CN37_MOUSE
ID CN37_MOUSE Reviewed; 420 AA.
AC P16330; Q61424; Q8C7C9; Q91V42; Q923F3;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase {ECO:0000305};
DE Short=CNP;
DE Short=CNPase;
DE EC=3.1.4.37 {ECO:0000250|UniProtKB:P06623};
DE Flags: Precursor;
GN Name=Cnp {ECO:0000312|MGI:MGI:88437}; Synonyms=Cnp1;
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 [GENOMIC DNA] (ISOFORM CNPI).
RC STRAIN=DBA;
RX PubMed=2558653; DOI=10.1016/0006-291x(89)92731-9;
RA Monoh K., Kurihara T., Sakimura K., Takahashi Y.;
RT "Structure of mouse 2',3'-cyclic-nucleotide 3'-phosphodiesterase gene.";
RL Biochem. Biophys. Res. Commun. 165:1213-1220(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS CNPI AND CNPII).
RC STRAIN=DBA; TISSUE=Brain;
RX PubMed=2167669; DOI=10.1016/0006-291x(90)90502-e;
RA Kurihara T., Monoh K., Sakimura K., Takahashi Y.;
RT "Alternative splicing of mouse brain 2',3'-cyclic-nucleotide 3'-
RT phosphodiesterase mRNA.";
RL Biochem. Biophys. Res. Commun. 170:1074-1081(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CNPI).
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CNPII).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-418 (ISOFORM CNPII).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [6]
RP PROTEIN SEQUENCE OF 94-101; 103-112; 117-127; 130-150; 164-174; 183-195;
RP 203-216; 235-243; 261-274; 276-293; 356-368; 379-385 AND 391-399.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP ISOPRENYLATION AT CYS-417, AND SUBCELLULAR LOCATION.
RX PubMed=18076147; DOI=10.1021/bi701474t;
RA Esposito C., Scrima M., Carotenuto A., Tedeschi A., Rovero P., D'Errico G.,
RA Malfitano A.M., Bifulco M., D'Ursi A.M.;
RT "Structures and micelle locations of the nonlipidated and lipidated C-
RT terminal membrane anchor of 2',3'-cyclic nucleotide-3'-phosphodiesterase.";
RL Biochemistry 47:308-319(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 179-398, ACTIVE SITE,
RP SUBSTRATE-BINDING SITES, RNA-BINDING, FUNCTION, AND SUBUNIT.
RX PubMed=22393399; DOI=10.1371/journal.pone.0032336;
RA Myllykoski M., Raasakka A., Han H., Kursula P.;
RT "Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand
RT binding and molecular conformation.";
RL PLoS ONE 7:E32336-E32336(2012).
CC -!- FUNCTION: Catalyzes the formation of 2'-nucleotide products from 2',3'-
CC cyclic substrates (By similarity). May participate in RNA metabolism in
CC the myelinating cell, CNP is the third most abundant protein in central
CC nervous system myelin (PubMed:22393399). {ECO:0000250|UniProtKB:P06623,
CC ECO:0000269|PubMed:22393399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-
CC phosphate + H(+); Xref=Rhea:RHEA:14489, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66954, ChEBI:CHEBI:78552; EC=3.1.4.37;
CC Evidence={ECO:0000250|UniProtKB:P06623};
CC -!- SUBUNIT: Exists as monomers and homodimers.
CC {ECO:0000269|PubMed:22393399}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18076147}; Lipid-
CC anchor {ECO:0000269|PubMed:18076147}. Melanosome
CC {ECO:0000250|UniProtKB:P09543}. Note=Firmly bound to membrane
CC structures of brain white matter.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=CNPII; Synonyms=DNAII;
CC IsoId=P16330-1; Sequence=Displayed;
CC Name=CNPI; Synonyms=DNAI;
CC IsoId=P16330-2; Sequence=VSP_004172;
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CNPase
CC family. {ECO:0000305}.
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DR EMBL; D38642; BAA07621.1; -; Genomic_DNA.
DR EMBL; D38642; BAA07622.1; -; Genomic_DNA.
DR EMBL; M31810; AAA37429.1; -; mRNA.
DR EMBL; M58045; AAA37430.1; -; mRNA.
DR EMBL; M58047; AAA37431.1; -; Genomic_DNA.
DR EMBL; M58046; AAA37431.1; JOINED; Genomic_DNA.
DR EMBL; AF332055; AAK56084.1; -; mRNA.
DR EMBL; AF332056; AAK56085.1; -; mRNA.
DR EMBL; BC005544; AAH05544.1; -; mRNA.
DR EMBL; BC021904; AAH21904.1; -; mRNA.
DR EMBL; AK050628; BAC34351.1; -; mRNA.
DR CCDS; CCDS25427.1; -. [P16330-1]
DR PIR; A35708; ESMS32.
DR RefSeq; NP_001139790.1; NM_001146318.1. [P16330-2]
DR RefSeq; NP_034053.2; NM_009923.2. [P16330-1]
DR RefSeq; XP_017169734.1; XM_017314245.1. [P16330-2]
DR PDB; 2XMI; X-ray; 1.74 A; A=179-398.
DR PDB; 2Y1P; X-ray; 1.82 A; A=179-398.
DR PDB; 2Y3X; X-ray; 2.10 A; A/B/E=179-398.
DR PDB; 2YDB; X-ray; 2.15 A; A=179-398.
DR PDB; 2YDC; X-ray; 2.05 A; A=179-398.
DR PDB; 2YDD; X-ray; 2.40 A; A=179-398.
DR PDB; 2YOZ; X-ray; 2.10 A; A=179-398.
DR PDB; 2YP0; X-ray; 2.30 A; A=179-398.
DR PDB; 2YPC; X-ray; 1.89 A; A=179-398.
DR PDB; 2YPE; X-ray; 1.90 A; A=179-398.
DR PDB; 2YPH; X-ray; 2.10 A; A=179-398.
DR PDB; 2YQ9; X-ray; 1.90 A; A=179-398.
DR PDB; 3ZBR; X-ray; 2.30 A; A/B=179-398.
DR PDB; 3ZBS; X-ray; 2.45 A; A=179-398.
DR PDB; 3ZBZ; X-ray; 2.10 A; A=179-398.
DR PDB; 4WBI; X-ray; 2.00 A; A=179-398.
DR PDB; 4WBL; X-ray; 2.50 A; A=179-398.
DR PDB; 4WC9; X-ray; 2.00 A; A=179-398.
DR PDB; 4WCA; X-ray; 1.85 A; A=179-398.
DR PDB; 4WCB; X-ray; 1.57 A; A=179-398.
DR PDB; 4WCC; X-ray; 2.70 A; A=179-398.
DR PDB; 4WDA; X-ray; 1.85 A; A=179-398.
DR PDB; 4WDB; X-ray; 1.60 A; A=179-398.
DR PDB; 4WDD; X-ray; 2.10 A; A=179-398.
DR PDB; 4WDE; X-ray; 2.40 A; A/B=179-398.
DR PDB; 4WDF; X-ray; 2.00 A; A=179-398.
DR PDB; 4WDG; X-ray; 2.05 A; A=179-398.
DR PDB; 4WDH; X-ray; 1.90 A; A=179-398.
DR PDB; 4WEX; X-ray; 2.10 A; A=179-398.
DR PDB; 4WFR; X-ray; 2.00 A; A=179-398.
DR PDB; 5AE0; X-ray; 1.04 A; A=179-398.
DR PDBsum; 2XMI; -.
DR PDBsum; 2Y1P; -.
DR PDBsum; 2Y3X; -.
DR PDBsum; 2YDB; -.
DR PDBsum; 2YDC; -.
DR PDBsum; 2YDD; -.
DR PDBsum; 2YOZ; -.
DR PDBsum; 2YP0; -.
DR PDBsum; 2YPC; -.
DR PDBsum; 2YPE; -.
DR PDBsum; 2YPH; -.
DR PDBsum; 2YQ9; -.
DR PDBsum; 3ZBR; -.
DR PDBsum; 3ZBS; -.
DR PDBsum; 3ZBZ; -.
DR PDBsum; 4WBI; -.
DR PDBsum; 4WBL; -.
DR PDBsum; 4WC9; -.
DR PDBsum; 4WCA; -.
DR PDBsum; 4WCB; -.
DR PDBsum; 4WCC; -.
DR PDBsum; 4WDA; -.
DR PDBsum; 4WDB; -.
DR PDBsum; 4WDD; -.
DR PDBsum; 4WDE; -.
DR PDBsum; 4WDF; -.
DR PDBsum; 4WDG; -.
DR PDBsum; 4WDH; -.
DR PDBsum; 4WEX; -.
DR PDBsum; 4WFR; -.
DR PDBsum; 5AE0; -.
DR AlphaFoldDB; P16330; -.
DR SMR; P16330; -.
DR BioGRID; 198792; 17.
DR IntAct; P16330; 15.
DR MINT; P16330; -.
DR STRING; 10090.ENSMUSP00000099409; -.
DR iPTMnet; P16330; -.
DR PhosphoSitePlus; P16330; -.
DR SwissPalm; P16330; -.
DR EPD; P16330; -.
DR jPOST; P16330; -.
DR MaxQB; P16330; -.
DR PaxDb; P16330; -.
DR PeptideAtlas; P16330; -.
DR PRIDE; P16330; -.
DR ProteomicsDB; 283390; -. [P16330-1]
DR ProteomicsDB; 283391; -. [P16330-2]
DR Antibodypedia; 3629; 544 antibodies from 45 providers.
DR DNASU; 12799; -.
DR Ensembl; ENSMUST00000103120; ENSMUSP00000099409; ENSMUSG00000006782. [P16330-1]
DR GeneID; 12799; -.
DR KEGG; mmu:12799; -.
DR UCSC; uc007llo.2; mouse. [P16330-1]
DR CTD; 1267; -.
DR MGI; MGI:88437; Cnp.
DR VEuPathDB; HostDB:ENSMUSG00000006782; -.
DR eggNOG; KOG2401; Eukaryota.
DR GeneTree; ENSGT00510000048410; -.
DR HOGENOM; CLU_039178_0_0_1; -.
DR InParanoid; P16330; -.
DR OMA; VEPKTSW; -.
DR PhylomeDB; P16330; -.
DR TreeFam; TF332157; -.
DR BRENDA; 3.1.4.37; 3474.
DR BioGRID-ORCS; 12799; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Cnp; mouse.
DR PRO; PR:P16330; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P16330; protein.
DR Bgee; ENSMUSG00000006782; Expressed in cranial nerve II and 243 other tissues.
DR ExpressionAtlas; P16330; baseline and differential.
DR Genevisible; P16330; MM.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR GO; GO:0035748; C:myelin sheath abaxonal region; ISO:MGI.
DR GO; GO:0035749; C:myelin sheath adaxonal region; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031143; C:pseudopodium; ISO:MGI.
DR GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IDA:MGI.
DR GO; GO:0030551; F:cyclic nucleotide binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0009214; P:cyclic nucleotide catabolic process; IEA:InterPro.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IDA:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008431; CNPase.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10156; PTHR10156; 1.
DR Pfam; PF05881; CNPase; 1.
DR PIRSF; PIRSF000970; CNPase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55144; SSF55144; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; Hydrolase;
KW Lipoprotein; Membrane; Methylation; Phosphoprotein; Prenylation;
KW Reference proteome; RNA-binding.
FT CHAIN 1..417
FT /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT /id="PRO_0000089962"
FT PROPEP 418..420
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000422297"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:22393399"
FT ACT_SITE 329
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:22393399"
FT BINDING 252
FT /ligand="substrate"
FT BINDING 331
FT /ligand="substrate"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09543"
FT MOD_RES 110
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13233"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13233"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13233"
FT MOD_RES 417
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 417
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000305|PubMed:18076147"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform CNPI)"
FT /evidence="ECO:0000303|PubMed:11471062,
FT ECO:0000303|PubMed:2167669"
FT /id="VSP_004172"
FT CONFLICT 115
FT /note="I -> M (in Ref. 1; BAA07621/BAA07622)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="M -> L (in Ref. 1; BAA07621/BAA07622)"
FT /evidence="ECO:0000305"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:5AE0"
FT HELIX 195..214
FT /evidence="ECO:0007829|PDB:5AE0"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:5AE0"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:5AE0"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:5AE0"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5AE0"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:5AE0"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:5AE0"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:5AE0"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:5AE0"
FT STRAND 280..290
FT /evidence="ECO:0007829|PDB:5AE0"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:5AE0"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:5AE0"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5AE0"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2YPH"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:5AE0"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:5AE0"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:5AE0"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:4WDB"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5AE0"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:5AE0"
FT STRAND 378..396
FT /evidence="ECO:0007829|PDB:5AE0"
SQ SEQUENCE 420 AA; 47123 MW; 2FAFFDE5F0E99EAB CRC64;
MNTSFTRKSH TFLPKLFFRK MSSSGAKEKP ELQFPFLQDE DTVATLHECK TLFILRGLPG
SGKSTLARLI LEKYHDGTKM VSADAYKIIP GSRADFSEAY KRLDEDLAGY CRRDIRVLVL
DDTNHERERL DQLFEMADQY QYQVVLVEPK TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL
EKDFLPLYFG WFLTKKSSET LRKAGQVFLE ELGNHKAFKK ELRHFISGDE PKEKLELVSY
FGKRPPGVLH CTTKFCDYGK AAGAEEYAQQ EVVKRSYGKA FKLSISALFV TPKTAGAQVV
LTDQELQLWP SDLDKPSASE GLPPGSRAHV TLGCAADVQP VQTGLDLLDI LQQVKGGSQG
EAVGELPRGK LYSLGKGRWM LSLTKKMEVK AIFTGYYGKG KPVPIHGSRK GGAMQICTII
