CNDP1_HUMAN
ID CNDP1_HUMAN Reviewed; 507 AA.
AC Q96KN2; Q14D40; Q17S05; Q2TBG0; Q6UWK2; Q9BT98;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 5.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Beta-Ala-His dipeptidase {ECO:0000305};
DE EC=3.4.13.20 {ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:24891507};
DE AltName: Full=CNDP dipeptidase 1;
DE AltName: Full=Carnosine dipeptidase 1;
DE AltName: Full=Glutamate carboxypeptidase-like protein 2;
DE AltName: Full=Serum carnosinase;
DE Flags: Precursor;
GN Name=CNDP1 {ECO:0000312|HGNC:HGNC:20675}; Synonyms=CN1, CPGL2;
GN ORFNames=UNQ1915/PRO4380;
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 [MRNA].
RC TISSUE=Brain;
RA Chen J.M., Barrett A.J.;
RT "Cloning and sequencing of a second human homologue of glutamate
RT carboxypeptidase in peptidase family M20.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], POLYMORPHISM, AND VARIANT LEU-20 INS.
RX PubMed=16046297; DOI=10.2337/diabetes.54.8.2320;
RA Janssen B., Hohenadel D., Brinkkoetter P., Peters V., Rind N., Fischer C.,
RA Rychlik I., Cerna M., Romzova M., de Heer E., Baelde H., Bakker S.J.,
RA Zirie M., Rondeau E., Mathieson P., Saleem M.A., Meyer J., Koppel H.,
RA Sauerhoefer S., Bartram C.R., Nawroth P., Hammes H.P., Yard B.A.,
RA Zschocke J., van der Woude F.J.;
RT "Carnosine as a protective factor in diabetic nephropathy: association with
RT a leucine repeat of the carnosinase gene CNDP1.";
RL Diabetes 54:2320-2327(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-20 INS.
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 [6]
RP CHARACTERIZATION.
RX PubMed=7116644; DOI=10.1016/0009-8981(82)90166-8;
RA Lenney J.F., George R.P., Weiss A.M., Kucera C.M., Chan P.W., Rinzler G.S.;
RT "Human serum carnosinase: characterization, distinction from cellular
RT carnosinase, and activation by cadmium.";
RL Clin. Chim. Acta 123:221-231(1982).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=6616870; DOI=10.1016/0009-8981(83)90243-7;
RA Lenney J.F., Peppers S.C., Kucera C.M., Sjaastad O.;
RT "Homocarnosinosis: lack of serum carnosinase is the defect probably
RT responsible for elevated brain and CSF homocarnosine.";
RL Clin. Chim. Acta 132:157-165(1983).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-132; ASP-165 AND
RP GLU-200.
RX PubMed=12473676; DOI=10.1074/jbc.m209764200;
RA Teufel M., Saudek V., Ledig J.P., Bernhardt A., Boularand S., Carreau A.,
RA Cairns N.J., Carter C., Cowley D.J., Duverger D., Ganzhorn A.J., Guenet C.,
RA Heintzelmann B., Laucher V., Sauvage C., Smirnova T.;
RT "Sequence identification and characterization of human carnosinase and a
RT closely related non-specific dipeptidase.";
RL J. Biol. Chem. 278:6521-6531(2003).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-322 AND ASN-382.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24891507; DOI=10.1074/jbc.m114.576579;
RA Veiga-da-Cunha M., Chevalier N., Stroobant V., Vertommen D.,
RA Van Schaftingen E.;
RT "Metabolite proofreading in carnosine and homocarnosine synthesis:
RT molecular identification of PM20D2 as beta-alanyl-lysine dipeptidase.";
RL J. Biol. Chem. 289:19726-19736(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 27-507 IN COMPLEX WITH ZINC IONS,
RP AND COFACTOR.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human carnosine dipeptidase 1.";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the peptide bond hydrolysis in Xaa-His dipeptides,
CC displaying the highest activity toward carnosine (beta-alanyl-L-
CC histidine) and anserine (beta-alanyl-3-methyl-histidine).
CC {ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:24891507}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential hydrolysis of the beta-Ala-|-His dipeptide
CC (carnosine), and also anserine, Xaa-|-His dipeptides and other
CC dipeptides including homocarnosine.; EC=3.4.13.20;
CC Evidence={ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:24891507};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carnosine + H2O = beta-alanine + L-histidine;
CC Xref=Rhea:RHEA:59360, ChEBI:CHEBI:15377, ChEBI:CHEBI:57485,
CC ChEBI:CHEBI:57595, ChEBI:CHEBI:57966; EC=3.4.13.20;
CC Evidence={ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:24891507};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59361;
CC Evidence={ECO:0000305|PubMed:12473676, ECO:0000305|PubMed:24891507};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=anserine + H2O = beta-alanine + N(pros)-methyl-L-histidine;
CC Xref=Rhea:RHEA:59576, ChEBI:CHEBI:15377, ChEBI:CHEBI:57966,
CC ChEBI:CHEBI:58445, ChEBI:CHEBI:143076; EC=3.4.13.20;
CC Evidence={ECO:0000269|PubMed:12473676};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59577;
CC Evidence={ECO:0000305|PubMed:12473676};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanyl-L-histidine = L-alanine + L-histidine;
CC Xref=Rhea:RHEA:37283, ChEBI:CHEBI:15377, ChEBI:CHEBI:57595,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:74388;
CC Evidence={ECO:0000269|PubMed:12473676};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37284;
CC Evidence={ECO:0000305|PubMed:12473676};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-L-histidine + H2O = glycine + L-histidine;
CC Xref=Rhea:RHEA:67376, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57595, ChEBI:CHEBI:169956;
CC Evidence={ECO:0000269|PubMed:12473676};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67377;
CC Evidence={ECO:0000305|PubMed:12473676};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-homocarnosine = 4-aminobutanoate + L-histidine;
CC Xref=Rhea:RHEA:59572, ChEBI:CHEBI:15377, ChEBI:CHEBI:57595,
CC ChEBI:CHEBI:59888, ChEBI:CHEBI:143075; EC=3.4.13.20;
CC Evidence={ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:24891507};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59573;
CC Evidence={ECO:0000305|PubMed:12473676, ECO:0000305|PubMed:24891507};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|Ref.11};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|Ref.11};
CC -!- ACTIVITY REGULATION: Activated by cadmium ions (PubMed:12473676).
CC Inhibited by the metal chelator 1,10-o-phenantrolin. The inhibitory
CC concentration 50% (IC(50)) is 5 uM. {ECO:0000269|PubMed:12473676}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.27 uM for carnosine (at 30 degrees Celsius and in the absence of
CC cadmium ions) {ECO:0000269|PubMed:12473676};
CC KM=11.00 uM for carnosine (at 30 degrees Celsius and in the presence
CC of 200 uM cadmium ions) {ECO:0000269|PubMed:12473676};
CC KM=0.13 mM for carnosine {ECO:0000269|PubMed:24891507};
CC KM=0.20 uM for homocarnosine (at 30 degrees Celsius and in the
CC absence of cadmium ions) {ECO:0000269|PubMed:12473676};
CC KM=1.0 uM for homocarnosine (at 30 degrees Celsius and in the
CC presence of 200 uM cadmium ions) {ECO:0000269|PubMed:12473676};
CC KM=8.7 mM for homocarnosine {ECO:0000269|PubMed:24891507};
CC Vmax=8.5 umol/min/mg enzyme toward carnosine
CC {ECO:0000269|PubMed:24891507};
CC Vmax=0.36 umol/min/mg enzyme toward homocarnosine
CC {ECO:0000269|PubMed:24891507};
CC Note=1 hour incubation in 50 mM Tris-HCl, pH 7.5.;
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:12473676};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.11}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12473676}.
CC -!- TISSUE SPECIFICITY: Found in serum and adult nervous central system.
CC Absent in serum from patients with homocarnosinosis.
CC {ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:6616870}.
CC -!- POLYMORPHISM: The number of trinucleotide (CTG) repeat varies among
CC different alleles leading to insertion of Leu residues in the signal
CC peptide. The allele with 5 leucines (as shown in the reference entry)
CC is known as the Mannheim allele. Diabetic patients with the CNDP1
CC Mannheim allele are less susceptible for nephropathy.
CC {ECO:0000269|PubMed:16046297}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AJ417564; CAD10388.1; -; mRNA.
DR EMBL; AY358756; AAQ89116.1; -; mRNA.
DR EMBL; BC004271; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC110295; AAI10296.1; -; mRNA.
DR EMBL; BC113512; AAI13513.1; -; mRNA.
DR EMBL; BC117122; AAI17123.1; -; mRNA.
DR CCDS; CCDS12007.1; -.
DR RefSeq; NP_116038.4; NM_032649.5.
DR PDB; 3DLJ; X-ray; 2.26 A; A/B=27-507.
DR PDBsum; 3DLJ; -.
DR AlphaFoldDB; Q96KN2; -.
DR BioGRID; 124230; 17.
DR IntAct; Q96KN2; 12.
DR STRING; 9606.ENSP00000351682; -.
DR MEROPS; M20.006; -.
DR GlyConnect; 1035; 16 N-Linked glycans (1 site).
DR GlyGen; Q96KN2; 4 sites, 18 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR iPTMnet; Q96KN2; -.
DR PhosphoSitePlus; Q96KN2; -.
DR BioMuta; CNDP1; -.
DR DMDM; 317373563; -.
DR CPTAC; CPTAC-1484; -.
DR jPOST; Q96KN2; -.
DR MassIVE; Q96KN2; -.
DR PaxDb; Q96KN2; -.
DR PeptideAtlas; Q96KN2; -.
DR PRIDE; Q96KN2; -.
DR ProteomicsDB; 77085; -.
DR Antibodypedia; 2197; 396 antibodies from 32 providers.
DR DNASU; 84735; -.
DR Ensembl; ENST00000358821.8; ENSP00000351682.3; ENSG00000150656.15.
DR GeneID; 84735; -.
DR KEGG; hsa:84735; -.
DR MANE-Select; ENST00000358821.8; ENSP00000351682.3; NM_032649.6; NP_116038.4.
DR UCSC; uc002llq.5; human.
DR CTD; 84735; -.
DR DisGeNET; 84735; -.
DR GeneCards; CNDP1; -.
DR HGNC; HGNC:20675; CNDP1.
DR HPA; ENSG00000150656; Tissue enriched (brain).
DR MIM; 609064; gene.
DR neXtProt; NX_Q96KN2; -.
DR OpenTargets; ENSG00000150656; -.
DR PharmGKB; PA134907547; -.
DR VEuPathDB; HostDB:ENSG00000150656; -.
DR eggNOG; KOG2276; Eukaryota.
DR GeneTree; ENSGT00940000160484; -.
DR InParanoid; Q96KN2; -.
DR OrthoDB; 733473at2759; -.
DR PhylomeDB; Q96KN2; -.
DR TreeFam; TF300633; -.
DR BioCyc; MetaCyc:HS07681-MON; -.
DR BRENDA; 3.4.13.20; 2681.
DR PathwayCommons; Q96KN2; -.
DR SABIO-RK; Q96KN2; -.
DR SignaLink; Q96KN2; -.
DR BioGRID-ORCS; 84735; 5 hits in 1065 CRISPR screens.
DR EvolutionaryTrace; Q96KN2; -.
DR GeneWiki; CNDP1; -.
DR GenomeRNAi; 84735; -.
DR Pharos; Q96KN2; Tbio.
DR PRO; PR:Q96KN2; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q96KN2; protein.
DR Bgee; ENSG00000150656; Expressed in inferior vagus X ganglion and 122 other tissues.
DR ExpressionAtlas; Q96KN2; baseline and differential.
DR Genevisible; Q96KN2; HS.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016805; F:dipeptidase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IDA:MGI.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR017153; CNDP/DUG1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Reference proteome; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..507
FT /note="Beta-Ala-His dipeptidase"
FT /id="PRO_0000026809"
FT ACT_SITE 134
FT /evidence="ECO:0000250"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 478
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.11"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HG3"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT VARIANT 6
FT /note="G -> R (in dbSNP:rs11151964)"
FT /id="VAR_027147"
FT VARIANT 20
FT /note="L -> LL"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16046297"
FT /id="VAR_027148"
FT VARIANT 113
FT /note="V -> I (in dbSNP:rs4263028)"
FT /id="VAR_027149"
FT MUTAGEN 132
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12473676"
FT MUTAGEN 165
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12473676"
FT MUTAGEN 200
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12473676"
FT CONFLICT 155
FT /note="D -> G (in Ref. 1; CAD10388 and 5; AAI10296)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="P -> L (in Ref. 1; CAD10388)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="P -> L (in Ref. 1; CAD10388)"
FT /evidence="ECO:0000305"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 68..87
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3DLJ"
FT TURN 161..166
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3DLJ"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:3DLJ"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:3DLJ"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:3DLJ"
FT TURN 293..298
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 304..311
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 346..355
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 367..377
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 383..399
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 404..415
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:3DLJ"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:3DLJ"
FT HELIX 486..504
FT /evidence="ECO:0007829|PDB:3DLJ"
SQ SEQUENCE 507 AA; 56692 MW; F3B51A9123C927C0 CRC64;
MDPKLGRMAA SLLAVLLLLL ERGMFSSPSP PPALLEKVFQ YIDLHQDEFV QTLKEWVAIE
SDSVQPVPRF RQELFRMMAV AADTLQRLGA RVASVDMGPQ QLPDGQSLPI PPVILAELGS
DPTKGTVCFY GHLDVQPADR GDGWLTDPYV LTEVDGKLYG RGATDNKGPV LAWINAVSAF
RALEQDLPVN IKFIIEGMEE AGSVALEELV EKEKDRFFSG VDYIVISDNL WISQRKPAIT
YGTRGNSYFM VEVKCRDQDF HSGTFGGILH EPMADLVALL GSLVDSSGHI LVPGIYDEVV
PLTEEEINTY KAIHLDLEEY RNSSRVEKFL FDTKEEILMH LWRYPSLSIH GIEGAFDEPG
TKTVIPGRVI GKFSIRLVPH MNVSAVEKQV TRHLEDVFSK RNSSNKMVVS MTLGLHPWIA
NIDDTQYLAA KRAIRTVFGT EPDMIRDGST IPIAKMFQEI VHKSVVLIPL GAVDDGEHSQ
NEKINRWNYI EGTKLFAAFF LEMAQLH
