CN37_HUMAN
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 03-AUG-2022, entry version 219.
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; 146.
DR IntAct; P09543; 73.
DR MINT; P09543; -.
DR STRING; 9606.ENSP00000377470; -.
DR iPTMnet; P09543; -.
DR PhosphoSitePlus; P09543; -.
DR SwissPalm; P09543; -.
DR BioMuta; CNP; -.
DR DMDM; 1705945; -.
DR UCD-2DPAGE; P09543; -.
DR EPD; P09543; -.
DR jPOST; P09543; -.
DR MassIVE; P09543; -.
DR MaxQB; P09543; -.
DR PaxDb; P09543; -.
DR PeptideAtlas; P09543; -.
DR PRIDE; P09543; -.
DR ProteomicsDB; 52244; -. [P09543-1]
DR ProteomicsDB; 52245; -. [P09543-2]
DR Antibodypedia; 3629; 544 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 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 OMA; VEPKTSW; -.
DR OrthoDB; 1248632at2759; -.
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 BioGRID-ORCS; 1267; 31 hits in 1081 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 199 other tissues.
DR ExpressionAtlas; P09543; baseline and differential.
DR Genevisible; P09543; HS.
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:0005886; C:plasma membrane; IDA:HPA.
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:0007568; P:aging; 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:0000226; P:microtubule cytoskeleton organization; 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; 3.40.50.300; -; 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 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; unknown pathological significance;
FT decreased protein levels in patient cells)"
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
