ENPL_CANLF
ID ENPL_CANLF Reviewed; 804 AA.
AC P41148;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Endoplasmin;
DE AltName: Full=94 kDa glucose-regulated protein;
DE Short=GRP-94;
DE AltName: Full=Heat shock protein 90 kDa beta member 1;
DE Flags: Precursor;
GN Name=HSP90B1; Synonyms=GRP94 {ECO:0000303|PubMed:8119936}, TRA1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP AND PHOSPHORYLATION.
RC TISSUE=Heart;
RX PubMed=8119936; DOI=10.1016/s0021-9258(17)37550-6;
RA Cala S.E., Jones L.R.;
RT "GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is
RT phosphorylated by casein kinase II.";
RL J. Biol. Chem. 269:5926-5931(1994).
RN [2] {ECO:0007744|PDB:1QY8, ECO:0007744|PDB:1QYE, ECO:0007744|PDB:1U2O, ECO:0007744|PDB:6D28}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 69-337 IN COMPLEX WITH ADENOSINE
RP ANALOG.
RX PubMed=12970348; DOI=10.1074/jbc.m308661200;
RA Soldano K.L., Jivan A., Nicchitta C.V., Gewirth D.T.;
RT "Structure of the N-terminal domain of GRP94. Basis for ligand specificity
RT and regulation.";
RL J. Biol. Chem. 278:48330-48338(2003).
RN [3] {ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6}
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 69-337 IN COMPLEXES WITH ATP; ADP
RP AND AMP, AND SUBUNIT.
RX PubMed=15292259; DOI=10.1074/jbc.m405253200;
RA Immormino R.M., Dollins D.E., Shaffer P.L., Soldano K.L., Walker M.A.,
RA Gewirth D.T.;
RT "Ligand-induced conformational shift in the N-terminal domain of GRP94, an
RT Hsp90 chaperone.";
RL J. Biol. Chem. 279:46162-46171(2004).
RN [4] {ECO:0007744|PDB:1YSZ, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:1YT1, ECO:0007744|PDB:1YT2}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 69-337 OF APOPROTEIN AND IN
RP COMPLEXES WITH ADP AND NECA.
RX PubMed=15951571; DOI=10.1074/jbc.m503761200;
RA Dollins D.E., Immormino R.M., Gewirth D.T.;
RT "Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for
RT nucleotide-induced conformational change.";
RL J. Biol. Chem. 280:30438-30447(2005).
RN [5] {ECO:0007744|PDB:2O1T, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V, ECO:0007744|PDB:2O1W}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 73-754 IN COMPLEXES WITH AMPPNP
RP AND ADP, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP GLU-103 AND ARG-448, AND CATALYTIC ACTIVITY.
RX PubMed=17936703; DOI=10.1016/j.molcel.2007.08.024;
RA Dollins D.E., Warren J.J., Immormino R.M., Gewirth D.T.;
RT "Structures of GRP94-nucleotide complexes reveal mechanistic differences
RT between the hsp90 chaperones.";
RL Mol. Cell 28:41-56(2007).
CC -!- FUNCTION: Molecular chaperone that functions in the processing and
CC transport of secreted proteins (By similarity). When associated with
CC CNPY3, required for proper folding of Toll-like receptors (By
CC similarity). Functions in endoplasmic reticulum associated degradation
CC (ERAD) (By similarity). Has ATPase activity (PubMed:17936703). May
CC participate in the unfolding of cytosolic leaderless cargos (lacking
CC the secretion signal sequence) such as the interleukin 1/IL-1 to
CC facilitate their translocation into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) and secretion; the translocation
CC process is mediated by the cargo receptor TMED10 (By similarity).
CC {ECO:0000250|UniProtKB:P08113, ECO:0000250|UniProtKB:P14625,
CC ECO:0000269|PubMed:17936703}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for ATP {ECO:0000269|PubMed:17936703};
CC -!- SUBUNIT: Homodimer; disulfide-linked. Component of an EIF2 complex at
CC least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1
CC and HSPA5 (By similarity). Part of a large chaperone multiprotein
CC complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6,
CC PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at
CC very low levels, CALR nor CANX. Interacts with AIMP1; regulates its
CC retention in the endoplasmic reticulum. Interacts with OS9 (By
CC similarity). Interacts with CNPY3; this interaction is disrupted in the
CC presence of ATP. Interacts with several TLRs, including TLR4 and TLR9,
CC but not with TLR3 (By similarity). Interacts with MZB1 in a calcium-
CC dependent manner (By similarity). Interacts with METTL23 (By
CC similarity). Interacts with IL1B; the interaction facilitates cargo
CC translocation into the ERGIC (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P14625}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P08113}. Sarcoplasmic reticulum lumen
CC {ECO:0000269|PubMed:8119936}. Melanosome
CC {ECO:0000250|UniProtKB:P14625}.
CC -!- TISSUE SPECIFICITY: Detected in heart muscle (at protein level).
CC {ECO:0000269|PubMed:8119936}.
CC -!- PTM: Phosphorylated by CK2. {ECO:0000269|PubMed:8119936}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; U01153; AAA17708.1; -; mRNA.
DR PIR; A53211; A53211.
DR RefSeq; NP_001003327.1; NM_001003327.2.
DR PDB; 1QY8; X-ray; 1.85 A; A=69-337.
DR PDB; 1QYE; X-ray; 2.10 A; A=69-337.
DR PDB; 1TBW; X-ray; 2.15 A; A/B=69-286, A/B=328-337.
DR PDB; 1TC0; X-ray; 2.20 A; A/B=69-286, A/B=328-337.
DR PDB; 1TC6; X-ray; 1.87 A; A/B=69-286, A/B=328-337.
DR PDB; 1U0Z; X-ray; 1.90 A; A/B=69-286, A/B=328-337.
DR PDB; 1U2O; X-ray; 2.10 A; A/B=69-286, A/B=328-337.
DR PDB; 1YSZ; X-ray; 2.65 A; A=69-286, A=328-337.
DR PDB; 1YT0; X-ray; 2.40 A; A=69-286, A=328-337.
DR PDB; 1YT1; X-ray; 2.20 A; A/B=69-286, A/B=328-337.
DR PDB; 1YT2; X-ray; 3.25 A; A=69-337.
DR PDB; 2ESA; X-ray; 1.90 A; A=69-286, A=328-337.
DR PDB; 2EXL; X-ray; 2.35 A; A/B=69-286, A/B=328-337.
DR PDB; 2FYP; X-ray; 1.95 A; A/B=69-286, A/B=328-337.
DR PDB; 2GFD; X-ray; 2.30 A; A/B=69-286, A/B=328-337.
DR PDB; 2GQP; X-ray; 1.50 A; A/B=69-286, A/B=328-337.
DR PDB; 2H8M; X-ray; 1.80 A; A/B=69-286, A/B=328-337.
DR PDB; 2HCH; X-ray; 2.30 A; A/B=69-286, A/B=328-337.
DR PDB; 2HG1; X-ray; 2.30 A; A/B=69-286.
DR PDB; 2O1T; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J=336-765.
DR PDB; 2O1U; X-ray; 2.40 A; A/B=73-286, A/B=328-754.
DR PDB; 2O1V; X-ray; 2.45 A; A/B=73-286, A/B=328-754.
DR PDB; 2O1W; X-ray; 3.40 A; A/B/C/D/E=73-286, A/B/C/D/E=328-594.
DR PDB; 3O2F; X-ray; 2.00 A; A/B=69-286, A/B=328-337.
DR PDB; 5IN9; X-ray; 2.60 A; A/B=69-286, A/B=328-337.
DR PDB; 5TTZ; X-ray; 2.71 A; A/B=69-286.
DR PDB; 5ULS; X-ray; 2.62 A; A/B=48-286, A/B=328-754.
DR PDB; 5WMT; X-ray; 2.75 A; A/B/C/D=69-286.
DR PDB; 6AOL; X-ray; 2.76 A; A=69-286.
DR PDB; 6AOM; X-ray; 2.87 A; A/B=69-286.
DR PDB; 6ASP; X-ray; 2.70 A; A/B=69-286.
DR PDB; 6ASQ; X-ray; 2.35 A; A/B=69-286.
DR PDB; 6BAW; X-ray; 2.70 A; A/B/C/D=69-286.
DR PDB; 6C91; X-ray; 2.90 A; B/C=69-286.
DR PDB; 6CYI; X-ray; 1.76 A; A=69-337.
DR PDB; 6D1X; X-ray; 2.30 A; A=69-337.
DR PDB; 6D28; X-ray; 1.75 A; A=69-337.
DR PDBsum; 1QY8; -.
DR PDBsum; 1QYE; -.
DR PDBsum; 1TBW; -.
DR PDBsum; 1TC0; -.
DR PDBsum; 1TC6; -.
DR PDBsum; 1U0Z; -.
DR PDBsum; 1U2O; -.
DR PDBsum; 1YSZ; -.
DR PDBsum; 1YT0; -.
DR PDBsum; 1YT1; -.
DR PDBsum; 1YT2; -.
DR PDBsum; 2ESA; -.
DR PDBsum; 2EXL; -.
DR PDBsum; 2FYP; -.
DR PDBsum; 2GFD; -.
DR PDBsum; 2GQP; -.
DR PDBsum; 2H8M; -.
DR PDBsum; 2HCH; -.
DR PDBsum; 2HG1; -.
DR PDBsum; 2O1T; -.
DR PDBsum; 2O1U; -.
DR PDBsum; 2O1V; -.
DR PDBsum; 2O1W; -.
DR PDBsum; 3O2F; -.
DR PDBsum; 5IN9; -.
DR PDBsum; 5TTZ; -.
DR PDBsum; 5ULS; -.
DR PDBsum; 5WMT; -.
DR PDBsum; 6AOL; -.
DR PDBsum; 6AOM; -.
DR PDBsum; 6ASP; -.
DR PDBsum; 6ASQ; -.
DR PDBsum; 6BAW; -.
DR PDBsum; 6C91; -.
DR PDBsum; 6CYI; -.
DR PDBsum; 6D1X; -.
DR PDBsum; 6D28; -.
DR AlphaFoldDB; P41148; -.
DR SMR; P41148; -.
DR STRING; 9612.ENSCAFP00000011044; -.
DR BindingDB; P41148; -.
DR ChEMBL; CHEMBL4748; -.
DR DrugCentral; P41148; -.
DR PaxDb; P41148; -.
DR Ensembl; ENSCAFT00030016065; ENSCAFP00030014018; ENSCAFG00030008539.
DR Ensembl; ENSCAFT00040040938; ENSCAFP00040035695; ENSCAFG00040021951.
DR Ensembl; ENSCAFT00845018625; ENSCAFP00845014533; ENSCAFG00845010421.
DR GeneID; 404019; -.
DR KEGG; cfa:404019; -.
DR CTD; 7184; -.
DR VEuPathDB; HostDB:ENSCAFG00845010421; -.
DR eggNOG; KOG0020; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR InParanoid; P41148; -.
DR OrthoDB; 924636at2759; -.
DR Reactome; R-CFA-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-CFA-3000480; Scavenging by Class A Receptors.
DR Reactome; R-CFA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CFA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-CFA-8957275; Post-translational protein phosphorylation.
DR SABIO-RK; P41148; -.
DR EvolutionaryTrace; P41148; -.
DR PRO; PR:P41148; -.
DR Proteomes; UP000002254; Chromosome 15.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Calcium; Chaperone;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydroxylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..804
FT /note="Endoplasmin"
FT /id="PRO_0000013597"
FT REGION 288..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 801..804
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 290..314
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..788
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15292259,
FT ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703,
FT ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6,
FT ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U,
FT ECO:0007744|PDB:2O1V"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15292259,
FT ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703,
FT ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0,
FT ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0,
FT ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15292259,
FT ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703,
FT ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0,
FT ECO:0007744|PDB:1TC6, ECO:0007744|PDB:2O1U,
FT ECO:0007744|PDB:2O1V"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15292259,
FT ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703,
FT ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0,
FT ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0,
FT ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V"
FT SITE 448
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000269|PubMed:17936703"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 168
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HD0"
FT MOD_RES 288
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 306
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P14625, ECO:0000255"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HD0"
FT MOD_RES 404
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 479
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 633
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 766
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 770
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 774
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 786
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P14625, ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 138
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT MUTAGEN 103
FT /note="E->A: Loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:17936703"
FT MUTAGEN 448
FT /note="R->A: Reduces ATPase activity by 85%."
FT /evidence="ECO:0000269|PubMed:17936703"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2GQP"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5ULS"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:2GQP"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2GQP"
FT HELIX 99..121
FT /evidence="ECO:0007829|PDB:2GQP"
FT TURN 123..128
FT /evidence="ECO:0007829|PDB:2GQP"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2GQP"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:2GQP"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2GQP"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:2GQP"
FT HELIX 169..184
FT /evidence="ECO:0007829|PDB:6D28"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:2GQP"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:2GQP"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:2GQP"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2O1V"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:2GQP"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:2GQP"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:2GQP"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:2GQP"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:2GQP"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:5ULS"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:2GQP"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:6D28"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:2O1U"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:2O1U"
FT TURN 395..403
FT /evidence="ECO:0007829|PDB:5ULS"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:2O1U"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:5ULS"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 434..442
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 448..452
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 455..474
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 477..482
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 484..498
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 503..507
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:5ULS"
FT HELIX 524..530
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 537..542
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 546..550
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 556..560
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 572..578
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 586..590
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 602..614
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 616..624
FT /evidence="ECO:0007829|PDB:2O1U"
FT TURN 625..630
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 631..636
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 644..649
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 656..668
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 670..673
FT /evidence="ECO:0007829|PDB:5ULS"
FT STRAND 677..680
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 683..687
FT /evidence="ECO:0007829|PDB:2O1U"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:5ULS"
FT HELIX 692..703
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 708..725
FT /evidence="ECO:0007829|PDB:2O1U"
FT HELIX 732..744
FT /evidence="ECO:0007829|PDB:2O1U"
FT TURN 751..757
FT /evidence="ECO:0007829|PDB:2O1T"
FT HELIX 758..760
FT /evidence="ECO:0007829|PDB:2O1T"
FT HELIX 762..764
FT /evidence="ECO:0007829|PDB:2O1T"
SQ SEQUENCE 804 AA; 92514 MW; 36AA126EDCFFC2D5 CRC64;
MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG
LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL
TDENALAGNE ELTVKIKCDK EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE
AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT
LGRGTTITLV LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK
EEKEDSDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EDDEYKAFYK
SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD
DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADEKY
NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHPSD ITSLDQYVER MKEKQDKIYF
MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
SEKTKESREA IEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIKDMLRR VKEDEDDKTV SDLAVVLFET
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PDAKVEEEPE EEPEETTEDT TEDTEQDDEE
EMDAGTDDEE QETVKKSTAE KDEL
