CAN2_RAT
ID CAN2_RAT Reviewed; 700 AA.
AC Q07009;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Calpain-2 catalytic subunit;
DE EC=3.4.22.53;
DE AltName: Full=Calcium-activated neutral proteinase 2;
DE Short=CANP 2;
DE AltName: Full=Calpain M-type;
DE AltName: Full=Calpain-2 large subunit;
DE AltName: Full=Millimolar-calpain;
DE Short=M-calpain;
DE Flags: Precursor;
GN Name=Capn2;
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].
RX PubMed=8218419; DOI=10.1016/0167-4781(93)90040-k;
RA Deluca C.I., Davies P.L., Samis J.A., Elce J.S.;
RT "Molecular cloning and bacterial expression of cDNA for rat calpain II 80
RT kDa subunit.";
RL Biochim. Biophys. Acta 1216:81-93(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=11342050; DOI=10.1016/s0167-4838(00)00286-7;
RA Moldoveanu T., Hosfield C.M., Jia Z., Elce J.S., Davies P.L.;
RT "Ca(2+)-induced structural changes in rat m-calpain revealed by partial
RT proteolysis.";
RL Biochim. Biophys. Acta 1545:245-254(2001).
RN [4]
RP MUTAGENESIS OF LYS-230; LYS-234 AND GLU-504.
RX PubMed=11102442; DOI=10.1074/jbc.m007352200;
RA Hosfield C.M., Moldoveanu T., Davies P.L., Elce J.S., Jia Z.;
RT "Calpain mutants with increased Ca2+ sensitivity and implications for the
RT role of the C(2)-like domain.";
RL J. Biol. Chem. 276:7404-7407(2001).
RN [5]
RP ACTIVE SITE, AND MUTAGENESIS OF CYS-105; HIS-262; ASN-286 AND TRP-288.
RX PubMed=7635186; DOI=10.1016/0014-5793(95)00691-2;
RA Arthur J.S., Gauthier S., Elce J.S.;
RT "Active site residues in m-calpain: identification by site-directed
RT mutagenesis.";
RL FEBS Lett. 368:397-400(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=10601010; DOI=10.1093/emboj/18.24.6880;
RA Hosfield C.M., Elce J.S., Davies P.L., Jia Z.;
RT "Crystal structure of calpain reveals the structural basis for Ca(2+)-
RT dependent protease activity and a novel mode of enzyme activation.";
RL EMBO J. 18:6880-6889(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH CAPNS1 AND
RP CALPASTATIN, CALCIUM-BINDING SITES, SUBUNIT, AND MUTAGENESIS OF ARG-417;
RP ARG-420 AND ARG-469.
RX PubMed=19020622; DOI=10.1038/nature07353;
RA Moldoveanu T., Gehring K., Green D.R.;
RT "Concerted multi-pronged attack by calpastatin to occlude the catalytic
RT cleft of heterodimeric calpains.";
RL Nature 456:404-408(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT SER-105 IN COMPLEX WITH
RP CAPNS1 AND CALPASTATIN, CALCIUM-BINDING SITES, AND SUBUNIT.
RX PubMed=19020623; DOI=10.1038/nature07451;
RA Hanna R.A., Campbell R.L., Davies P.L.;
RT "Calcium-bound structure of calpain and its mechanism of inhibition by
RT calpastatin.";
RL Nature 456:409-412(2008).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze
CC limited proteolysis of substrates involved in cytoskeletal remodeling
CC and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'.
CC Proteolytically cleaves CPEB3 following neuronal stimulation which
CC abolishes CPEB3 translational repressor activity, leading to
CC translation of CPEB3 target mRNAs. {ECO:0000250|UniProtKB:O08529,
CC ECO:0000250|UniProtKB:P17655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase specificity.; EC=3.4.22.53;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 7 Ca(2+) ions.;
CC -!- ACTIVITY REGULATION: Activated by 200-1000 micromolar concentrations of
CC calcium and inhibited by calpastatin.
CC -!- SUBUNIT: Forms a heterodimer with a small (regulatory) subunit (CAPNS1)
CC (PubMed:19020622, PubMed:19020623). Interacts with CPEB3; this leads to
CC cleavage of CPEB3 (By similarity). {ECO:0000250|UniProtKB:O08529,
CC ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623}.
CC -!- INTERACTION:
CC Q07009; Q64537: Capns1; NbExp=8; IntAct=EBI-1040438, EBI-918712;
CC Q07009; P27321: Cast; NbExp=10; IntAct=EBI-1040438, EBI-7441624;
CC Q07009; G5EFH4: srp-6; Xeno; NbExp=2; IntAct=EBI-1040438, EBI-1549936;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Translocates to the plasma membrane upon Ca(2+)
CC binding. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; L09120; AAA16327.1; -; mRNA.
DR EMBL; BC065306; AAH65306.1; -; mRNA.
DR PIR; S38361; S38361.
DR RefSeq; NP_058812.1; NM_017116.2.
DR PDB; 1DF0; X-ray; 2.60 A; A=1-700.
DR PDB; 1MDW; X-ray; 1.95 A; A/B=19-346.
DR PDB; 1QXP; X-ray; 2.80 A; A/B=1-49, A/B=639-700.
DR PDB; 1U5I; X-ray; 2.86 A; A=1-700.
DR PDB; 3BOW; X-ray; 2.40 A; A=1-700.
DR PDB; 3DF0; X-ray; 2.95 A; A=1-700.
DR PDBsum; 1DF0; -.
DR PDBsum; 1MDW; -.
DR PDBsum; 1QXP; -.
DR PDBsum; 1U5I; -.
DR PDBsum; 3BOW; -.
DR PDBsum; 3DF0; -.
DR AlphaFoldDB; Q07009; -.
DR SMR; Q07009; -.
DR BioGRID; 247837; 3.
DR DIP; DIP-6139N; -.
DR IntAct; Q07009; 5.
DR MINT; Q07009; -.
DR STRING; 10116.ENSRNOP00000046509; -.
DR MEROPS; C02.002; -.
DR iPTMnet; Q07009; -.
DR PhosphoSitePlus; Q07009; -.
DR jPOST; Q07009; -.
DR PaxDb; Q07009; -.
DR PRIDE; Q07009; -.
DR Ensembl; ENSRNOT00000045326; ENSRNOP00000046509; ENSRNOG00000034015.
DR GeneID; 29154; -.
DR KEGG; rno:29154; -.
DR UCSC; RGD:2268; rat.
DR CTD; 824; -.
DR RGD; 2268; Capn2.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000154784; -.
DR HOGENOM; CLU_010982_0_1_1; -.
DR InParanoid; Q07009; -.
DR OMA; CLETRNT; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; Q07009; -.
DR TreeFam; TF314748; -.
DR BRENDA; 3.4.22.53; 5301.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR EvolutionaryTrace; Q07009; -.
DR PRO; PR:Q07009; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000034015; Expressed in lung and 20 other tissues.
DR Genevisible; Q07009; RN.
DR GO; GO:0110158; C:calpain complex; ISO:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0005925; C:focal adhesion; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0031143; C:pseudopodium; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0048266; P:behavioral response to pain; IDA:RGD.
DR GO; GO:0001824; P:blastocyst development; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0007520; P:myoblast fusion; ISO:RGD.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:RGD.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
DR GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; IMP:RGD.
DR GO; GO:0016540; P:protein autoprocessing; IDA:RGD.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:RGD.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:InterPro.
DR GO; GO:0032675; P:regulation of interleukin-6 production; IMP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR CDD; cd16199; EFh_PEF_CAPN2; 1.
DR DisProt; DP01996; -.
DR InterPro; IPR033883; C2_III.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR029539; CAPN2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR042736; EFh_PEF_CAPN2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183:SF268; PTHR10183:SF268; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Membrane; Metal-binding; Protease;
KW Reference proteome; Repeat; Thiol protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P17655"
FT PROPEP 2..19
FT /note="Anchors to the small subunit"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026493"
FT CHAIN 20..700
FT /note="Calpain-2 catalytic subunit"
FT /id="PRO_0000026494"
FT DOMAIN 45..344
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 572..605
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 602..637
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 667..700
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 345..514
FT /note="Domain III"
FT REGION 515..529
FT /note="Linker"
FT REGION 530..700
FT /note="Domain IV"
FT ACT_SITE 105
FT /evidence="ECO:0000269|PubMed:7635186"
FT ACT_SITE 262
FT /evidence="ECO:0000269|PubMed:7635186"
FT ACT_SITE 286
FT /evidence="ECO:0000269|PubMed:7635186"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 545
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 585
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 587
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 589
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 591
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 596
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 615
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 617
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 619
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 621
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 626
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 658
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 661
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P17655"
FT MUTAGEN 105
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7635186"
FT MUTAGEN 226
FT /note="K->S: 12% decrease in activity."
FT MUTAGEN 230
FT /note="K->E: 84% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11102442"
FT MUTAGEN 230
FT /note="K->S: No effect."
FT /evidence="ECO:0000269|PubMed:11102442"
FT MUTAGEN 234
FT /note="K->E: 85% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11102442"
FT MUTAGEN 234
FT /note="K->S: 20% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11102442"
FT MUTAGEN 262
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7635186"
FT MUTAGEN 286
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7635186"
FT MUTAGEN 288
FT /note="W->Y: 95% decrease in activity."
FT /evidence="ECO:0000269|PubMed:7635186"
FT MUTAGEN 417
FT /note="R->A: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:19020622"
FT MUTAGEN 420
FT /note="R->A: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:19020622"
FT MUTAGEN 469
FT /note="R->A: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:19020622"
FT MUTAGEN 504
FT /note="E->S: 10% decrease in activity."
FT /evidence="ECO:0000269|PubMed:11102442"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:1DF0"
FT TURN 15..19
FT /evidence="ECO:0007829|PDB:1DF0"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1DF0"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1MDW"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1DF0"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1MDW"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1MDW"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1DF0"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:1MDW"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3DF0"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:1MDW"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:1MDW"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:1MDW"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1MDW"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:3DF0"
FT STRAND 264..274
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:3DF0"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:1MDW"
FT HELIX 309..315
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:1MDW"
FT HELIX 328..334
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:1MDW"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:3DF0"
FT STRAND 355..365
FT /evidence="ECO:0007829|PDB:3BOW"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 404..415
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 450..455
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 465..477
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 479..490
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 495..507
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:1U5I"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 532..542
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 546..549
FT /evidence="ECO:0007829|PDB:1U5I"
FT HELIX 550..561
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 574..584
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 594..614
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 624..633
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 640..650
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:1QXP"
FT HELIX 659..676
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:3BOW"
FT STRAND 685..690
FT /evidence="ECO:0007829|PDB:3BOW"
FT HELIX 691..700
FT /evidence="ECO:0007829|PDB:3BOW"
SQ SEQUENCE 700 AA; 79919 MW; 296B0DC3BEEF5B90 CRC64;
MAGIAMKLAK DREAAEGLGS HERAIKYLNQ DYETLRNECL EAGALFQDPS FPALPSSLGF
KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG ALGDCWLLAA IASLTLNEEI
LARVVPLDQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELRKP PPNLFKIIQK ALEKGSLLGC
SIDITSAADS EAVTYQKLVK GHAYSVTGAE EVESSGSLQK LIRIRNPWGQ VEWTGKWNDN
CPSWNTVDPE VRANLTERQE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTC DSYKKWKLTK
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDDED GERGCTFLVG LIQKHRRRQR
KMGEDMHTIG FGIYEVPEEL TGQTNIHLSK NFFLTTRARE RSDTFINLRE VLNRFKLPPG
EYVLVPSTFE PHKNGDFCIR VFSEKKADYQ TVDDEIEANI EEIEANEEDI GDGFRRLFAQ
LAGEDAEISA FELQTILRRV LAKREDIKSD GFSIETCKIM VDMLDEDGSG KLGLKEFYIL
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKLPC QLHQVIVARF ADDELIIDFD
NFVRCLVRLE ILFKIFKQLD PENTGTIQLD LISWLSFSVL
