ID ENPP3_RAT Reviewed; 875 AA.
AC P97675; P70641; P97676; Q4V8L6; Q63490;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 27-MAR-2024, entry version 165.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 3;
DE Short=E-NPP 3;
DE AltName: Full=B10 {ECO:0000303|PubMed:9096610};
DE AltName: Full=Phosphodiesterase I beta;
DE Short=PD-Ibeta;
DE AltName: Full=Phosphodiesterase I/nucleotide pyrophosphatase 3;
DE AltName: Full=RB13-6 antigen {ECO:0000303|PubMed:7730366};
DE AltName: CD_antigen=CD203c;
DE Includes:
DE RecName: Full=Alkaline phosphodiesterase I;
DE EC=3.1.4.1 {ECO:0000269|PubMed:9096610};
DE Includes:
DE RecName: Full=Nucleotide pyrophosphatase;
DE Short=NPPase;
DE EC=3.6.1.9 {ECO:0000250|UniProtKB:O14638};
DE AltName: Full=Nucleotide diphosphatase {ECO:0000305};
GN Name=Enpp3; Synonyms=Pdnp3;
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], PROTEIN SEQUENCE OF 331-339; 473-504; 544-558
RP AND 605-618, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC STRAIN=Sprague-Dawley; TISSUE=Fetal brain;
RX PubMed=7730366; DOI=10.1074/jbc.270.17.9849;
RA Deissler H., Lottspeich F., Rajewsky M.F.;
RT "Affinity purification and cDNA cloning of rat neural differentiation and
RT tumor cell surface antigen gp130RB13-6 reveals relationship to human and
RT murine PC-1.";
RL J. Biol. Chem. 270:9849-9855(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 494-503 AND 726-746,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC STRAIN=Sprague-Dawley; TISSUE=Intestine;
RX PubMed=9096610; DOI=10.1002/hep.510250434;
RA Scott L.J., Delautier D., Meerson N.R., Trugnan G., Goding J.W.,
RA Maurice M.;
RT "Biochemical and molecular identification of distinct forms of alkaline
RT phosphodiesterase I expressed on the apical and basolateral plasma membrane
RT surfaces of rat hepatocytes.";
RL Hepatology 25:995-1002(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Small intestine;
RA Sano K.;
RT "Molecular cloning of phosphodiesterase I cDNA from rat small intestine.";
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=11069764; DOI=10.1242/jcs.113.23.4193;
RA Meerson N.R., Bello V., Delaunay J.-L., Slimane T.A., Delautier D.,
RA Lenoir C., Trugnan G., Maurice M.;
RT "Intracellular traffic of the ecto-nucleotide
RT pyrophosphatase/phosphodiesterase NPP3 to the apical plasma membrane of
RT MDCK and Caco-2 cells: apical targeting occurs in the absence of N-
RT glycosylation.";
RL J. Cell Sci. 113:4193-4202(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Hydrolase that metabolizes extracellular nucleotides,
CC including ATP, GTP, UTP and CTP (By similarity). Limits mast cell and
CC basophil responses during inflammation and during the chronic phases of
CC allergic responses by eliminating the extracellular ATP that functions
CC as signaling molecule and activates basophils and mast cells and
CC induces the release of inflammatory cytokines. Metabolizes
CC extracellular ATP in the lumen of the small intestine, and thereby
CC prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic
CC cells (By similarity). Has also alkaline phosphodiesterase activity
CC (PubMed:9096610). {ECO:0000250|UniProtKB:O14638,
CC ECO:0000250|UniProtKB:Q6DYE8, ECO:0000269|PubMed:9096610}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolytically removes 5'-nucleotides successively from the
CC 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.;
CC EC=3.1.4.1; Evidence={ECO:0000269|PubMed:9096610};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000250|UniProtKB:O14638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC Evidence={ECO:0000250|UniProtKB:O14638};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O14638};
CC Note=Binds 2 zinc ions per subunit. {ECO:0000250|UniProtKB:O14638};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:O14638}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7730366};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:O14638}.
CC Apical cell membrane {ECO:0000269|PubMed:11069764,
CC ECO:0000269|PubMed:9096610}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O14638}. Secreted
CC {ECO:0000250|UniProtKB:O14638}. Note=Detected at the cell surface of
CC basophils. Detected at the apical plasma membrane of bile duct cells.
CC Located to the apical surface in intestinal and kidney epithelial
CC cells. Secreted in serum, and in lumen of epithelial cells.
CC {ECO:0000250|UniProtKB:O14638}.
CC -!- TISSUE SPECIFICITY: Detected in intestinal epithelium and liver (at
CC protein level). {ECO:0000269|PubMed:9096610}.
CC -!- PTM: The N-terminal is blocked.
CC -!- PTM: N-glycosylated (PubMed:7730366, PubMed:9096610). N-glycosylation
CC is necessary for normal transport to the cell membrane, but is not the
CC apical targeting signal (PubMed:11069764).
CC {ECO:0000269|PubMed:11069764, ECO:0000269|PubMed:7730366,
CC ECO:0000269|PubMed:9096610}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC 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; Z47987; CAA88029.1; -; mRNA.
DR EMBL; U78787; AAB61535.1; -; mRNA.
DR EMBL; U78788; AAB61536.1; -; mRNA.
DR EMBL; D30649; BAA06333.1; -; mRNA.
DR EMBL; BC097326; AAH97326.1; -; mRNA.
DR PIR; A57080; A57080.
DR RefSeq; NP_062243.2; NM_019370.2.
DR PDB; 6F2T; X-ray; 2.40 A; A/B=140-875.
DR PDB; 6F2V; X-ray; 2.50 A; A/B=140-875.
DR PDB; 6F2Y; X-ray; 2.40 A; A/B=140-875.
DR PDB; 6F30; X-ray; 2.30 A; A/B=140-875.
DR PDB; 6F33; X-ray; 3.00 A; A/B=140-875.
DR PDB; 6G4G; X-ray; 2.80 A; A/B/C/D=49-875.
DR PDBsum; 6F2T; -.
DR PDBsum; 6F2V; -.
DR PDBsum; 6F2Y; -.
DR PDBsum; 6F30; -.
DR PDBsum; 6F33; -.
DR PDBsum; 6G4G; -.
DR AlphaFoldDB; P97675; -.
DR SMR; P97675; -.
DR STRING; 10116.ENSRNOP00000018695; -.
DR GlyCosmos; P97675; 8 sites, No reported glycans.
DR GlyGen; P97675; 8 sites.
DR iPTMnet; P97675; -.
DR PhosphoSitePlus; P97675; -.
DR PaxDb; 10116-ENSRNOP00000018695; -.
DR GeneID; 54410; -.
DR KEGG; rno:54410; -.
DR AGR; RGD:708511; -.
DR CTD; 5169; -.
DR RGD; 708511; Enpp3.
DR VEuPathDB; HostDB:ENSRNOG00000013791; -.
DR eggNOG; KOG2645; Eukaryota.
DR HOGENOM; CLU_012256_0_1_1; -.
DR InParanoid; P97675; -.
DR OrthoDB; 1366859at2759; -.
DR PhylomeDB; P97675; -.
DR TreeFam; TF330032; -.
DR BRENDA; 3.6.1.9; 5301.
DR SABIO-RK; P97675; -.
DR PRO; PR:P97675; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000013791; Expressed in duodenum and 19 other cell types or tissues.
DR Genevisible; P97675; RN.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; TAS:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004551; F:dinucleotide phosphatase activity; TAS:RGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0047429; F:nucleoside triphosphate diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0004528; F:phosphodiesterase I activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
DR GO; GO:0002276; P:basophil activation involved in immune response; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; ISS:UniProtKB.
DR GO; GO:0070667; P:negative regulation of mast cell proliferation; ISS:UniProtKB.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; ISO:RGD.
DR GO; GO:0055062; P:phosphate ion homeostasis; ISO:RGD.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; ISO:RGD.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; ISS:UniProtKB.
DR GO; GO:0051150; P:regulation of smooth muscle cell differentiation; NAS:RGD.
DR CDD; cd16018; Enpp; 1.
DR CDD; cd00091; NUC; 1.
DR Gene3D; 4.10.410.20; -; 2.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10151:SF107; ECTONUCLEOTIDE PYROPHOSPHATASE_PHOSPHODIESTERASE FAMILY MEMBER 3; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF01033; Somatomedin_B; 2.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR SUPFAM; SSF90188; Somatomedin B domain; 2.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..875
FT /note="Ectonucleotide pyrophosphatase/phosphodiesterase
FT family member 3"
FT /id="PRO_0000188571"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..875
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 51..94
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 95..139
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT REGION 141..510
FT /note="Phosphodiesterase"
FT REGION 605..875
FT /note="Nuclease"
FT MOTIF 79..81
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 206
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15396"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 752
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 754
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 756
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 758
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 760
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 59..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 70..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 76..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 99..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 104..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 114..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 120..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 145..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 153..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 381..478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 429..818
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 562..623
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 575..679
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 577..664
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 787..797
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT VARIANT 124
FT /note="K -> E"
FT VARIANT 201
FT /note="M -> V"
FT VARIANT 596..597
FT /note="SG -> NR"
FT CONFLICT 111
FT /note="A -> T (in Ref. 3; BAA06333)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="P -> L (in Ref. 1; CAA88029)"
FT /evidence="ECO:0000305"
FT CONFLICT 475..476
FT /note="SS -> VP (in Ref. 3; BAA06333)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="N -> KP (in Ref. 3; BAA06333)"
FT /evidence="ECO:0000305"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6G4G"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:6G4G"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:6G4G"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:6G4G"
FT TURN 101..105
FT /evidence="ECO:0007829|PDB:6G4G"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6G4G"
FT TURN 118..124
FT /evidence="ECO:0007829|PDB:6G4G"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:6G4G"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:6G4G"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:6F30"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:6F2T"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:6F30"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6F30"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6F2T"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:6F30"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 326..332
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 337..359
FT /evidence="ECO:0007829|PDB:6F30"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:6F30"
FT TURN 411..417
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 517..524
FT /evidence="ECO:0007829|PDB:6F30"
FT TURN 536..539
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 597..607
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 622..626
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 631..635
FT /evidence="ECO:0007829|PDB:6F30"
FT TURN 636..639
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 640..648
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:6F2V"
FT STRAND 669..671
FT /evidence="ECO:0007829|PDB:6F2T"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 681..684
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 686..694
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 702..705
FT /evidence="ECO:0007829|PDB:6F30"
FT TURN 706..708
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 711..713
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 714..718
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 719..730
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 732..739
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 742..750
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 762..764
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 778..789
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 794..796
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 801..809
FT /evidence="ECO:0007829|PDB:6F30"
FT TURN 815..817
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 824..826
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 828..834
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 839..846
FT /evidence="ECO:0007829|PDB:6F30"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:6F30"
FT HELIX 858..865
FT /evidence="ECO:0007829|PDB:6F30"
SQ SEQUENCE 875 AA; 99072 MW; 4205F263E8A933EA CRC64;
MDSRLALATE EPIKKDSLKR YKILCAVLLA LLVIVSLGLG LGLGLRKPEE HIGSCRKKCF
DSSHRGLEGC RCDSGCTDRG DCCWDFEDTC VKSTQIWTCN SFRCGETRLE AALCSCADDC
LQRKDCCTDY KAVCQGEVPW VTEACASSQE PQCPEGFDQP PVILFSMDGF RAEYLQTWST
LLPNINKLKT CGLHSKYMRA MYPTKTFPNH YTIVTGLYPE SHGIIDNNMY DVYLNKNFSL
SSVEKSNPAW WSGQPIWLTA MYQGLKAASY YWPGSDVAVN GSFPNIYRNY SNSVPYESRI
ATLLQWLDLP KAERPSFYTI YVEEPDSAGH KSGPVSAGVI KALQLVDDAF GMLMEGLKQR
NLHNCVNIIV LADHGMDQTS CDRVEYMTDY FPEINFYMYQ GPAPRIRTRN IPQDFFTFNS
EEIVRDLSCR KSDQHFKPYL TPDLPKRLHY AKNVRIDKVH LMVDRQWLAY RNKGSSNCEG
GTHGYNNEFK SMEAIFLAHG PSFKEKTVIE PFENIEVYNL LCDLLHIQPA PNNGSHGSLN
HLLKAPFYQP SHAEELSKSA GCGFTTPLPK DSLNCSCLAL QTSGQEEQVN QRLNLSGGEV
SATEKTNLPF GRPRVIQKNK DHCLLYHREY VSGFGKAMKM PMWSSYTVPK PGDTSSLPPT
VPDCLRADVR VDPSESQKCS FYLADQNIDH GFLYPPAIKG NNESQYDALI TSNLVPMYKE
FKKMWDYFHK VLLIKYAIER NGVNVVSGPI FDYNYDGHFD APDEITNYVA GTDVPVPTHY
FVVLTSCKNK THTPDSCPGW LDVLPFVVPH RPTNVESCPE NKAEDLWVEE RFKAHIARVR
DVELLTGLDF YQEKTQPVSE ILQLKTYLPT FETII
//
