ID IDE_RAT Reviewed; 1019 AA. AC P35559; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 02-SEP-2026, entry version 191. DE RecName: Full=Insulin-degrading enzyme; DE EC=3.4.24.56 {ECO:0000269|PubMed:10684867, ECO:0000269|PubMed:1445854, ECO:0000269|PubMed:14527953, ECO:0000269|PubMed:1836994, ECO:0000269|PubMed:21731629, ECO:0000269|PubMed:22049080}; DE AltName: Full=Insulin protease; DE Short=Insulinase; DE AltName: Full=Insulysin {ECO:0000303|PubMed:21731629}; GN Name=Ide; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Brain; RX PubMed=8425612; DOI=10.1016/0014-5793(93)81286-9; RA Baumeister H., Mueller D., Rehbein M., Richter D.; RT "The rat insulin-degrading enzyme. Molecular cloning and characterization RT of tissue-specific transcripts."; RL FEBS Lett. 317:250-254(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 898-995. RC STRAIN=Sprague-Dawley; RX PubMed=7678795; DOI=10.1210/endo.132.2.7678795; RA Kuo W.L., Montag A.G., Rosner M.R.; RT "Insulin-degrading enzyme is differentially expressed and developmentally RT regulated in various rat tissues."; RL Endocrinology 132:604-611(1993). RN [3] RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY ON ANP, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=1836994; DOI=10.1111/j.1432-1033.1991.tb16374.x; RA Mueller D., Baumeister H., Buck F., Richter D.; RT "Atrial natriuretic peptide (ANP) is a high-affinity substrate for rat RT insulin-degrading enzyme."; RL Eur. J. Biochem. 202:285-292(1991). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY ON ANP; BNP AND CNP. RX PubMed=1445854; DOI=10.1021/bi00160a026; RA Mueller D., Schulze C., Baumeister H., Buck F., Richter D.; RT "Rat insulin-degrading enzyme: cleavage pattern of the natriuretic peptide RT hormones ANP, BNP, and CNP revealed by HPLC and mass spectrometry."; RL Biochemistry 31:11138-11143(1992). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=10684867; DOI=10.1523/jneurosci.20-05-01657.2000; RA Vekrellis K., Ye Z., Qiu W.Q., Walsh D., Hartley D., Chesneau V., RA Rosner M.R., Selkoe D.J.; RT "Neurons regulate extracellular levels of amyloid beta-protein via RT proteolysis by insulin-degrading enzyme."; RL J. Neurosci. 20:1657-1665(2000). RN [6] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=12941771; DOI=10.2337/diabetes.52.9.2315; RA Bennett R.G., Hamel F.G., Duckworth W.C.; RT "An insulin-degrading enzyme inhibitor decreases amylin degradation, RT increases amylin-induced cytotoxicity, and increases amyloid formation in RT insulinoma cell cultures."; RL Diabetes 52:2315-2320(2003). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS RP OF GLU-111 AND HIS-112. RX PubMed=14527953; DOI=10.1074/jbc.m308983200; RA Song E.S., Juliano M.A., Juliano L., Hersh L.B.; RT "Substrate activation of insulin-degrading enzyme (insulysin). A potential RT target for drug development."; RL J. Biol. Chem. 278:49789-49794(2003). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 42-1019 OF WILD TYPE AND MUTANT RP PHE-111, CATALYTIC ACTIVITY, COFACTOR, ZINC-BINDING SITES, ACTIVITY RP REGULATION, ALLOSTERIC REGULATION, AND MUTAGENESIS OF GLU-111; VAL-360; RP ILE-374 AND TYR-609. RX PubMed=21731629; DOI=10.1371/journal.pone.0020864; RA Noinaj N., Bhasin S.K., Song E.S., Scoggin K.E., Juliano M.A., Juliano L., RA Hersh L.B., Rodgers D.W.; RT "Identification of the allosteric regulatory site of insulysin."; RL PLoS ONE 6:E20864-E20864(2011). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS), ATP-BINDING SITE, FUNCTION, RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF ARG-429; RP LYS-898; LYS-899 AND SER-901. RX PubMed=22049080; DOI=10.1074/jbc.m111.264614; RA Noinaj N., Song E.S., Bhasin S., Alper B.J., Schmidt W.K., Hersh L.B., RA Rodgers D.W.; RT "Anion activation site of insulin-degrading enzyme."; RL J. Biol. Chem. 287:48-57(2012). CC -!- FUNCTION: Plays a role in the cellular breakdown of insulin, APP CC peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, CC kallidin, and other peptides, and thereby plays a role in intercellular CC peptide signaling (PubMed:10684867, PubMed:12941771, PubMed:1445854, CC PubMed:14527953, PubMed:1836994, PubMed:22049080). Substrate binding CC induces important conformation changes, making it possible to bind and CC degrade larger substrates, such as insulin (By similarity). Contributes CC to the regulation of peptide hormone signaling cascades and regulation CC of blood glucose homeostasis via its role in the degradation of CC insulin, glucagon and IAPP (By similarity). Plays a role in the CC degradation and clearance of APP-derived amyloidogenic peptides that CC are secreted by neurons and microglia (PubMed:10684867). Degrades the CC natriuretic peptides ANP, BNP and CNP, inactivating their ability to CC raise intracellular cGMP (By similarity). Also degrades an aberrant CC frameshifted 40-residue form of NPPA (fsNPPA) which is associated with CC familial atrial fibrillation in heterozygous patients (By similarity). CC Involved in antigen processing. Produces both the N terminus and the C CC terminus of MAGEA3-derived antigenic peptide (EVDPIGHLY) that is CC presented to cytotoxic T lymphocytes by MHC class I. CC {ECO:0000250|UniProtKB:P14735, ECO:0000250|UniProtKB:Q9JHR7, CC ECO:0000269|PubMed:10684867, ECO:0000269|PubMed:12941771, CC ECO:0000269|PubMed:1445854, ECO:0000269|PubMed:14527953, CC ECO:0000269|PubMed:1836994, ECO:0000269|PubMed:22049080}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Degradation of insulin, glucagon and other polypeptides. No CC action on proteins.; EC=3.4.24.56; CC Evidence={ECO:0000269|PubMed:10684867, ECO:0000269|PubMed:1445854, CC ECO:0000269|PubMed:14527953, ECO:0000269|PubMed:1836994, CC ECO:0000269|PubMed:21731629, ECO:0000269|PubMed:22049080}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:21731629}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21731629}; CC -!- ACTIVITY REGULATION: Activated by ATP, other nucleotide triphosphates CC and small peptides (PubMed:14527953, PubMed:21731629, PubMed:22049080). CC Inhibited by bacitracin (PubMed:12941771). CC {ECO:0000269|PubMed:12941771, ECO:0000269|PubMed:14527953, CC ECO:0000269|PubMed:21731629, ECO:0000269|PubMed:22049080}. CC -!- SUBUNIT: Homodimer. Can also form homotetramers. CC {ECO:0000269|PubMed:14527953}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10684867, CC ECO:0000269|PubMed:1836994}. Cell membrane CC {ECO:0000269|PubMed:10684867}. Secreted {ECO:0000269|PubMed:10684867}. CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level). CC {ECO:0000269|PubMed:1836994}. CC -!- DOMAIN: The SlyX motif may be involved in the non-conventional CC secretion of the protein. {ECO:0000250|UniProtKB:Q9JHR7}. CC -!- MISCELLANEOUS: ATP-binding induces a conformation change. CC {ECO:0000250|UniProtKB:P14735}. CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X67269; CAA47689.1; -; mRNA. DR EMBL; S53721; AAB25205.1; -; mRNA. DR PIR; S29509; S29509. DR RefSeq; NP_037291.1; NM_013159.2. DR PDB; 3P7L; X-ray; 2.08 A; A=42-1019. DR PDB; 3P7O; X-ray; 2.14 A; A=1-1019. DR PDB; 3TUV; X-ray; 2.27 A; A=1-1019. DR AlphaFoldDB; P35559; -. DR SMR; P35559; -. DR BioGRID; 247729; 3. DR FunCoup; P35559; 3285. DR IntAct; P35559; 1. DR STRING; 10116.ENSRNOP00000023342; -. DR MEROPS; M16.002; -. DR iPTMnet; P35559; -. DR PhosphoSitePlus; P35559; -. DR jPOST; P35559; -. DR PaxDb; 10116-ENSRNOP00000023342; -. DR Ensembl; ENSRNOT00000085303.3; ENSRNOP00000074304.3; ENSRNOG00000016833.9. DR Ensembl; ENSRNOT00055047407; ENSRNOP00055038987; ENSRNOG00055027358. DR Ensembl; ENSRNOT00065048381; ENSRNOP00065039691; ENSRNOG00065028018. DR GeneID; 25700; -. DR KEGG; rno:25700; -. DR UCSC; RGD:2861; rat. DR AGR; RGD:2861; -. DR CTD; 3416; -. DR RGD; 2861; Ide. DR VEuPathDB; HostDB:ENSRNOG00000016833; -. DR eggNOG; KOG0959; Eukaryota. DR GeneTree; ENSGT00940000155780; -. DR InParanoid; P35559; -. DR PhylomeDB; P35559; -. DR BRENDA; 3.4.24.56; 5301. DR Reactome; R-RNO-5689880; Ub-specific processing proteases. DR Reactome; R-RNO-77387; Insulin receptor recycling. DR Reactome; R-RNO-9033241; Peroxisomal protein import. DR SABIO-RK; P35559; -. DR EvolutionaryTrace; P35559; -. DR PRO; PR:P35559; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000016833; Expressed in esophagus and 20 other cell types or tissues. DR ExpressionAtlas; P35559; baseline and differential. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD. DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0031597; C:cytosolic proteasome complex; IDA:RGD. DR GO; GO:0031904; C:endosome lumen; ISO:RGD. DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD. DR GO; GO:0070062; C:extracellular exosome; ISO:RGD. DR GO; GO:0005576; C:extracellular region; IDA:ARUK-UCL. DR GO; GO:0005739; C:mitochondrion; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0005782; C:peroxisomal matrix; IDA:RGD. DR GO; GO:0005777; C:peroxisome; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0001540; F:amyloid-beta binding; IPI:RGD. DR GO; GO:0005524; F:ATP binding; IMP:RGD. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:RGD. DR GO; GO:0031626; F:beta-endorphin binding; IMP:RGD. DR GO; GO:0004175; F:endopeptidase activity; ISO:RGD. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0043559; F:insulin binding; IMP:RGD. DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:RGD. DR GO; GO:0008233; F:peptidase activity; TAS:RGD. DR GO; GO:0042277; F:peptide binding; ISO:RGD. DR GO; GO:0017046; F:peptide hormone binding; IPI:RGD. DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD. DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD. DR GO; GO:0008270; F:zinc ion binding; IMP:RGD. DR GO; GO:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL. DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IMP:ARUK-UCL. DR GO; GO:0050435; P:amyloid-beta metabolic process; IMP:RGD. DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; ISS:UniProtKB. DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB. DR GO; GO:0042447; P:hormone catabolic process; IDA:RGD. DR GO; GO:1901143; P:insulin catabolic process; ISS:UniProtKB. DR GO; GO:1901142; P:insulin metabolic process; ISO:RGD. DR GO; GO:0038020; P:insulin receptor recycling; ISO:RGD. DR GO; GO:0045861; P:negative regulation of proteolysis; IDA:RGD. DR GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB. DR GO; GO:0030163; P:protein catabolic process; IDA:RGD. DR GO; GO:0006508; P:proteolysis; ISO:RGD. DR GO; GO:1903715; P:regulation of aerobic respiration; ISO:RGD. DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD. DR GO; GO:0010992; P:ubiquitin recycling; ISO:RGD. DR FunFam; 3.30.830.10:FF:000003; Insulin-degrading enzyme; 1. DR FunFam; 3.30.830.10:FF:000007; Insulin-degrading enzyme; 1. DR FunFam; 3.30.830.10:FF:000004; Putative insulin-degrading enzyme; 1. DR FunFam; 3.30.830.10:FF:000006; Putative insulin-degrading enzyme; 1. DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4. DR InterPro; IPR011249; Metalloenz_LuxS/M16. DR InterPro; IPR011765; Pept_M16_N. DR InterPro; IPR001431; Pept_M16_Zn_BS. DR InterPro; IPR050626; Peptidase_M16. DR InterPro; IPR007863; Peptidase_M16_C. DR InterPro; IPR032632; Peptidase_M16_M. DR InterPro; IPR054734; PqqF-like_C_4. DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1. DR PANTHER; PTHR43690; NARDILYSIN; 1. DR Pfam; PF00675; Peptidase_M16; 1. DR Pfam; PF05193; Peptidase_M16_C; 1. DR Pfam; PF16187; Peptidase_M16_M; 1. DR Pfam; PF22456; PqqF-like_C_4; 1. DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4. DR PROSITE; PS00143; INSULINASE; 1. DR PDBsum; 3P7L; -. DR PDBsum; 3P7O; -. DR PDBsum; 3TUV; -. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; ATP-binding; Cell membrane; Cytoplasm; KW Direct protein sequencing; Hydrolase; Membrane; Metal-binding; KW Metalloprotease; Nucleotide-binding; Protease; Reference proteome; KW Secreted; Zinc. FT CHAIN 1..1019 FT /note="Insulin-degrading enzyme" FT /id="PRO_0000074406" FT MOTIF 853..858 FT /note="SlyX motif" FT /evidence="ECO:0000250|UniProtKB:Q9JHR7" FT ACT_SITE 111 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096" FT BINDING 108 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:21731629, FT ECO:0007744|PDB:3P7L" FT BINDING 112 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:21731629, FT ECO:0007744|PDB:3P7L" FT BINDING 189 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:21731629, FT ECO:0007744|PDB:3P7L" FT BINDING 359..363 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P14735" FT BINDING 429 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:22049080, FT ECO:0007744|PDB:3TUV" FT BINDING 895..901 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:22049080, FT ECO:0007744|PDB:3TUV" FT MOD_RES 192 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9JHR7" FT MOD_RES 697 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9JHR7" FT MUTAGEN 111 FT /note="E->F: Expected to abolish catalytic activity." FT /evidence="ECO:0000269|PubMed:21731629" FT MUTAGEN 111 FT /note="E->V: Abolishes catalytic activity. No effect on FT substrate binding." FT /evidence="ECO:0000269|PubMed:14527953" FT MUTAGEN 112 FT /note="H->Q: Abolishes catalytic activity. Decreases FT substrate binding affinity." FT /evidence="ECO:0000269|PubMed:14527953" FT MUTAGEN 360 FT /note="V->S: Strongly reduced catalytic activity. Strongly FT reduced stimulation of activity by ATP." FT /evidence="ECO:0000269|PubMed:21731629" FT MUTAGEN 374 FT /note="I->S: Strongly reduced catalytic activity. Abolishes FT stimulation of activity by ATP." FT /evidence="ECO:0000269|PubMed:21731629" FT MUTAGEN 429 FT /note="R->S: Greatly decreased activation by polyphosphate FT anions." FT /evidence="ECO:0000269|PubMed:22049080" FT MUTAGEN 609 FT /note="Y->F: Strongly reduced catalytic activity. Abolishes FT stimulation of activity by ATP." FT /evidence="ECO:0000269|PubMed:21731629" FT MUTAGEN 898 FT /note="K->A: Greatly decreased activation by polyphosphate FT anions, and deficient in activation by small peptides; when FT associated with A-899 and A-901." FT /evidence="ECO:0000269|PubMed:22049080" FT MUTAGEN 899 FT /note="K->A: Greatly decreased activation by polyphosphate FT anions, and deficient in activation by small peptides; when FT associated with A-898 and A-901." FT /evidence="ECO:0000269|PubMed:22049080" FT MUTAGEN 901 FT /note="S->A: Greatly decreased activation by polyphosphate FT anions, and deficient in activation by small peptides; when FT associated with A-898 and A-899." FT /evidence="ECO:0000269|PubMed:22049080" FT STRAND 47..51 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 63..69 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 84..93 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:3P7O" FT HELIX 106..114 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 126..132 FT /evidence="ECO:0007829|PDB:3P7L" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 137..142 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 147..154 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 158..166 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 176..194 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 197..206 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:3TUV" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 224..228 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 229..232 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 237..248 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 254..262 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 264..275 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 283..286 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 298..305 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:3TUV" FT STRAND 312..320 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 323..325 FT /evidence="ECO:0007829|PDB:3P7L" FT TURN 326..328 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 330..338 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 346..352 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 355..367 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 370..379 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 381..385 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 387..404 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 408..423 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 425..429 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 430..440 FT /evidence="ECO:0007829|PDB:3P7L" FT TURN 441..443 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 446..448 FT /evidence="ECO:0007829|PDB:3P7L" FT TURN 449..454 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 461..470 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 473..475 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 477..481 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 483..485 FT /evidence="ECO:0007829|PDB:3P7L" FT TURN 494..496 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 499..504 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 507..514 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 523..526 FT /evidence="ECO:0007829|PDB:3P7O" FT HELIX 536..541 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 549..553 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 555..563 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 570..579 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 581..583 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 584..586 FT /evidence="ECO:0007829|PDB:3P7O" FT HELIX 587..613 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 616..622 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 624..635 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 638..650 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 656..672 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 673..675 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 678..690 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 691..693 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 697..704 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 709..721 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 722..732 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 735..753 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 760..762 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 763..767 FT /evidence="ECO:0007829|PDB:3P7O" FT STRAND 775..782 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 787..799 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 802..819 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 820..826 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 833..840 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 843..854 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 856..875 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 879..894 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 900..912 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 920..929 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 933..939 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 940..944 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 952..959 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 981..985 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 987..989 FT /evidence="ECO:0007829|PDB:3P7L" FT STRAND 990..993 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 995..1000 FT /evidence="ECO:0007829|PDB:3P7L" FT HELIX 1007..1009 FT /evidence="ECO:0007829|PDB:3P7L" SQ SEQUENCE 1019 AA; 117710 MW; 9DB297A7F1877CEC CRC64; MRNGLVWLLH PALPSTLHSI LGARPPPVKR LCGFPKQIYS TMNNPAIQRI EDHIVKSPED KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIPGLSHFC EHMLFLGTKK YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLFDASCKD REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVREE LLKFHSTYYS SNLMAICVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ LYKIVPIKDI RNLYVTFPIP DLQQYYKSNP GHYLGHLIGH EGPGSLLSEL KSKGWVNTLV GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV AFRFKDKERP RGYTSKIAGK LHYYPLNGVL TAEYLLEEFR PDLIDMVLDK LRPENVRVAI VSKSFEGKTD RTEQWYGTQY KQEAIPEDVI QKWQNADLNG KFKLPTKNEF IPTNFEILAL EKDATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKITEKMA TFEIDKKRFE IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL SRLHIEALLH GNITKQAALG VMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ RRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKAIEDMTEE AFQKHIQALA IRRLDKPKKL SAECAKYWGE IISQQYNYDR DNIEVAYLKT LSKDDIIKFY KEMLAVDAPR RHKVSVHVLA REMDSCPVVG EFPSQNDINL SEAPPLPQPE VIHNMTEFKR GLPLFPLVKP HINFMAAKL //