DCOR_MOUSE
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 03-AUG-2022, entry version 185.
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; P00860; -.
DR PRIDE; P00860; -.
DR ProteomicsDB; 279314; -.
DR Antibodypedia; 781; 905 antibodies from 34 providers.
DR DNASU; 18263; -.
DR Ensembl; ENSMUST00000171737; ENSMUSP00000128661; ENSMUSG00000011179.
DR GeneID; 18263; -.
DR KEGG; mmu:18263; -.
DR UCSC; uc007ncv.1; mouse.
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; YCRSMAS; -.
DR OrthoDB; 725914at2759; -.
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 75 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 268 other tissues.
DR ExpressionAtlas; P00860; baseline and differential.
DR Genevisible; P00860; MM.
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 Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 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; PTHR11482; 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; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
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
