PPCE_HUMAN
ID PPCE_HUMAN Reviewed; 710 AA.
AC P48147; Q8N6D4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Prolyl endopeptidase;
DE Short=PE;
DE EC=3.4.21.26;
DE AltName: Full=Post-proline cleaving enzyme;
GN Name=PREP; Synonyms=PEP;
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=Blood;
RX PubMed=7959018; DOI=10.1016/0378-1119(94)90177-5;
RA Vanhoof G., Goossens F., Hendriks L., De Meester I., Hendriks D.,
RA Vriend G., van Broeckhoven C., Scharpe S.;
RT "Cloning and sequence analysis of the gene encoding human lymphocyte prolyl
RT endopeptidase.";
RL Gene 149:363-366(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-706.
RX PubMed=8089089; DOI=10.1093/oxfordjournals.jbchem.a124402;
RA Shirasawa Y., Osawa T., Hirashima A.;
RT "Molecular cloning and characterization of prolyl endopeptidase from human
RT T cells.";
RL J. Biochem. 115:724-729(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tarrago T., Giralt E.;
RT "cDNA cloning and recombinant expression of human brain prolyl
RT oligopeptidase.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 136-149, SUBUNIT, AND CHARACTERIZATION.
RC TISSUE=Lymphocyte;
RX PubMed=7588785; DOI=10.1111/j.1432-1033.1995.432_2.x;
RA Goossens F., De Meester I., Vanhoof G., Hendriks D., Vriend G., Scharpe S.;
RT "The purification, characterization and analysis of primary and secondary-
RT structure of prolyl oligopeptidase from human lymphocytes. Evidence that
RT the enzyme belongs to the alpha/beta hydrolase fold family.";
RL Eur. J. Biochem. 233:432-441(1995).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 2-710 IN COMPLEX WITH INHIBITOR.
RX PubMed=18606544; DOI=10.1016/j.bmcl.2008.06.067;
RA Haffner C.D., Diaz C.J., Miller A.B., Reid R.A., Madauss K.P., Hassell A.,
RA Hanlon M.H., Porter D.J., Becherer J.D., Carter L.H.;
RT "Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of
RT prolyl oligopeptidase (POP).";
RL Bioorg. Med. Chem. Lett. 18:4360-4363(2008).
CC -!- FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl
CC residues within peptides that are up to approximately 30 amino acids
CC long.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18606544,
CC ECO:0000269|PubMed:7588785}.
CC -!- INTERACTION:
CC P48147; P04406: GAPDH; NbExp=5; IntAct=EBI-1049962, EBI-354056;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR EMBL; X74496; CAA52605.1; -; mRNA.
DR EMBL; D21102; BAA04661.1; -; mRNA.
DR EMBL; AY660966; AAV70495.1; -; mRNA.
DR EMBL; AL590871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48426.1; -; Genomic_DNA.
DR EMBL; BC030636; AAH30636.1; -; mRNA.
DR CCDS; CCDS5053.1; -.
DR PIR; I38134; I38134.
DR PIR; JC2257; JC2257.
DR RefSeq; NP_002717.3; NM_002726.4.
DR PDB; 3DDU; X-ray; 1.56 A; A=2-710.
DR PDBsum; 3DDU; -.
DR AlphaFoldDB; P48147; -.
DR SMR; P48147; -.
DR BioGRID; 111541; 41.
DR IntAct; P48147; 10.
DR STRING; 9606.ENSP00000358106; -.
DR BindingDB; P48147; -.
DR ChEMBL; CHEMBL3202; -.
DR DrugBank; DB07148; (6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)pyrrolo[1,2-a]pyrazin-4(6H)-one.
DR DrugBank; DB01684; 1-Hydroxy-1-Thio-Glycerol.
DR DrugBank; DB08738; 1-{3-oxo-3-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]propyl}-3-phenylquinoxalin-2(1H)-one.
DR DrugBank; DB08739; 2-{3-[(2S)-4,4-difluoro-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-3-oxopropyl}-isoindole-1,3(2H)-dione.
DR DrugBank; DB03864; Monothioglycerol.
DR DrugBank; DB00107; Oxytocin.
DR DrugBank; DB03382; S-oxy-L-cysteine.
DR DrugBank; DB03535; Z-Pro-Prolinal.
DR DrugCentral; P48147; -.
DR GuidetoPHARMACOLOGY; 2395; -.
DR ESTHER; human-PREP; S9N_PPCE_Peptidase_S9.
DR MEROPS; S09.001; -.
DR GlyGen; P48147; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P48147; -.
DR MetOSite; P48147; -.
DR PhosphoSitePlus; P48147; -.
DR SwissPalm; P48147; -.
DR BioMuta; PREP; -.
DR DMDM; 215273868; -.
DR EPD; P48147; -.
DR jPOST; P48147; -.
DR MassIVE; P48147; -.
DR MaxQB; P48147; -.
DR PaxDb; P48147; -.
DR PeptideAtlas; P48147; -.
DR PRIDE; P48147; -.
DR ProteomicsDB; 55866; -.
DR Antibodypedia; 32113; 218 antibodies from 33 providers.
DR DNASU; 5550; -.
DR Ensembl; ENST00000652536.2; ENSP00000499089.1; ENSG00000085377.15.
DR GeneID; 5550; -.
DR KEGG; hsa:5550; -.
DR MANE-Select; ENST00000652536.2; ENSP00000499089.1; NM_002726.5; NP_002717.3.
DR UCSC; uc003prc.4; human.
DR CTD; 5550; -.
DR DisGeNET; 5550; -.
DR GeneCards; PREP; -.
DR HGNC; HGNC:9358; PREP.
DR HPA; ENSG00000085377; Tissue enhanced (skeletal).
DR MIM; 600400; gene.
DR neXtProt; NX_P48147; -.
DR OpenTargets; ENSG00000085377; -.
DR PharmGKB; PA33730; -.
DR VEuPathDB; HostDB:ENSG00000085377; -.
DR eggNOG; KOG2237; Eukaryota.
DR GeneTree; ENSGT00530000063426; -.
DR HOGENOM; CLU_011290_1_1_1; -.
DR InParanoid; P48147; -.
DR OMA; ACMTQRP; -.
DR OrthoDB; 225446at2759; -.
DR PhylomeDB; P48147; -.
DR TreeFam; TF300655; -.
DR BRENDA; 3.4.21.26; 2681.
DR PathwayCommons; P48147; -.
DR SignaLink; P48147; -.
DR BioGRID-ORCS; 5550; 10 hits in 1087 CRISPR screens.
DR ChiTaRS; PREP; human.
DR EvolutionaryTrace; P48147; -.
DR GeneWiki; Prolyl_endopeptidase; -.
DR GenomeRNAi; 5550; -.
DR Pharos; P48147; Tchem.
DR PRO; PR:P48147; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P48147; protein.
DR Bgee; ENSG00000085377; Expressed in secondary oocyte and 182 other tissues.
DR ExpressionAtlas; P48147; baseline and differential.
DR Genevisible; P48147; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0070012; F:oligopeptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Protease; Reference proteome; Serine protease.
FT CHAIN 1..710
FT /note="Prolyl endopeptidase"
FT /id="PRO_0000122401"
FT ACT_SITE 554
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 641
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 680
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 157
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 351
FT /note="L -> V (in dbSNP:rs12192054)"
FT /id="VAR_047790"
FT VARIANT 706
FT /note="V -> I (in dbSNP:rs1051484)"
FT /evidence="ECO:0000269|PubMed:8089089"
FT /id="VAR_047791"
FT CONFLICT 4
FT /note="L -> F (in Ref. 1; CAA52605 and 2; BAA04661)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="V -> I (in Ref. 2; BAA04661)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="R -> C (in Ref. 2; BAA04661)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="T -> A (in Ref. 2; BAA04661)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="R -> W (in Ref. 1; CAA52605)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="I -> L (in Ref. 2; BAA04661)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="G -> S (in Ref. 2; BAA04661)"
FT /evidence="ECO:0000305"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 37..55
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3DDU"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 246..257
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:3DDU"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 358..365
FT /evidence="ECO:0007829|PDB:3DDU"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 392..399
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 435..443
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 449..457
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 486..495
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 511..516
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 524..539
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 548..553
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 555..566
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 572..578
FT /evidence="ECO:0007829|PDB:3DDU"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 592..595
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 596..599
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 605..614
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 632..638
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 647..659
FT /evidence="ECO:0007829|PDB:3DDU"
FT TURN 660..662
FT /evidence="ECO:0007829|PDB:3DDU"
FT STRAND 670..677
FT /evidence="ECO:0007829|PDB:3DDU"
FT HELIX 686..704
FT /evidence="ECO:0007829|PDB:3DDU"
SQ SEQUENCE 710 AA; 80700 MW; 139072B990820B90 CRC64;
MLSLQYPDVY RDETAVQDYH GHKICDPYAW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR
GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVFLDPNILS
DDGTVALRGY AFSEDGEYFA YGLSASGSDW VTIKFMKVDG AKELPDVLER VKFSCMAWTH
DGKGMFYNSY PQQDGKSDGT ETSTNLHQKL YYHVLGTDQS EDILCAEFPD EPKWMGGAEL
SDDGRYVLLS IREGCDPVNR LWYCDLQQES SGIAGILKWV KLIDNFEGEY DYVTNEGTVF
TFKTNRQSPN YRVINIDFRD PEESKWKVLV PEHEKDVLEW IACVRSNFLV LCYLHDVKNI
LQLHDLTTGA LLKTFPLDVG SIVGYSGQKK DTEIFYQFTS FLSPGIIYHC DLTKEELEPR
VFREVTVKGI DASDYQTVQI FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI
TPNYSVSRLI FVRHMGGILA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE
GYTSPKRLTI NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKYT IGHAWTTDYG
CSDSKQHFEW LVKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL KFIATLQYIV
GRSRKQSNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI ARCLNVDWIP
