ID   DCOR_MOUSE              Reviewed;         461 AA.
AC   P00860; Q61997; Q61998; Q6PB87;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Ornithine decarboxylase;
DE            Short=ODC;
DE            EC=4.1.1.17;
GN   Name=Odc1; Synonyms=Odc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2982844; DOI=10.1016/s0021-9258(18)89457-1;
RA   Gupta M., Coffino P.;
RT   "Mouse ornithine decarboxylase. Complete amino acid sequence deduced from
RT   cDNA.";
RL   J. Biol. Chem. 260:2941-2944(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3856848; DOI=10.1073/pnas.82.6.1673;
RA   Kahana C., Nathans D.;
RT   "Nucleotide sequence of murine ornithine decarboxylase mRNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:1673-1677(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=3362685; DOI=10.1093/nar/16.6.2731;
RA   Coffino P., Chen E.L.;
RT   "Nucleotide sequence of the mouse ornithine decarboxylase gene.";
RL   Nucleic Acids Res. 16:2731-2731(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3372502; DOI=10.1016/s0021-9258(18)68541-2;
RA   Katz A., Kahana C.;
RT   "Isolation and characterization of the mouse ornithine decarboxylase
RT   gene.";
RL   J. Biol. Chem. 263:7604-7609(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8350350; DOI=10.1007/bf00556360;
RA   Johannes G.J., Berger F.G.;
RT   "Domains within the mammalian ornithine decarboxylase messenger RNA have
RT   evolved independently and episodically.";
RL   J. Mol. Evol. 36:555-567(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Kunming;
RA   Yu Y., Luo X.;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 178-461.
RX   PubMed=3456155; DOI=10.1073/pnas.83.3.594;
RA   Hickok N.J., Seppaenen P.J., Kontula K.K., Jaenne P.A., Bardin C.W.,
RA   Jaenne O.A.;
RT   "Two ornithine decarboxylase mRNA species in mouse kidney arise from size
RT   heterogeneity at their 3' termini.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:594-598(1986).
RN   [11]
RP   PHOSPHORYLATION AT SER-303 BY CKII.
RX   PubMed=2026163; DOI=10.1111/j.1432-1033.1991.tb15927.x;
RA   Rosenberg-Hasson Y., Strumpf D., Kahana C.;
RT   "Mouse ornithine decarboxylase is phosphorylated by casein kinase-II at a
RT   predominant single location (serine 303).";
RL   Eur. J. Biochem. 197:419-424(1991).
RN   [12]
RP   ACTIVE SITE, AND PYRIDOXAL PHOSPHATE AT LYS-69.
RX   PubMed=1730582; DOI=10.1016/s0021-9258(18)48472-4;
RA   Poulin R., Lu L., Ackermann B., Bey P., Pegg A.E.;
RT   "Mechanism of the irreversible inactivation of mouse ornithine
RT   decarboxylase by alpha-difluoromethylornithine. Characterization of
RT   sequences at the inhibitor and coenzyme binding sites.";
RL   J. Biol. Chem. 267:150-158(1992).
RN   [13]
RP   ACTIVE SITE.
RX   PubMed=8504104; DOI=10.1021/bi00073a017;
RA   Tobias K.E., Kahana C.;
RT   "Intersubunit location of the active site of mammalian ornithine
RT   decarboxylase as determined by hybridization of site-directed mutants.";
RL   Biochemistry 32:5842-5847(1993).
RN   [14]
RP   MUTAGENESIS OF GLY-387.
RX   PubMed=8243470; DOI=10.1111/j.1432-1033.1993.tb18371.x;
RA   Tobias K.E., Mamroud-Kidron E., Kahana C.;
RT   "Gly387 of murine ornithine decarboxylase is essential for the formation of
RT   stable homodimers.";
RL   Eur. J. Biochem. 218:245-250(1993).
RN   [15]
RP   SUBUNIT.
RX   PubMed=8106349; DOI=10.1016/s0021-9258(17)41842-4;
RA   Coleman C.S., Stanley B.A., Viswanath R., Pegg A.E.;
RT   "Rapid exchange of subunits of mammalian ornithine decarboxylase.";
RL   J. Biol. Chem. 269:3155-3158(1994).
RN   [16]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=18973822; DOI=10.1016/j.biocel.2008.09.029;
RA   Lopez-Contreras A.J., Ramos-Molina B., Martinez-de-la-Torre M.,
RA   Penafiel-Verdu C., Puelles L., Cremades A., Penafiel R.;
RT   "Expression of antizyme inhibitor 2 in male haploid germinal cells suggests
RT   a role in spermiogenesis.";
RL   Int. J. Biochem. Cell Biol. 41:1070-1078(2009).
RN   [17]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=24967154; DOI=10.1016/j.fob.2014.05.004;
RA   Ramos-Molina B., Lambertos A., Lopez-Contreras A.J., Kasprzak J.M.,
RA   Czerwoniec A., Bujnicki J.M., Cremades A., Penafiel R.;
RT   "Structural and degradative aspects of ornithine decarboxylase antizyme
RT   inhibitor 2.";
RL   FEBS Open Bio 4:510-521(2014).
RN   [18] {ECO:0007744|PDB:7ODC}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-424 IN COMPLEX WITH COFACTOR,
RP   AND PYRIDOXAL PHOSPHATE AT LYS-69.
RX   PubMed=10378276; DOI=10.1016/s0969-2126(99)80073-2;
RA   Kern A.D., Oliveira M.A., Coffino P., Hackert M.L.;
RT   "Structure of mammalian ornithine decarboxylase at 1.6 A resolution:
RT   stereochemical implications of PLP-dependent amino acid decarboxylases.";
RL   Structure 7:567-581(1999).
CC   -!- FUNCTION: Catalyzes the first and rate-limiting step of polyamine
CC       biosynthesis that converts ornithine into putrescine, which is the
CC       precursor for the polyamines, spermidine and spermine. Polyamines are
CC       essential for cell proliferation and are implicated in cellular
CC       processes, ranging from DNA replication to apoptosis.
CC       {ECO:0000269|PubMed:18973822, ECO:0000269|PubMed:24967154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:326268; EC=4.1.1.17;
CC         Evidence={ECO:0000250|UniProtKB:P11926};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:10378276, ECO:0000269|PubMed:1730582};
CC   -!- ACTIVITY REGULATION: Inhibited by antizymes (AZs) OAZ1, OAZ2 and OAZ3
CC       in response to polyamine levels. AZs inhibit the assembly of the
CC       functional homodimer by binding to ODC monomers. Additionally, OAZ1
CC       targets ODC monomers for ubiquitin-independent proteolytic destruction
CC       by the 26S proteasome. {ECO:0000250|UniProtKB:P11926}.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC   -!- SUBUNIT: Homodimer. Only the dimer is catalytically active, as the
CC       active sites are constructed of residues from both monomers
CC       (PubMed:8106349, PubMed:10378276). Does not form a heterodimer with
CC       AZIN2 (PubMed:24967154). {ECO:0000269|PubMed:10378276,
CC       ECO:0000269|PubMed:24967154, ECO:0000269|PubMed:8106349}.
CC   -!- TISSUE SPECIFICITY: Expressed during testis development in the outer
CC       part of the seminiferous tubules. {ECO:0000269|PubMed:18973822}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000305}.
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DR   EMBL; M20617; AAA51638.1; -; mRNA.
DR   EMBL; M10624; AAA39845.1; -; mRNA.
DR   EMBL; X07392; CAA30301.1; -; Genomic_DNA.
DR   EMBL; J03733; AAA39849.1; -; Genomic_DNA.
DR   EMBL; S64539; AAB27809.1; -; mRNA.
DR   EMBL; EU684749; ACD81645.1; -; mRNA.
DR   EMBL; AK139610; BAE24082.1; -; mRNA.
DR   EMBL; CH466582; EDK98494.1; -; Genomic_DNA.
DR   EMBL; BC059826; AAH59826.1; -; mRNA.
DR   EMBL; BC083122; AAH83122.1; -; mRNA.
DR   EMBL; M12330; AAA39846.1; -; mRNA.
DR   EMBL; M12331; AAA39848.1; -; mRNA.
DR   CCDS; CCDS25829.1; -.
DR   PIR; A01077; DCMSO.
DR   PIR; I56477; I56477.
DR   RefSeq; NP_038642.2; NM_013614.2.
DR   RefSeq; XP_017170479.1; XM_017314990.1.
DR   PDB; 7ODC; X-ray; 1.60 A; A=1-424.
DR   PDBsum; 7ODC; -.
DR   AlphaFoldDB; P00860; -.
DR   SMR; P00860; -.
DR   BioGRID; 201896; 1.
DR   IntAct; P00860; 1.
DR   STRING; 10090.ENSMUSP00000128661; -.
DR   ChEMBL; CHEMBL2840; -.
DR   iPTMnet; P00860; -.
DR   PhosphoSitePlus; P00860; -.
DR   EPD; P00860; -.
DR   MaxQB; P00860; -.
DR   PaxDb; 10090-ENSMUSP00000128661; -.
DR   ProteomicsDB; 279314; -.
DR   Pumba; P00860; -.
DR   Antibodypedia; 781; 974 antibodies from 34 providers.
DR   DNASU; 18263; -.
DR   Ensembl; ENSMUST00000171737.3; ENSMUSP00000128661.2; ENSMUSG00000011179.9.
DR   GeneID; 18263; -.
DR   KEGG; mmu:18263; -.
DR   UCSC; uc007ncv.1; mouse.
DR   AGR; MGI:97402; -.
DR   CTD; 4953; -.
DR   MGI; MGI:97402; Odc1.
DR   VEuPathDB; HostDB:ENSMUSG00000011179; -.
DR   eggNOG; KOG0622; Eukaryota.
DR   GeneTree; ENSGT00950000182995; -.
DR   HOGENOM; CLU_026444_1_1_1; -.
DR   InParanoid; P00860; -.
DR   OMA; AYCRSMA; -.
DR   OrthoDB; 48358at2759; -.
DR   PhylomeDB; P00860; -.
DR   TreeFam; TF300760; -.
DR   BRENDA; 4.1.1.17; 3474.
DR   Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-MMU-351202; Metabolism of polyamines.
DR   SABIO-RK; P00860; -.
DR   UniPathway; UPA00535; UER00288.
DR   BioGRID-ORCS; 18263; 4 hits in 80 CRISPR screens.
DR   ChiTaRS; Odc1; mouse.
DR   EvolutionaryTrace; P00860; -.
DR   PRO; PR:P00860; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; P00860; Protein.
DR   Bgee; ENSMUSG00000011179; Expressed in spermatid and 271 other cell types or tissues.
DR   ExpressionAtlas; P00860; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0006595; P:polyamine metabolic process; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0009446; P:putrescine biosynthetic process; ISO:MGI.
DR   GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IDA:UniProtKB.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR   CDD; cd00622; PLPDE_III_ODC; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022657; De-COase2_CS.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR002433; Orn_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR11482; ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR11482:SF42; ORNITHINE DECARBOXYLASE; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   PRINTS; PR01182; ORNDCRBXLASE.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
DR   Genevisible; P00860; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Decarboxylase; Lyase; Phosphoprotein; Polyamine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; S-nitrosylation.
FT   CHAIN           1..461
FT                   /note="Ornithine decarboxylase"
FT                   /id="PRO_0000149892"
FT   ACT_SITE        360
FT                   /note="Proton donor; shared with dimeric partner"
FT                   /evidence="ECO:0000269|PubMed:10378276,
FT                   ECO:0000269|PubMed:1730582, ECO:0000269|PubMed:8504104"
FT   BINDING         200
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         237
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:10378276"
FT   BINDING         274..277
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:10378276"
FT   BINDING         331..332
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P07805"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P07805"
FT   BINDING         389
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:10378276"
FT   SITE            197
FT                   /note="Stacks against the aromatic ring of pyridoxal
FT                   phosphate and stabilizes reaction intermediates"
FT                   /evidence="ECO:0000305|PubMed:10378276"
FT   MOD_RES         69
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:10378276,
FT                   ECO:0000269|PubMed:1730582, ECO:0007744|PDB:7ODC"
FT   MOD_RES         303
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:2026163"
FT   MOD_RES         360
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   MUTAGEN         387
FT                   /note="G->A: Partial loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8243470"
FT   MUTAGEN         387
FT                   /note="G->C,D,E,F,H,I,K,L,M,N,P,Q,R,S,T,V,W,Y: Loss of
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8243470"
FT   CONFLICT        178
FT                   /note="R -> W (in Ref. 10; AAA39846)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="E -> D (in Ref. 1; AAA51638, 2; AAA39845, 3;
FT                   CAA30301, 4; AAA39849 and 5; AAB27809)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="Y -> H (in Ref. 10; AAA39848)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..6
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          9..14
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           20..28
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          40..44
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           45..58
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           74..83
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           92..100
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           117..125
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          130..133
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           136..145
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          150..155
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           174..186
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          190..195
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           206..225
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          241..246
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           248..262
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           265..267
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          270..273
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           277..280
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           281..283
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          284..296
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          313..319
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   TURN            322..326
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           327..331
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          339..342
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          350..356
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          358..360
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          365..373
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          380..383
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          388..390
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           391..393
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           397..399
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   STRAND          404..410
FT                   /evidence="ECO:0007829|PDB:7ODC"
FT   HELIX           411..417
FT                   /evidence="ECO:0007829|PDB:7ODC"
SQ   SEQUENCE   461 AA;  51177 MW;  B581753F57AC0A30 CRC64;
     MSSFTKDEFD CHILDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK KHLRWLKALP
     RVTPFYAVKC NDSRAIVSTL AAIGTGFDCA SKTEIQLVQG LGVPAERVIY ANPCKQVSQI
     KYAASNGVQM MTFDSEIELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLKTSRLL
     LERAKELNID VIGVSFHVGS GCTDPETFVQ AVSDARCVFD MATEVGFSMH LLDIGGGFPG
     SEDTKLKFEE ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKTVWKEQ
     PGSDDEDESN EQTFMYYVND GVYGSFNCIL YDHAHVKALL QKRPKPDEKY YSSSIWGPTC
     DGLDRIVERC NLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPNIYYVMS RPMWQLMKQI
     QSHGFPPEVE EQDDGTLPMS CAQESGMDRH PAACASARIN V
//