ID   CN37_HUMAN              Reviewed;         421 AA.
AC   P09543;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 228.
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|HGNC:HGNC:2158};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1385234; DOI=10.1042/bst0200621;
RA   Thompson R.J.;
RT   "2',3'-cyclic nucleotide-3'-phosphohydrolase and signal transduction in
RT   central nervous system myelin.";
RL   Biochem. Soc. Trans. 20:621-626(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CNPI).
RC   TISSUE=Brain;
RX   PubMed=2835044; DOI=10.1016/s0006-291x(88)80114-1;
RA   Kurihara T., Takahashi Y., Nishiyama A., Kumanishi T.;
RT   "cDNA cloning and amino acid sequence of human brain 2',3'-cyclic-
RT   nucleotide 3'-phosphodiesterase.";
RL   Biochem. Biophys. Res. Commun. 152:837-842(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8392017; DOI=10.1016/0378-1119(93)90283-9;
RA   Monoh K., Kurihara T., Takahashi Y., Ichikawa T., Kumanishi T., Hayashi S.,
RA   Minoshima S., Shimizu N.;
RT   "Structure, expression and chromosomal localization of the gene encoding
RT   human 2',3'-cyclic-nucleotide 3'-phosphodiesterase.";
RL   Gene 129:297-301(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1360194; DOI=10.1111/j.1469-1809.1992.tb01149.x;
RA   Douglas A.J., Fox M.F., Abbott C.M., Hinks L.J., Sharpe G., Povey S.,
RA   Thompson R.J.;
RT   "Structure and chromosomal localization of the human 2',3'-cyclic
RT   nucleotide 3'-phosphodiesterase gene.";
RL   Ann. Hum. Genet. 56:243-254(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS CNPI AND CNPII).
RC   TISSUE=Brain, and Skin;
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   [7]
RP   PROTEIN SEQUENCE OF 21-58.
RX   PubMed=9268698; DOI=10.1006/bbrc.1997.7125;
RA   Stricker R., Kalbacher H., Reiser G.;
RT   "The epitope recognized by a monoclonal antibody in the myelin-associated
RT   protein CNP.";
RL   Biochem. Biophys. Res. Commun. 237:266-270(1997).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=12643545; DOI=10.1021/pr025562r;
RA   Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA   Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA   Appella E.;
RT   "Proteomic analysis of early melanosomes: identification of novel
RT   melanosomal proteins.";
RL   J. Proteome Res. 2:69-79(2003).
RN   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA   Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA   Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-9 AND SER-170, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 186-399 IN COMPLEX WITH PHOSPHATE.
RX   PubMed=15713463; DOI=10.1016/j.jmb.2004.12.024;
RA   Sakamoto Y., Tanaka N., Ichimiya T., Kurihara T., Nakamura K.T.;
RT   "Crystal structure of the catalytic fragment of human brain 2',3'-cyclic-
RT   nucleotide 3'-phosphodiesterase.";
RL   J. Mol. Biol. 346:789-800(2005).
RN   [16]
RP   VARIANT HLD20 LEU-82, CHARACTERIZATION OF VARIANT HLD20 LEU-82, AND
RP   INVOLVEMENT IN HLD20.
RX   PubMed=32128616; DOI=10.1007/s00439-020-02144-4;
RA   Al-Abdi L., Al Murshedi F., Elmanzalawy A., Al Habsi A., Helaby R.,
RA   Ganesh A., Ibrahim N., Patel N., Alkuraya F.S.;
RT   "CNP deficiency causes severe hypomyelinating leukodystrophy in humans.";
RL   Hum. Genet. 139:615-622(2020).
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 (By similarity). {ECO:0000250|UniProtKB:P06623,
CC       ECO:0000250|UniProtKB:P16330}.
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:0000250|UniProtKB:P16330}.
CC   -!- INTERACTION:
CC       P09543; P42858: HTT; NbExp=10; IntAct=EBI-1059219, EBI-466029;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P16330}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:P16330}. Melanosome
CC       {ECO:0000269|PubMed:12643545}. Note=Firmly bound to membrane structures
CC       of brain white matter. {ECO:0000250|UniProtKB:P16330}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=CNPII; Synonyms=DNAII;
CC         IsoId=P09543-1; Sequence=Displayed;
CC       Name=CNPI; Synonyms=DNAI;
CC         IsoId=P09543-2; Sequence=VSP_004171;
CC   -!- DISEASE: Leukodystrophy, hypomyelinating, 20 (HLD20) [MIM:619071]: An
CC       autosomal recessive disorder characterized by neuroregression and loss
CC       of motor, language and cognitive skills, after a normal early
CC       development. Disease onset is between 12 and 18 month of age. Patients
CC       show poor overall growth, microcephaly, feeding difficulties and
CC       spastic quadriplegia. Some patients may have seizures. Death in
CC       childhood may occur. Hypomyelinating leukodystrophy with subcortical
CC       and periventricular white matter abnormalities is seen on brain
CC       imaging. {ECO:0000269|PubMed:32128616}. Note=The disease may be caused
CC       by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CNPase
CC       family. {ECO:0000305}.
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DR   EMBL; S46849; AAB23928.2; -; Genomic_DNA.
DR   EMBL; S46843; AAB23928.2; JOINED; Genomic_DNA.
DR   EMBL; S46845; AAB23928.2; JOINED; Genomic_DNA.
DR   EMBL; S46846; AAB23928.2; JOINED; Genomic_DNA.
DR   EMBL; M19650; AAA35704.1; -; mRNA.
DR   EMBL; D13146; BAA39694.1; -; Genomic_DNA.
DR   EMBL; D13146; BAA02435.1; -; Genomic_DNA.
DR   EMBL; S50017; AAB24298.2; -; Genomic_DNA.
DR   EMBL; S50013; AAB24298.2; JOINED; Genomic_DNA.
DR   EMBL; S50014; AAB24298.2; JOINED; Genomic_DNA.
DR   EMBL; S50016; AAB24298.2; JOINED; Genomic_DNA.
DR   EMBL; AC125257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001362; AAH01362.1; -; mRNA.
DR   EMBL; BC006392; AAH06392.1; -; mRNA.
DR   EMBL; BC011046; AAH11046.1; -; mRNA.
DR   EMBL; BC028040; AAH28040.1; -; mRNA.
DR   CCDS; CCDS11414.2; -. [P09543-1]
DR   CCDS; CCDS82123.1; -. [P09543-2]
DR   PIR; JC1517; JC1517.
DR   RefSeq; NP_001317145.1; NM_001330216.1. [P09543-2]
DR   RefSeq; NP_149124.3; NM_033133.4. [P09543-1]
DR   RefSeq; XP_011522642.1; XM_011524340.2. [P09543-2]
DR   PDB; 1WOJ; X-ray; 1.80 A; A=186-399.
DR   PDBsum; 1WOJ; -.
DR   AlphaFoldDB; P09543; -.
DR   SMR; P09543; -.
DR   BioGRID; 107667; 198.
DR   IntAct; P09543; 89.
DR   MINT; P09543; -.
DR   STRING; 9606.ENSP00000377470; -.
DR   GlyGen; P09543; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P09543; -.
DR   PhosphoSitePlus; P09543; -.
DR   SwissPalm; P09543; -.
DR   BioMuta; CNP; -.
DR   DMDM; 1705945; -.
DR   EPD; P09543; -.
DR   jPOST; P09543; -.
DR   MassIVE; P09543; -.
DR   MaxQB; P09543; -.
DR   PaxDb; 9606-ENSP00000377470; -.
DR   PeptideAtlas; P09543; -.
DR   ProteomicsDB; 52244; -. [P09543-1]
DR   ProteomicsDB; 52245; -. [P09543-2]
DR   Pumba; P09543; -.
DR   Antibodypedia; 3629; 657 antibodies from 45 providers.
DR   DNASU; 1267; -.
DR   Ensembl; ENST00000393888.1; ENSP00000377466.1; ENSG00000173786.17. [P09543-2]
DR   Ensembl; ENST00000393892.8; ENSP00000377470.2; ENSG00000173786.17. [P09543-1]
DR   GeneID; 1267; -.
DR   KEGG; hsa:1267; -.
DR   MANE-Select; ENST00000393892.8; ENSP00000377470.2; NM_033133.5; NP_149124.3.
DR   UCSC; uc002hyl.2; human. [P09543-1]
DR   AGR; HGNC:2158; -.
DR   CTD; 1267; -.
DR   DisGeNET; 1267; -.
DR   GeneCards; CNP; -.
DR   HGNC; HGNC:2158; CNP.
DR   HPA; ENSG00000173786; Tissue enriched (brain).
DR   MalaCards; CNP; -.
DR   MIM; 123830; gene.
DR   MIM; 619071; phenotype.
DR   neXtProt; NX_P09543; -.
DR   OpenTargets; ENSG00000173786; -.
DR   PharmGKB; PA26680; -.
DR   VEuPathDB; HostDB:ENSG00000173786; -.
DR   eggNOG; KOG2401; Eukaryota.
DR   GeneTree; ENSGT00510000048410; -.
DR   HOGENOM; CLU_039178_0_0_1; -.
DR   InParanoid; P09543; -.
DR   OMA; DAYKINP; -.
DR   OrthoDB; 5489998at2759; -.
DR   PhylomeDB; P09543; -.
DR   TreeFam; TF332157; -.
DR   BRENDA; 3.1.4.37; 2681.
DR   BRENDA; 3.1.4.58; 2681.
DR   PathwayCommons; P09543; -.
DR   SignaLink; P09543; -.
DR   SIGNOR; P09543; -.
DR   BioGRID-ORCS; 1267; 32 hits in 1159 CRISPR screens.
DR   ChiTaRS; CNP; human.
DR   EvolutionaryTrace; P09543; -.
DR   GeneWiki; 2%27,3%27-Cyclic-nucleotide_3%27-phosphodiesterase; -.
DR   GenomeRNAi; 1267; -.
DR   Pharos; P09543; Tbio.
DR   PRO; PR:P09543; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P09543; Protein.
DR   Bgee; ENSG00000173786; Expressed in inferior olivary complex and 201 other cell types or tissues.
DR   ExpressionAtlas; P09543; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR   GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR   GO; GO:0035748; C:myelin sheath abaxonal region; IEA:Ensembl.
DR   GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0031143; C:pseudopodium; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; ISS:UniProtKB.
DR   GO; GO:0030551; F:cyclic nucleotide binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR   GO; GO:0009214; P:cyclic nucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR   Gene3D; 3.90.1740.10; 2',3'-cyclic nucleotide 3'-phosphodiesterase superfamily; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR008431; CNPase.
DR   InterPro; IPR047325; CNPase_cat.
DR   InterPro; IPR009097; Cyclic_Pdiesterase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10156; 2',3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR10156:SF0; 2',3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE; 1.
DR   Pfam; PF13671; AAA_33; 1.
DR   Pfam; PF05881; CNPase; 1.
DR   PIRSF; PIRSF000970; CNPase; 1.
DR   SUPFAM; SSF55144; LigT-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   UCD-2DPAGE; P09543; -.
DR   Genevisible; P09543; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing; Hydrolase;
KW   Leukodystrophy; Lipoprotein; Membrane; Methylation; Neurodegeneration;
KW   Phosphoprotein; Prenylation; Reference proteome; RNA-binding.
FT   CHAIN           1..418
FT                   /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT                   /id="PRO_0000089961"
FT   PROPEP          419..421
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000422296"
FT   ACT_SITE        251
FT                   /note="Proton acceptor"
FT   ACT_SITE        330
FT                   /note="Proton donor"
FT   BINDING         253
FT                   /ligand="substrate"
FT   BINDING         332
FT                   /ligand="substrate"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         110
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P16330"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13233"
FT   MOD_RES         418
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           418
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..20
FT                   /note="Missing (in isoform CNPI)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:2835044"
FT                   /id="VSP_004171"
FT   VARIANT         82
FT                   /note="S -> L (in HLD20; uncertain significance; decreased
FT                   protein levels in patient cells; dbSNP:rs2050933471)"
FT                   /evidence="ECO:0000269|PubMed:32128616"
FT                   /id="VAR_085056"
FT   VARIANT         207
FT                   /note="Q -> R (in dbSNP:rs34353668)"
FT                   /id="VAR_033746"
FT   STRAND          188..194
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   HELIX           196..215
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   HELIX           217..221
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   HELIX           223..226
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   HELIX           238..241
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   STRAND          251..256
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   HELIX           258..260
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   HELIX           265..270
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   HELIX           272..277
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   STRAND          281..291
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   STRAND          293..301
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   HELIX           306..309
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   TURN            325..328
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   STRAND          330..335
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   HELIX           343..356
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   STRAND          362..367
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   STRAND          370..376
FT                   /evidence="ECO:0007829|PDB:1WOJ"
FT   STRAND          379..397
FT                   /evidence="ECO:0007829|PDB:1WOJ"
SQ   SEQUENCE   421 AA;  47579 MW;  CA6D0097DFD87255 CRC64;
     MNRGFSRKSH TFLPKIFFRK MSSSGAKDKP ELQFPFLQDE DTVATLLECK TLFILRGLPG
     SGKSTLARVI VDKYRDGTKM VSADAYKITP GARGAFSEEY KRLDEDLAAY CRRRDIRILV
     LDDTNHERER LEQLFEMADQ YQYQVVLVEP KTAWRLDCAQ LKEKNQWQLS ADDLKKLKPG
     LEKDFLPLYF GWFLTKKSSE TLRKAGQVFL EELGNHKAFK KELRQFVPGD EPREKMDLVT
     YFGKRPPGVL HCTTKFCDYG KAPGAEEYAQ QDVLKKSYSK AFTLTISALF VTPKTTGARV
     ELSEQQLQLW PSDVDKLSPT DNLPRGSRAH ITLGCAADVE AVQTGLDLLE ILRQEKGGSR
     GEEVGELSRG KLYSLGNGRW MLTLAKNMEV RAIFTGYYGK GKPVPTQGSR KGGALQSCTI
     I
//