. NM_002539.1.

UniGene

Hs.467701.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D7K	X-ray	2.10	A/B	7-427	[»]
2ON3	X-ray	3.00	A/B	1-461	[»]
2OO0	X-ray	1.90	A/B	1-461	[»]

ProteinModelPortal

P11926.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11926. 1 interaction.

MINT

MINT-1208473.

STRING

9606.ENSP00000234111.

PTM databases

PhosphoSite

P11926.

Polymorphism databases

DMDM

118377.

Proteomic databases

PaxDb

P11926.

PRIDE

P11926.

Protocols and materials databases

DNASU

4953.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000234111; ENSP00000234111; ENSG00000115758.
ENST00000405333; ENSP00000385333; ENSG00000115758.

GeneID

4953.

KEGG

hsa:4953.

UCSC

uc002rao.1. human.

Organism-specific databases

CTD

4953.

GeneCards

GC02M010580.

HGNC

HGNC:8109. ODC1.

HPA

CAB035996.
HPA001536.

MIM

165640. gene.

neXtProt

NX_P11926.

PharmGKB

PA31897.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0019.

HOGENOM

HOG000274133.

HOVERGEN

HBG005456.

InParanoid

P11926.

KO

K01581.

OMA

GPICETS.

OrthoDB

EOG4ZGPC6.

PhylomeDB

P11926.

Enzyme and pathway databases

BioCyc

MetaCyc:HS03935-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P11926.

UniPathway

UPA00535; UER00288.

Gene expression databases

ArrayExpress

P11926.

Bgee

P11926.

CleanEx

HS_ODC1.

Genevestigator

P11926.

GermOnline

ENSG00000115758. Homo sapiens.

Family and domain databases

Gene3D

2.40.37.10. 1 hit.

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]

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

BindingDB

P11926.

ChEMBL

CHEMBL1869.

ChiTaRS

ODC1. human.

DrugBank

DB00114. Pyridoxal Phosphate.
DB00127. Spermine.

EvolutionaryTrace

P11926.

GenomeRNAi

4953.

NextBio

19080.

SOURCE

Search...

Entry information

Entry name

DCOR_HUMAN

Accession

Primary (citable) accession number: P11926
Secondary accession number(s): Q53TU3, Q6LDS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 146 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.