IDE_RAT
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 03-AUG-2022, entry version 174.
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:1836994, PubMed:1445854, PubMed:10684867,
CC PubMed:12941771, PubMed:14527953, 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}.
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DR EMBL; X67269; CAA47689.1; -; mRNA.
DR EMBL; S53721; AAB25205.1; -; mRNA.
DR PIR; S29509; S29509.
DR RefSeq; NP_037291.1; NM_013159.1.
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 PDBsum; 3P7L; -.
DR PDBsum; 3P7O; -.
DR PDBsum; 3TUV; -.
DR AlphaFoldDB; P35559; -.
DR SMR; P35559; -.
DR BioGRID; 247729; 3.
DR IntAct; P35559; 1.
DR STRING; 10116.ENSRNOP00000023342; -.
DR MEROPS; M16.002; -.
DR iPTMnet; P35559; -.
DR PhosphoSitePlus; P35559; -.
DR jPOST; P35559; -.
DR PaxDb; P35559; -.
DR PRIDE; P35559; -.
DR GeneID; 25700; -.
DR KEGG; rno:25700; -.
DR UCSC; RGD:2861; rat.
DR CTD; 3416; -.
DR RGD; 2861; Ide.
DR VEuPathDB; HostDB:ENSRNOG00000016833; -.
DR eggNOG; KOG0959; Eukaryota.
DR InParanoid; P35559; -.
DR OMA; WIFDEMK; -.
DR OrthoDB; 1008844at2759; -.
DR PhylomeDB; P35559; -.
DR TreeFam; TF106275; -.
DR BRENDA; 3.4.24.56; 5301.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
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 tissues.
DR ExpressionAtlas; P35559; baseline and differential.
DR Genevisible; P35559; RN.
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; IDA:RGD.
DR GO; GO:0031597; C:cytosolic proteasome complex; IDA: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:0005615; C:extracellular space; IDA:ARUK-UCL.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:RGD.
DR GO; GO:0005777; C:peroxisome; ISO:RGD.
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:0140036; F:ubiquitin-dependent protein binding; ISO: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:0008340; P:determination of adult lifespan; ISO:RGD.
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:0045861; P:negative regulation of proteolysis; IDA:RGD.
DR GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:0030163; P:protein catabolic process; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP: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 InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
DR PROSITE; PS00143; INSULINASE; 1.
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 223..226
FT /evidence="ECO:0007829|PDB:3P7L"
FT HELIX 228..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 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 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 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 STRAND 775..782
FT /evidence="ECO:0007829|PDB:3P7L"
FT STRAND 787..799
FT /evidence="ECO:0007829|PDB:3P7L"
FT HELIX 802..823
FT /evidence="ECO:0007829|PDB:3P7L"
FT TURN 824..827
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..943
FT /evidence="ECO:0007829|PDB:3P7L"
FT STRAND 952..959
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"
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
