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Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (E-NPP 2) (EC 3.1.4.39) (Autotaxin) (Extracellular lysophospholipase D) (LysoPLD)

 ENPP2_RAT               Reviewed;         887 AA.
Q64610; Q66HQ0;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 2.
22-NOV-2017, entry version 140.
RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 2;
Short=E-NPP 2;
EC=3.1.4.39;
AltName: Full=Autotaxin;
AltName: Full=Extracellular lysophospholipase D;
Short=LysoPLD;
Flags: Precursor;
Name=Enpp2; Synonyms=Atx, Npps2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=7961762;
Narita M., Goji J., Nakamura H., Sano K.;
"Molecular cloning, expression, and localization of a brain-specific
phosphodiesterase I/nucleotide pyrophosphatase (PD-Ialpha) from rat
brain.";
J. Biol. Chem. 269:28235-28242(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 28-32 AND
36-41, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=16436050; DOI=10.1111/j.1365-2443.2006.00924.x;
Koike S., Keino-Masu K., Ohto T., Masu M.;
"The N-terminal hydrophobic sequence of autotaxin (ENPP2) functions as
a signal peptide.";
Genes Cells 11:133-142(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12119361; DOI=10.1083/jcb.200204026;
Umezu-Goto M., Kishi Y., Taira A., Hama K., Dohmae N., Takio K.,
Yamori T., Mills G.B., Inoue K., Aoki J., Arai H.;
"Autotaxin has lysophospholipase D activity leading to tumor cell
growth and motility by lysophosphatidic acid production.";
J. Cell Biol. 158:227-233(2002).
[5]
CHARACTERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-171;
THR-209; ASP-311 AND HIS-315.
PubMed=12633853; DOI=10.1016/S0014-5793(03)00133-9;
Gijsbers R., Aoki J., Arai H., Bollen M.;
"The hydrolysis of lysophospholipids and nucleotides by autotaxin
(NPP2) involves a single catalytic site.";
FEBS Lett. 538:60-64(2003).
[6]
PROTEOLYTIC PROCESSING, PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION
CHARACTERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-13;
16-PHE--PHE-18; 18-PHE--SER-21; 21-SER--ILE-24; 24-ILE--CYS-25 AND
28-PHE--ALA-30.
PubMed=15985467; DOI=10.1242/jcs.02438;
Jansen S., Stefan C., Creemers J.W., Waelkens E., Van Eynde A.,
Stalmans W., Bollen M.;
"Proteolytic maturation and activation of autotaxin (NPP2), a secreted
metastasis-enhancing lysophospholipase D.";
J. Cell Sci. 118:3081-3089(2005).
[7]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-862 IN COMPLEX WITH
INHIBITOR AND ZINC IONS, CATALYTIC ACTIVITY, COFACTOR, CALCIUM
BINDING, DISULFIDE BONDS, GLYCOSYLATION AT ASN-524, ACTIVE SITE,
MUTAGENESIS OF LYS-430 AND 764-ASP--ASP-768, AND SUBCELLULAR LOCATION.
PubMed=21240271; DOI=10.1038/nsmb.1980;
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T.,
Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J.,
van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E.,
Kasiem M., Harlos K., Kooi C.W., Smyth S.S., Ovaa H., Bollen M.,
Morris A.J., Moolenaar W.H., Perrakis A.;
"Structural basis of substrate discrimination and integrin binding by
autotaxin.";
Nat. Struct. Mol. Biol. 18:198-204(2011).
-!- FUNCTION: Hydrolyzes lysophospholipids to produce lysophosphatidic
acid (LPA) in extracellular fluids. Major substrate is
lysophosphatidylcholine. Also can act on
sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a
modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to
some extent pNP-TMP, and barely ATP. Involved in several motility-
related processes such as angiogenesis and neurite outgrowth. Acts
as an angiogenic factor by stimulating migration of smooth muscle
cells and microtubule formation. Stimulates migration of melanoma
cells, probably via a pertussis toxin-sensitive G protein. May
have a role in induction of parturition. Possible involvement in
cell proliferation and adipose tissue development. Tumor cell
motility-stimulating factor. {ECO:0000269|PubMed:12119361,
ECO:0000269|PubMed:15985467}.
-!- CATALYTIC ACTIVITY: 1-alkyl-sn-glycero-3-phosphoethanolamine +
H(2)O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine.
{ECO:0000269|PubMed:21240271}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:21240271};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:21240271};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:21240271};
Note=Binds 1 Ca(2+) ion per subunit.
{ECO:0000269|PubMed:21240271};
-!- ENZYME REGULATION: Inhibited by lysophosphatidic acid (LPA) and
sphingosine-1-phosphate (S1P). Inhibited by EDTA and EGTA (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12119361,
ECO:0000269|PubMed:12633853, ECO:0000269|PubMed:15985467,
ECO:0000269|PubMed:16436050, ECO:0000269|PubMed:21240271}.
Note=Secreted by most body fluids including serum and CSF. Also by
adipocytes and numerous cancer cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q64610-1; Sequence=Displayed;
Name=2;
IsoId=Q64610-2; Sequence=VSP_024018;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Abundantly expressed in cerebrum and
cerebellum. Localized in secretory epithelial cells in the brain
and the eye including choroid plexus epithelial cells, ciliary
epithelial cells, iris pigment epithelial cells, and retinal
pigment cells. {ECO:0000269|PubMed:16436050,
ECO:0000269|PubMed:7961762}.
-!- PTM: N-glycosylation, but not furin-cleavage, plays a critical
role on secretion and on lysoPLD activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
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EMBL; D28560; BAA05910.1; -; mRNA.
EMBL; DQ131564; AAZ99725.1; -; mRNA.
EMBL; BC081747; AAH81747.1; -; mRNA.
PIR; A55453; A55453.
RefSeq; NP_476445.2; NM_057104.2.
UniGene; Rn.20403; -.
PDB; 2XR9; X-ray; 2.05 A; A=36-887.
PDB; 2XRG; X-ray; 3.20 A; A=1-887.
PDB; 5DLT; X-ray; 1.60 A; A=36-887.
PDB; 5DLV; X-ray; 2.00 A; A/B=36-887.
PDB; 5DLW; X-ray; 1.80 A; A=36-887.
PDB; 5IJQ; X-ray; 2.05 A; A=36-887.
PDB; 5IJS; X-ray; 2.20 A; A=36-887.
PDB; 5L0B; X-ray; 2.41 A; A/B=1-887.
PDB; 5L0E; X-ray; 3.06 A; A/B=1-887.
PDB; 5L0K; X-ray; 2.73 A; A/B=51-884.
PDB; 5LQQ; X-ray; 2.40 A; A=36-887.
PDB; 5M0D; X-ray; 2.40 A; A=36-887.
PDB; 5M0E; X-ray; 1.95 A; A=36-887.
PDB; 5M0M; X-ray; 2.10 A; A=36-887.
PDB; 5M0S; X-ray; 2.10 A; A=36-887.
PDBsum; 2XR9; -.
PDBsum; 2XRG; -.
PDBsum; 5DLT; -.
PDBsum; 5DLV; -.
PDBsum; 5DLW; -.
PDBsum; 5IJQ; -.
PDBsum; 5IJS; -.
PDBsum; 5L0B; -.
PDBsum; 5L0E; -.
PDBsum; 5L0K; -.
PDBsum; 5LQQ; -.
PDBsum; 5M0D; -.
PDBsum; 5M0E; -.
PDBsum; 5M0M; -.
PDBsum; 5M0S; -.
ProteinModelPortal; Q64610; -.
SMR; Q64610; -.
MINT; MINT-4997409; -.
ChEMBL; CHEMBL3826870; -.
SwissLipids; SLP:000000394; -.
iPTMnet; Q64610; -.
PRIDE; Q64610; -.
GeneID; 84050; -.
KEGG; rno:84050; -.
UCSC; RGD:69298; rat. [Q64610-1]
CTD; 5168; -.
RGD; 69298; Enpp2.
HOGENOM; HOG000037439; -.
HOVERGEN; HBG051484; -.
InParanoid; Q64610; -.
KO; K01122; -.
PhylomeDB; Q64610; -.
BRENDA; 3.1.4.39; 5301.
SABIO-RK; Q64610; -.
EvolutionaryTrace; Q64610; -.
PRO; PR:Q64610; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0004551; F:nucleotide diphosphatase activity; IEA:InterPro.
GO; GO:0004528; F:phosphodiesterase I activity; IMP:RGD.
GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; IMP:RGD.
GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
GO; GO:0044849; P:estrous cycle; IEP:RGD.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IDA:RGD.
GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
GO; GO:0009395; P:phospholipid catabolic process; ISO:RGD.
GO; GO:0006644; P:phospholipid metabolic process; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:RGD.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:RGD.
GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; ISO:RGD.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IDA:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:RGD.
GO; GO:0045765; P:regulation of angiogenesis; IEA:InterPro.
GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
GO; GO:1903165; P:response to polycyclic arene; IEP:RGD.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
InterPro; IPR029881; ENPP2.
InterPro; IPR020821; Extracellular_endonuc_su_A.
InterPro; IPR002591; Phosphodiest/P_Trfase.
InterPro; IPR036024; Somatomedin_B-like_dom_sf.
InterPro; IPR020436; Somatomedin_B_chordata.
InterPro; IPR001212; Somatomedin_B_dom.
PANTHER; PTHR10151:SF21; PTHR10151:SF21; 1.
Pfam; PF01223; Endonuclease_NS; 1.
Pfam; PF01663; Phosphodiest; 1.
Pfam; PF01033; Somatomedin_B; 2.
PRINTS; PR00022; SOMATOMEDINB.
SMART; SM00892; Endonuclease_NS; 1.
SMART; SM00477; NUC; 1.
SMART; SM00201; SO; 2.
SUPFAM; SSF53649; SSF53649; 1.
SUPFAM; SSF90188; SSF90188; 2.
PROSITE; PS00524; SMB_1; 2.
PROSITE; PS50958; SMB_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Chemotaxis;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Lipid degradation; Lipid metabolism; Metal-binding; Obesity;
Reference proteome; Repeat; Secreted; Signal; Zinc.
SIGNAL 1 27 {ECO:0000269|PubMed:15985467,
ECO:0000269|PubMed:16436050}.
PROPEP 28 35 Removed by furin.
{ECO:0000269|PubMed:15985467,
ECO:0000269|PubMed:16436050}.
/FTId=PRO_0000281651.
CHAIN 36 887 Ectonucleotide
pyrophosphatase/phosphodiesterase family
member 2.
/FTId=PRO_0000188569.
DOMAIN 54 97 SMB 1. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DOMAIN 98 142 SMB 2. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
REGION 210 213 Substrate binding. {ECO:0000250}.
REGION 243 254 Substrate binding. {ECO:0000250}.
REGION 854 875 Required for secretion. {ECO:0000250}.
MOTIF 126 128 Cell attachment site. {ECO:0000255}.
ACT_SITE 209 209 Nucleophile. {ECO:0000250}.
METAL 171 171 Zinc 1; catalytic.
METAL 209 209 Zinc 1; catalytic.
METAL 311 311 Zinc 2; catalytic.
METAL 315 315 Zinc 2; catalytic.
METAL 315 315 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 358 358 Zinc 1; catalytic.
METAL 359 359 Zinc 1; catalytic.
METAL 359 359 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 474 474 Zinc 2; catalytic.
METAL 474 474 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 764 764 Calcium.
METAL 766 766 Calcium.
METAL 768 768 Calcium.
METAL 770 770 Calcium; via carbonyl oxygen.
METAL 772 772 Calcium.
BINDING 230 230 Substrate. {ECO:0000250}.
BINDING 306 306 Substrate. {ECO:0000250}.
SITE 877 877 Essential for catalytic activity.
{ECO:0000250}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 398 398 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21240271}.
CARBOHYD 610 610 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 831 831 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 58 75 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 62 93 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 73 86 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 79 85 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 102 119 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 107 137 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 117 130 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 123 129 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 148 194 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 156 350 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 366 468 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 413 830 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 566 691 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 568 676 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
DISULFID 799 809 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:21240271}.
VAR_SEQ 591 615 Missing (in isoform 2).
{ECO:0000303|PubMed:16436050}.
/FTId=VSP_024018.
MUTAGEN 13 13 I->L: No effect on secretion.
{ECO:0000269|PubMed:15985467}.
MUTAGEN 16 18 FTF->VLS: No effect on secretion.
{ECO:0000269|PubMed:15985467}.
MUTAGEN 18 21 FAIS->SVCV: No effect on secretion.
{ECO:0000269|PubMed:15985467}.
MUTAGEN 21 24 SVNI->VLTT: No effect on secretion.
{ECO:0000269|PubMed:15985467}.
MUTAGEN 24 25 IC->TI: No effect on secretion.
{ECO:0000269|PubMed:15985467}.
MUTAGEN 28 30 FTA->CIF: No effect on secretion.
{ECO:0000269|PubMed:15985467}.
MUTAGEN 171 171 D->N: Abolishes lysophospholipase D
activity. {ECO:0000269|PubMed:12633853}.
MUTAGEN 209 209 T->A: Abolishes lysophospholipase D
activity. {ECO:0000269|PubMed:12633853}.
MUTAGEN 209 209 T->S: 15% of wild-type lysophospholipase
D activity.
{ECO:0000269|PubMed:12633853}.
MUTAGEN 311 311 D->N: Abolishes lysophospholipase D
activity. {ECO:0000269|PubMed:12633853}.
MUTAGEN 315 315 H->Q: 20% of wild-type lysophospholipase
D activity.
{ECO:0000269|PubMed:12633853}.
MUTAGEN 430 430 K->A: Impaired secretion. No effect on
lysophospholipase activity.
{ECO:0000269|PubMed:21240271}.
MUTAGEN 764 768 DYNYD->SYAYS: Abolishes secretion.
Strongly reduced lysophospholipase
activity. {ECO:0000269|PubMed:21240271}.
CONFLICT 97 97 A -> V (in Ref. 1; BAA05910).
{ECO:0000305}.
CONFLICT 107 107 C -> S (in Ref. 1; BAA05910).
{ECO:0000305}.
CONFLICT 120 120 S -> P (in Ref. 1; BAA05910).
{ECO:0000305}.
CONFLICT 147 162 DCEEIKVPECPAGFVR -> AARNQSSECLQVCP (in
Ref. 1; BAA05910). {ECO:0000305}.
CONFLICT 198 198 A -> V (in Ref. 1; BAA05910).
{ECO:0000305}.
CONFLICT 201 201 M -> T (in Ref. 1; BAA05910).
{ECO:0000305}.
TURN 59 63 {ECO:0000244|PDB:5DLT}.
STRAND 70 72 {ECO:0000244|PDB:5DLV}.
TURN 77 83 {ECO:0000244|PDB:5DLT}.
HELIX 89 92 {ECO:0000244|PDB:5DLT}.
TURN 98 100 {ECO:0000244|PDB:5DLT}.
HELIX 104 106 {ECO:0000244|PDB:5DLT}.
STRAND 107 109 {ECO:0000244|PDB:5L0K}.
STRAND 115 118 {ECO:0000244|PDB:5DLT}.
HELIX 123 126 {ECO:0000244|PDB:5DLT}.
HELIX 133 137 {ECO:0000244|PDB:5DLT}.
HELIX 143 145 {ECO:0000244|PDB:5DLT}.
STRAND 165 171 {ECO:0000244|PDB:5DLT}.
HELIX 175 180 {ECO:0000244|PDB:5DLT}.
TURN 182 184 {ECO:0000244|PDB:5DLT}.
HELIX 186 194 {ECO:0000244|PDB:5DLT}.
STRAND 195 197 {ECO:0000244|PDB:5DLT}.
HELIX 209 218 {ECO:0000244|PDB:5DLT}.
HELIX 222 225 {ECO:0000244|PDB:5DLT}.
STRAND 230 234 {ECO:0000244|PDB:5DLT}.
TURN 235 238 {ECO:0000244|PDB:5DLT}.
STRAND 239 241 {ECO:0000244|PDB:5DLT}.
STRAND 243 246 {ECO:0000244|PDB:5DLT}.
HELIX 247 249 {ECO:0000244|PDB:5DLT}.
HELIX 251 253 {ECO:0000244|PDB:5DLT}.
HELIX 259 265 {ECO:0000244|PDB:5DLT}.
HELIX 281 292 {ECO:0000244|PDB:5DLT}.
TURN 296 298 {ECO:0000244|PDB:5DLT}.
STRAND 301 310 {ECO:0000244|PDB:5DLT}.
HELIX 311 317 {ECO:0000244|PDB:5DLT}.
HELIX 322 324 {ECO:0000244|PDB:5DLT}.
HELIX 325 344 {ECO:0000244|PDB:5DLT}.
TURN 348 350 {ECO:0000244|PDB:5DLT}.
STRAND 352 358 {ECO:0000244|PDB:5DLT}.
STRAND 368 371 {ECO:0000244|PDB:5DLT}.
HELIX 372 374 {ECO:0000244|PDB:5DLT}.
HELIX 379 381 {ECO:0000244|PDB:5DLT}.
STRAND 382 385 {ECO:0000244|PDB:5DLT}.
STRAND 387 395 {ECO:0000244|PDB:5DLT}.
STRAND 396 398 {ECO:0000244|PDB:5L0B}.
HELIX 404 410 {ECO:0000244|PDB:5DLT}.
STRAND 419 424 {ECO:0000244|PDB:5DLT}.
HELIX 425 427 {ECO:0000244|PDB:5DLT}.
HELIX 430 432 {ECO:0000244|PDB:5DLT}.
STRAND 442 447 {ECO:0000244|PDB:5DLT}.
STRAND 452 456 {ECO:0000244|PDB:5DLT}.
HELIX 457 459 {ECO:0000244|PDB:5DLW}.
STRAND 471 473 {ECO:0000244|PDB:5DLW}.
HELIX 481 483 {ECO:0000244|PDB:5DLT}.
STRAND 487 494 {ECO:0000244|PDB:5DLT}.
STRAND 496 499 {ECO:0000244|PDB:5DLT}.
HELIX 505 507 {ECO:0000244|PDB:5DLT}.
HELIX 508 515 {ECO:0000244|PDB:5DLT}.
TURN 527 530 {ECO:0000244|PDB:5DLT}.
HELIX 531 533 {ECO:0000244|PDB:5DLT}.
STRAND 534 536 {ECO:0000244|PDB:5DLT}.
HELIX 559 561 {ECO:0000244|PDB:5DLT}.
HELIX 577 580 {ECO:0000244|PDB:5DLT}.
TURN 583 586 {ECO:0000244|PDB:5DLT}.
HELIX 587 591 {ECO:0000244|PDB:5DLV}.
HELIX 617 620 {ECO:0000244|PDB:5DLT}.
STRAND 634 638 {ECO:0000244|PDB:5DLT}.
STRAND 643 647 {ECO:0000244|PDB:5DLT}.
TURN 648 651 {ECO:0000244|PDB:5DLT}.
STRAND 652 660 {ECO:0000244|PDB:5DLT}.
HELIX 671 673 {ECO:0000244|PDB:5DLT}.
HELIX 685 687 {ECO:0000244|PDB:5DLT}.
HELIX 691 696 {ECO:0000244|PDB:5DLT}.
STRAND 701 706 {ECO:0000244|PDB:5DLT}.
HELIX 708 710 {ECO:0000244|PDB:5DLT}.
HELIX 714 717 {ECO:0000244|PDB:5DLT}.
HELIX 718 721 {ECO:0000244|PDB:5DLT}.
HELIX 723 725 {ECO:0000244|PDB:5DLT}.
STRAND 726 729 {ECO:0000244|PDB:5DLT}.
HELIX 731 742 {ECO:0000244|PDB:5DLT}.
HELIX 744 752 {ECO:0000244|PDB:5DLT}.
STRAND 754 762 {ECO:0000244|PDB:5DLT}.
STRAND 768 770 {ECO:0000244|PDB:5DLT}.
HELIX 774 776 {ECO:0000244|PDB:5DLT}.
STRAND 790 801 {ECO:0000244|PDB:5DLT}.
HELIX 806 808 {ECO:0000244|PDB:5DLT}.
STRAND 813 821 {ECO:0000244|PDB:5DLT}.
TURN 830 833 {ECO:0000244|PDB:5DLT}.
HELIX 836 838 {ECO:0000244|PDB:5DLT}.
HELIX 840 846 {ECO:0000244|PDB:5DLT}.
HELIX 851 858 {ECO:0000244|PDB:5DLT}.
STRAND 859 861 {ECO:0000244|PDB:5M0E}.
STRAND 865 868 {ECO:0000244|PDB:5M0E}.
HELIX 870 878 {ECO:0000244|PDB:5DLT}.
SEQUENCE 887 AA; 101576 MW; 40AD1C957F833869 CRC64;
MARQGCLGSF QVISLFTFAI SVNICLGFTA SRIKRAEWDE GPPTVLSDSP WTNTSGSCKG
RCFELQEVGP PDCRCDNLCK SYSSCCHDFD ELCLKTARGW ECTKDRCGEV RNEENACHCS
EDCLSRGDCC TNYQVVCKGE SHWVDDDCEE IKVPECPAGF VRPPLIIFSV DGFRASYMKK
GSKVMPNIEK LRSCGTHAPY MRPVYPTKTF PNLYTLATGL YPESHGIVGN SMYDPVFDAS
FHLRGREKFN HRWWGGQPLW ITATKQGVRA GTFFWSVSIP HERRILTILQ WLSLPDNERP
SVYAFYSEQP DFSGHKYGPF GPEMTNPLRE IDKTVGQLMD GLKQLRLHRC VNVIFVGDHG
MEDVTCDRTE FLSNYLTNVD DITLVPGTLG RIRAKSINNS KYDPKTIIAN LTCKKPDQHF
KPYMKQHLPK RLHYANNRRI EDIHLLVDRR WHVARKPLDV YKKPSGKCFF QGDHGFDNKV
NSMQTVFVGY GPTFKYRTKV PPFENIELYN VMCDLLGLKP APNNGTHGSL NHLLRTNTFR
PTMPDEVSRP NYPGIMYLQS EFDLGCTCDD KVEPKNKLEE LNKRLHTKGS TEAETGKFRG
SKHENKKNLN GSVEPRKERH LLYGRPAVLY RTSYDILYHT DFESGYSEIF LMPLWTSYTI
SKQAEVSSIP EHLTNCVRPD VRVSPGFSQN CLAYKNDKQM SYGFLFPPYL SSSPEAKYDA
FLVTNMVPMY PAFKRVWAYF QRVLVKKYAS ERNGVNVISG PIFDYNYDGL RDTEDEIKQY
VEGSSIPVPT HYYSIITSCL DFTQPADKCD GPLSVSSFIL PHRPDNDESC NSSEDESKWV
EELMKMHTAR VRDIEHLTGL DFYRKTSRSY SEILTLKTYL HTYESEI


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