ID   PTPRS_RAT               Reviewed;        1907 AA.
AC   Q64605; Q07808; Q3KRE9; Q64621; Q64675;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase S;
DE            Short=R-PTP-S;
DE            EC=3.1.3.48 {ECO:0000269|PubMed:8068021};
DE   AltName: Full=Leukocyte common antigen-related protein-tyrosine phosphatase 2;
DE            Short=LAR-PTP2 {ECO:0000303|PubMed:8068021};
DE   AltName: Full=Receptor-type tyrosine-protein phosphatase sigma;
DE            Short=R-PTP-sigma;
DE   Flags: Precursor;
GN   Name=Ptprs;
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] (ISOFORM 2), CATALYTIC ACTIVITY, FUNCTION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8068021; DOI=10.1042/bj3020039;
RA   Zhang W.-R., Hashimoto N., Ahmad F., Ding W., Goldstein B.J.;
RT   "Molecular cloning and expression of a unique receptor-like protein-
RT   tyrosine-phosphatase in the leucocyte-common-antigen-related phosphate
RT   family.";
RL   Biochem. J. 302:39-47(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   INTERACTION WITH NTRK1 AND NTRK3.
RX   PubMed=17967490; DOI=10.1016/j.bbamcr.2007.06.008;
RA   Faux C., Hawadle M., Nixon J., Wallace A., Lee S., Murray S., Stoker A.;
RT   "PTPsigma binds and dephosphorylates neurotrophin receptors and can
RT   suppress NGF-dependent neurite outgrowth from sensory neurons.";
RL   Biochim. Biophys. Acta 1773:1689-1700(2007).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=22519304; DOI=10.1111/j.1471-4159.2012.07762.x;
RA   Horn K.E., Xu B., Gobert D., Hamam B.N., Thompson K.M., Wu C.L.,
RA   Bouchard J.F., Uetani N., Racine R.J., Tremblay M.L., Ruthazer E.S.,
RA   Chapman C.A., Kennedy T.E.;
RT   "Receptor protein tyrosine phosphatase sigma regulates synapse structure,
RT   function and plasticity.";
RL   J. Neurochem. 122:147-161(2012).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1328-1614.
RX   PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
RA   Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
RA   Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
RA   Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
RA   Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
RA   Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
RT   "Structural genomics of protein phosphatases.";
RL   J. Struct. Funct. Genomics 8:121-140(2007).
CC   -!- FUNCTION: Cell surface receptor that binds to glycosaminoglycans,
CC       including chondroitin sulfate proteoglycans and heparan sulfate
CC       proteoglycans. Binding to chondroitin sulfate and heparan sulfate
CC       proteoglycans has opposite effects on PTPRS oligomerization and
CC       regulation of neurite outgrowth. Contributes to the inhibition of
CC       neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also
CC       after nerve transection. Plays a role in stimulating neurite outgrowth
CC       in response to the heparan sulfate proteoglycan GPC2. Required for
CC       normal brain development, especially for normal development of the
CC       pituitary gland and the olfactory bulb (By similarity). Functions as
CC       tyrosine phosphatase (PubMed:8068021). Mediates dephosphorylation of
CC       NTRK1, NTRK2 and NTRK3 (By similarity). Plays a role in down-regulation
CC       of signaling cascades that lead to the activation of Akt and MAP
CC       kinases. Down-regulates TLR9-mediated activation of NF-kappa-B, as well
CC       as production of TNF, interferon alpha and interferon beta (By
CC       similarity). {ECO:0000250|UniProtKB:B0V2N1,
CC       ECO:0000250|UniProtKB:F1NWE3, ECO:0000269|PubMed:8068021}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044, ECO:0000269|PubMed:8068021};
CC   -!- SUBUNIT: Binding to large heparan sulfate proteoglycan structures
CC       promotes oligomerization. Binding to chondroitin sulfate proteoglycan
CC       does not lead to oligomerization (By similarity). Interacts (via Ig-
CC       like domains) with NTRK1 and NTRK3, but does not form detectable
CC       complexes with NTRK2 (PubMed:17967490). Interacts with PPFIA1, PPFIA2
CC       and PPFIA3 (By similarity). {ECO:0000250|UniProtKB:B0V2N1,
CC       ECO:0000250|UniProtKB:Q13332, ECO:0000269|PubMed:17967490}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22519304};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:B0V2N1}.
CC       Cell projection, axon {ECO:0000250|UniProtKB:B0V2N1}. Perikaryon
CC       {ECO:0000250|UniProtKB:B0V2N1}. Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane {ECO:0000269|PubMed:22519304}. Synapse,
CC       synaptosome {ECO:0000269|PubMed:22519304}. Postsynaptic density
CC       {ECO:0000269|PubMed:22519304}. Cell projection, neuron projection
CC       {ECO:0000250|UniProtKB:B0V2N1}. Cell projection, growth cone
CC       {ECO:0000250|UniProtKB:B0V2N1}. Note=Is rapidly internalized when
CC       dendritic cells are stimulated with the TLR9 ligand cytidine-phosphate-
CC       guanosine (CpG). Detected in a punctate pattern along neurites and axon
CC       growth cones. {ECO:0000250|UniProtKB:B0V2N1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q64605-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q64605-2; Sequence=VSP_026932;
CC   -!- TISSUE SPECIFICITY: Detected in brain neocortex (at protein level)
CC       (PubMed:22519304). Detected in heart, testis and liver
CC       (PubMed:8068021). Detected at lower levels in skeletal muscle, brain,
CC       spleen and kidney (PubMed:8068021). {ECO:0000269|PubMed:22519304,
CC       ECO:0000269|PubMed:8068021}.
CC   -!- PTM: A cleavage occurs, separating the extracellular domain from the
CC       transmembrane segment. This process called 'ectodomain shedding' is
CC       thought to be involved in receptor desensitization, signal transduction
CC       and/or membrane localization (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily. {ECO:0000305}.
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DR   EMBL; L11587; AAC37656.1; -; mRNA.
DR   EMBL; BC105753; AAI05754.1; -; mRNA.
DR   PIR; I58148; I58148.
DR   PIR; S46217; S46217.
DR   RefSeq; NP_062013.1; NM_019140.2. [Q64605-2]
DR   PDB; 2NV5; X-ray; 2.00 A; A/B/C=1328-1614.
DR   PDBsum; 2NV5; -.
DR   AlphaFoldDB; Q64605; -.
DR   SMR; Q64605; -.
DR   BioGRID; 247561; 3.
DR   STRING; 10116.ENSRNOP00000065227; -.
DR   GlyCosmos; Q64605; 4 sites, No reported glycans.
DR   GlyGen; Q64605; 4 sites.
DR   iPTMnet; Q64605; -.
DR   PhosphoSitePlus; Q64605; -.
DR   PaxDb; 10116-ENSRNOP00000065227; -.
DR   ABCD; Q64605; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000073991.4; ENSRNOP00000065227.3; ENSRNOG00000047247.4. [Q64605-2]
DR   Ensembl; ENSRNOT00000103214.1; ENSRNOP00000084874.1; ENSRNOG00000047247.4. [Q64605-1]
DR   Ensembl; ENSRNOT00055026900; ENSRNOP00055021755; ENSRNOG00055015334. [Q64605-1]
DR   Ensembl; ENSRNOT00060037142; ENSRNOP00060030636; ENSRNOG00060019713. [Q64605-1]
DR   Ensembl; ENSRNOT00065021883; ENSRNOP00065016959; ENSRNOG00065013010. [Q64605-1]
DR   GeneID; 25529; -.
DR   KEGG; rno:25529; -.
DR   AGR; RGD:3452; -.
DR   CTD; 5802; -.
DR   RGD; 3452; Ptprs.
DR   eggNOG; KOG4228; Eukaryota.
DR   GeneTree; ENSGT00940000153617; -.
DR   InParanoid; Q64605; -.
DR   OrthoDB; 2875525at2759; -.
DR   PhylomeDB; Q64605; -.
DR   Reactome; R-RNO-388844; Receptor-type tyrosine-protein phosphatases.
DR   Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR   EvolutionaryTrace; Q64605; -.
DR   PRO; PR:Q64605; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0098839; C:postsynaptic density membrane; IDA:UniProtKB.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
DR   GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR   GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:RGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
DR   GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR   GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR   GO; GO:0022038; P:corpus callosum development; ISO:RGD.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:RGD.
DR   GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
DR   GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
DR   GO; GO:0048671; P:negative regulation of collateral sprouting; ISS:UniProtKB.
DR   GO; GO:0061000; P:negative regulation of dendritic spine development; ISS:UniProtKB.
DR   GO; GO:0032687; P:negative regulation of interferon-alpha production; ISO:RGD.
DR   GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:RGD.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; ISO:RGD.
DR   GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
DR   GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR   GO; GO:0021510; P:spinal cord development; ISO:RGD.
DR   GO; GO:0050808; P:synapse organization; ISO:RGD.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR   GO; GO:0099537; P:trans-synaptic signaling; ISO:RGD.
DR   CDD; cd00063; FN3; 7.
DR   CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR   CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR   CDD; cd14627; R-PTP-S-2; 1.
DR   CDD; cd14625; R-PTPc-S-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF8; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE S; 1.
DR   Pfam; PF00041; fn3; 6.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 5.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50853; FN3; 8.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW   Cell projection; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW   Heparin-binding; Hydrolase; Immunoglobulin domain; Membrane;
KW   Protein phosphatase; Receptor; Reference proteome; Repeat; Signal; Synapse;
KW   Synaptosome; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..1907
FT                   /note="Receptor-type tyrosine-protein phosphatase S"
FT                   /id="PRO_5000142153"
FT   TOPO_DOM        30..1257
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1258..1278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1279..1907
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          33..123
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          135..224
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          232..314
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          321..411
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          416..510
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          514..603
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          608..705
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          710..809
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          810..906
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          907..1008
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1011..1095
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1352..1607
FT                   /note="Tyrosine-protein phosphatase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   DOMAIN          1639..1898
FT                   /note="Tyrosine-protein phosphatase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          68..72
FT                   /note="Important for binding to glycosaminoglycan chains"
FT                   /evidence="ECO:0000250|UniProtKB:B0V2N1"
FT   REGION          691..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1286..1313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1548
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1839
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1516
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1548..1554
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1592
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            1172..1173
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        720
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        916
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        156..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        253..298
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         624..668
FT                   /note="VSWRPPPPETHNGALVGYSVRYRPLGSEDPDPKEVNNIPPTTTQI -> I
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8068021"
FT                   /id="VSP_026932"
FT   CONFLICT        597
FT                   /note="R -> C (in Ref. 1; AAC37656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        753
FT                   /note="A -> T (in Ref. 1; AAC37656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        913
FT                   /note="A -> P (in Ref. 1; AAC37656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        934
FT                   /note="R -> G (in Ref. 1; AAC37656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        950
FT                   /note="A -> T (in Ref. 1; AAC37656)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1334..1336
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   HELIX           1337..1358
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   HELIX           1369..1371
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   TURN            1373..1375
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   HELIX           1376..1378
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   HELIX           1388..1390
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1391..1393
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   TURN            1401..1404
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1405..1413
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1416..1423
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   HELIX           1428..1430
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   HELIX           1431..1440
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1445..1448
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1452..1454
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1457..1460
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1466..1472
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1475..1484
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1486..1497
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1504..1511
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1516..1519
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   HELIX           1524..1536
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1544..1553
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   HELIX           1554..1571
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   STRAND          1572..1574
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   HELIX           1576..1584
FT                   /evidence="ECO:0007829|PDB:2NV5"
FT   HELIX           1594..1608
FT                   /evidence="ECO:0007829|PDB:2NV5"
SQ   SEQUENCE   1907 AA;  211931 MW;  5CD377A88377CDA4 CRC64;
     MAPTWRPSVV SVVGPVGLFL VLLARGCLAE EPPRFIREPK DQIGVSGGVA SFVCQATGDP
     KPRVTWNKKG KKVNSQRFET IDFDESSGAV LRIQPLRTPR DENVYECVAQ NSVGEITVHA
     KLTVLREDQL PPGFPNIDMG PQLKVVERTR TATMLCAASG NPDPEITWFK DFLPVDPSAS
     NGRIKQLRSG ALQIESSEET DQGKYECVAT NSAGVRYSSP ANLYVRVRRV APRFSILPMS
     HEIMPGGNVN ITCVAVGSPM PYVKWMQGAE DLTPEDDMPV GRNVLELTDV KDSANYTCVA
     MSSLGVIEAV AQITVKSLPK APGTPVVTEN TATSITVTWD SGNPDPVSYY VIEYKSKSQD
     GPYQIKEDIT TTRYSIGGLS PNSEYEIWVS AVNSIGQGPP SESVVTRTGE QAPASAPRNV
     QARMLSATTM IVQWEEPVEP NGLIRGYRVY YTMEPEHPVG NWQKHNVDDS LLTTVGSLLE
     DETYTVRVLA FTSVGDGPLS DPIQVKTQQG VPGQPMNLRA EAKSETSIGL SWSAPRQESV
     IKYELLFREG DRGREVGRTF DPTTAFVVED LKPNTEYAFR LAARSPQGLG AFTAVVRQRT
     LQAKPSAPPQ DVKCTSLRST AILVSWRPPP PETHNGALVG YSVRYRPLGS EDPDPKEVNN
     IPPTTTQILL EALEKWTEYR VTAVAYTEVG PGPESSPVVV RTDEDVPSAP PRKVEAEALN
     ATAIRVLWRS PTPGRQHGQI RGYQVHYVRM EGAEARGPPR IKDIMLADAQ EMVITNLQPE
     TAYSITVAAY TMKGDGARSK PKVVVTKGAV LGRPTLSVQQ TPEGSLLARW EPPADAAEDP
     VLGYRLQFGR EDAAPATLEL AAWERRFAAP AHKGATYVFR LAARGRAGLG EEASAALSIP
     EDAPRGFPQI LGAAGNVSAG SVILRWLPPV PAERNGAIIK YTVSVREAGA PGPATETELA
     AAAQPGAETA LTLQGLRPET AYELRVRAHT RRGPGPFSPP LRYRLARDPV SPKNFKVKMI
     MKTSVLLSWE FPDNYNSPTP YKIQYNGLTL DVDGRTTKKL ITHLKPHTFY NFVLTNRGSS
     LGGLQQTVTA RTAFNMLSGK PSVAPKPDND GSIVVYLPDG QSPVTVQNYF IVMVPLRKSR
     GGQFPILLGS PEDMDLEELI QDLSRLQRRS LRHSRQLEVP RPYIAARFSI LPAVFHPGNQ
     KQYGGFDNRG LEPGHRYVLF VLAVLQKNEP TFAASPFSDP FQLDNPDPQP IVDGEEGLIW
     VIGPVLAVVF IICIVIAILL YKNKPDSKRK DSEPRTKCLL NNADLAPHHP KDPVEMRRIN
     FQTPGMLSHP PIPITDMAEH MERLKANDSL KLSQEYESID PGQQFTWEHS NLEANKPKNR
     YANVIAYDHS RVILQPLEGI MGSDYINANY VDGYRRQNAY IATQGPLPET FGDFWRMVWE
     QRSATVVMMT RLEEKSRVKC DQYWPNRGTE TYGFIQVTLL DTMELATFCV RTFSLHKNGS
     SEKREVRHFQ FTAWPDHGVP EYPTPFLAFL RRVKTCNPPD AGPVVVHCSA GVGRTGCFIV
     IDAMLERIRT EKTVDVYGHV TLMRSQRNYM VQTEDQYSFI HEALLEAVGC GNTEVPARSL
     YTYIQKLAQV EPGEHVTGME LEFKRLASSK AHTSRFITAS LPCNKFKNRL VNILPYESSR
     VCLQPIRGVE GSDYINASFI DGYRQQKAYI ATQGPLAETT EDFWRALWEN NSTIVVMLTK
     LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTVRQFQF
     TDWPEQGAPK SGEGFIDFIG QVHKTKEQFG QDGPISVHCS AGVGRTGVFI TLSIVLERMR
     YEGVVDIFQT VKVLRTQRPA MVQTEDEYQF CFQAALEYLG SFDHYAT
//