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 24-JAN-2024, entry version 206. 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}. 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; 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; 10116-ENSRNOP00000046509; -. DR Ensembl; ENSRNOT00000045326.4; ENSRNOP00000046509.3; ENSRNOG00000034015.4. DR Ensembl; ENSRNOT00055021594; ENSRNOP00055017508; ENSRNOG00055012648. DR Ensembl; ENSRNOT00060012759; ENSRNOP00060009674; ENSRNOG00060007713. DR Ensembl; ENSRNOT00065029816; ENSRNOP00065023675; ENSRNOG00065017813. DR GeneID; 29154; -. DR KEGG; rno:29154; -. DR UCSC; RGD:2268; rat. DR AGR; RGD:2268; -. 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; XVESSGS; -. DR OrthoDB; 142935at2759; -. 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 cell types or tissues. 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; ISS:BHF-UCL. 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:0045121; C:membrane raft; ISO:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0005634; C:nucleus; ISO: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: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: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 Gene3D; 2.60.120.380; -; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. 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; 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; CALPAIN; 1. DR PANTHER; PTHR10183:SF268; CALPAIN-2 CATALYTIC SUBUNIT; 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; SSF49758; Calpain large subunit, middle domain (domain III); 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF47473; EF-hand; 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. DR Genevisible; Q07009; RN. 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 //