ID   PTPRT_MOUSE             Reviewed;        1454 AA.
AC   Q99M80; Q99M81; Q99M82; Q9JIZ1; Q9JIZ2; Q9JKC2; Q9JLP0;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase T;
DE            Short=R-PTP-T;
DE            EC=3.1.3.48;
DE   AltName: Full=RPTPmam4;
DE   AltName: Full=Receptor-type tyrosine-protein phosphatase rho;
DE            Short=RPTP-rho;
DE            Short=mRPTPrho;
DE   Flags: Precursor;
GN   Name=Ptprt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), AND ALTERNATIVE SPLICING.
RC   STRAIN=C57BL/6J;
RX   PubMed=11423001; DOI=10.1186/1471-2164-2-1;
RA   Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A.;
RT   "Genomic organization and alternative splicing of the human and mouse
RT   RPTPrho genes.";
RL   BMC Genomics 2:1-1(2001).
RN   [2]
RP   ERRATUM OF PUBMED:11423001.
RX   PubMed=11814386; DOI=10.1186/1471-2164-2-5;
RA   Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A.;
RL   BMC Genomics 2:5-5(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RA   Buchli A.D., Zimmermann D.R., Pfister F., Vaughan L.;
RT   "RPTPmam4: a fourth member of the MAM family of receptor protein tyrosine
RT   phosphatases expressed in adult brain.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RA   Mizuta M., Bergman B., Miki T., Hutton J.C.;
RT   "Molecular cloning and functional characterization on mouse receptor-like
RT   protein tyrosine phosphatase, mRPTPrho, which mediates cell-cell adhesion
RT   of pancreatic beta cells.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=9486824;
RX   DOI=10.1002/(sici)1096-9861(19980222)391:4<444::aid-cne3>3.0.co;2-0;
RA   McAndrew P.E., Frostholm A., Evans J.E., Zdilar D., Goldowitz D.,
RA   Chiu I.-M., Burghes A.H.M., Rotter A.;
RT   "Novel receptor protein tyrosine phosphatase (RPTPrho) and acidic
RT   fibroblast growth factor (FGF-1) transcripts delineate a rostrocaudal
RT   boundary in the granule cell layer of the murine cerebellar cortex.";
RL   J. Comp. Neurol. 391:444-455(1998).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1221, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May be involved in both signal transduction and cellular
CC       adhesion in the CNS. May have specific signaling roles in the tyrosine
CC       phosphorylation/dephosphorylation pathway in the anterior compartment
CC       of the adult cerebellar cortex.
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};
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q99M80-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99M80-2; Sequence=VSP_007803, VSP_007806;
CC       Name=3; Synonyms=RPTPrho2;
CC         IsoId=Q99M80-3; Sequence=VSP_007803, VSP_007804;
CC       Name=4; Synonyms=RPTPrho1;
CC         IsoId=Q99M80-4; Sequence=VSP_007803;
CC       Name=5;
CC         IsoId=Q99M80-5; Sequence=VSP_007803, VSP_007805;
CC   -!- TISSUE SPECIFICITY: Expression is restricted to the CNS. Distributed
CC       throughout the brain and spinal cord. {ECO:0000269|PubMed:9486824}.
CC   -!- DEVELOPMENTAL STAGE: Exceptionally high levels found in the cortex and
CC       olfactory bulbs during perinatal development and are down-regulated
CC       during postnatal week 2. Expression in the cerebellar cortex is
CC       restricted to the granule cell layer of lobules 1-6. Anterior and
CC       posterior compartments become discernible only during postnatal weeks 2
CC       and 6.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2B subfamily. {ECO:0000305}.
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DR   EMBL; AF152556; AAD34158.4; -; mRNA.
DR   EMBL; AY026861; AAK18741.1; -; mRNA.
DR   EMBL; AY026862; AAK18742.1; -; mRNA.
DR   EMBL; AY026863; AAK18743.1; -; mRNA.
DR   EMBL; AF244125; AAF44712.1; -; mRNA.
DR   EMBL; AF162856; AAF82400.2; -; mRNA.
DR   EMBL; AF162857; AAF82401.1; -; mRNA.
DR   CCDS; CCDS17001.1; -. [Q99M80-4]
DR   CCDS; CCDS71182.1; -. [Q99M80-2]
DR   CCDS; CCDS71183.1; -. [Q99M80-3]
DR   RefSeq; NP_001278078.1; NM_001291149.1. [Q99M80-2]
DR   RefSeq; NP_001278079.1; NM_001291150.1. [Q99M80-3]
DR   RefSeq; NP_067439.1; NM_021464.5. [Q99M80-4]
DR   RefSeq; XP_011237686.1; XM_011239384.2. [Q99M80-5]
DR   AlphaFoldDB; Q99M80; -.
DR   SMR; Q99M80; -.
DR   STRING; 10090.ENSMUSP00000105067; -.
DR   GlyCosmos; Q99M80; 10 sites, No reported glycans.
DR   GlyGen; Q99M80; 11 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q99M80; -.
DR   PhosphoSitePlus; Q99M80; -.
DR   MaxQB; Q99M80; -.
DR   PaxDb; 10090-ENSMUSP00000105071; -.
DR   ProteomicsDB; 302021; -. [Q99M80-1]
DR   ProteomicsDB; 302022; -. [Q99M80-2]
DR   ProteomicsDB; 302023; -. [Q99M80-3]
DR   ProteomicsDB; 302024; -. [Q99M80-4]
DR   ProteomicsDB; 302025; -. [Q99M80-5]
DR   Antibodypedia; 2780; 120 antibodies from 32 providers.
DR   DNASU; 19281; -.
DR   Ensembl; ENSMUST00000109441.2; ENSMUSP00000105067.2; ENSMUSG00000053141.17. [Q99M80-2]
DR   Ensembl; ENSMUST00000109443.8; ENSMUSP00000105069.2; ENSMUSG00000053141.17. [Q99M80-3]
DR   Ensembl; ENSMUST00000109445.9; ENSMUSP00000105071.3; ENSMUSG00000053141.17. [Q99M80-4]
DR   GeneID; 19281; -.
DR   KEGG; mmu:19281; -.
DR   UCSC; uc008nrw.2; mouse. [Q99M80-4]
DR   UCSC; uc008nrx.2; mouse. [Q99M80-3]
DR   UCSC; uc008nrz.2; mouse. [Q99M80-2]
DR   AGR; MGI:1321152; -.
DR   CTD; 11122; -.
DR   MGI; MGI:1321152; Ptprt.
DR   VEuPathDB; HostDB:ENSMUSG00000053141; -.
DR   eggNOG; KOG4228; Eukaryota.
DR   GeneTree; ENSGT00940000155326; -.
DR   HOGENOM; CLU_001645_0_1_1; -.
DR   InParanoid; Q99M80; -.
DR   OMA; XPMQETV; -.
DR   OrthoDB; 2875525at2759; -.
DR   TreeFam; TF312900; -.
DR   BioGRID-ORCS; 19281; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Ptprt; mouse.
DR   PRO; PR:Q99M80; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q99M80; Protein.
DR   Bgee; ENSMUSG00000053141; Expressed in piriform cortex and 116 other cell types or tissues.
DR   ExpressionAtlas; Q99M80; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0051393; F:alpha-actinin binding; IDA:MGI.
DR   GO; GO:0045294; F:alpha-catenin binding; IDA:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
DR   GO; GO:0045296; F:cadherin binding; IPI:MGI.
DR   GO; GO:0070097; F:delta-catenin binding; IPI:MGI.
DR   GO; GO:0045295; F:gamma-catenin binding; IPI:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:MGI.
DR   GO; GO:0097677; F:STAT family protein binding; ISO:MGI.
DR   GO; GO:0016790; F:thiolester hydrolase activity; IDA:MGI.
DR   GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISO:MGI.
DR   GO; GO:0071354; P:cellular response to interleukin-6; ISO:MGI.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR   GO; GO:1904893; P:negative regulation of receptor signaling pathway via STAT; ISO:MGI.
DR   GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:MGI.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd06263; MAM; 1.
DR   CDD; cd14630; R-PTPc-T-1; 1.
DR   CDD; cd14634; R-PTPc-T-2; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; IPR000998; MAM_dom.
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; PTHR24051:SF8; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00020; MAMDOMAIN.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00740; MAM_1; 1.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
DR   Genevisible; Q99M80; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Protein phosphatase;
KW   Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..1454
FT                   /note="Receptor-type tyrosine-protein phosphatase T"
FT                   /id="PRO_0000025464"
FT   TOPO_DOM        30..770
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        771..791
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        792..1454
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          34..195
FT                   /note="MAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   DOMAIN          197..288
FT                   /note="Ig-like C2-type"
FT   DOMAIN          295..388
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          393..487
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          488..594
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          670..767
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          902..1156
FT                   /note="Tyrosine-protein phosphatase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   DOMAIN          1188..1450
FT                   /note="Tyrosine-protein phosphatase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          800..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..852
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1097
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1391
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1065
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1097..1103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        425
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        605
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        658
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        688
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        217..271
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         731..749
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11423001, ECO:0000303|Ref.3,
FT                   ECO:0000303|Ref.4"
FT                   /id="VSP_007803"
FT   VAR_SEQ         794
FT                   /note="R -> RRNAYSYSYYL (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT                   /id="VSP_007804"
FT   VAR_SEQ         794
FT                   /note="R -> RRNAYSYSYYLSQR (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11423001"
FT                   /id="VSP_007805"
FT   VAR_SEQ         1007
FT                   /note="R -> RHPAEHTVGTATLGRAASPGM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11423001, ECO:0000303|Ref.3"
FT                   /id="VSP_007806"
FT   CONFLICT        13..16
FT                   /note="Missing (in Ref. 1; AAD34158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="R -> P (in Ref. 1; AAD34158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34..37
FT                   /note="GGCS -> RGVF (in Ref. 1; AAD34158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="A -> T (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="A -> S (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        266
FT                   /note="I -> V (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        602
FT                   /note="T -> S (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        822
FT                   /note="A -> T (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        825
FT                   /note="G -> S (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        844..845
FT                   /note="TD -> N (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1016
FT                   /note="D -> A (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1049
FT                   /note="Y -> H (in Ref. 1; AAD34158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1050
FT                   /note="H -> N (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1076
FT                   /note="L -> V (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1103
FT                   /note="R -> K (in Ref. 1; AAD34158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1259
FT                   /note="F -> L (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1266
FT                   /note="L -> I (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1269
FT                   /note="T -> S (in Ref. 4; AAF82401)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1454 AA;  163012 MW;  C60464F7B423F8A8 CRC64;
     MGSLGGLALC LLRLLLLGLQ RPPLPGAGAQ SAAGGCSFDE HYSNCGYSVA LGTNGFTWEQ
     INTWEKPMLD PAVPTGSFMM VNSSGRASGQ KAHLLLPTLK ENDTHCIDFH YYFSSRDRSS
     PGALNVYVKV NGGPQGNPVW NVSGVVTEGW VKAELAISTF WPHFYQVIFE SVSLKGHPGY
     IAVDEVRVLA HPCRKAPHFL RLQNVEVNVG QNATFQCIAG GKWSQHDKLW LQQWNGRDTA
     LMVTRVVNHR RFSATVSVAD TSQRSISKYR CVIRSDGGSG VSNYAELIVK EPPTPIAPPE
     LLAVGATYLW IKPNANSIIG DGPIILKEVE YRTTTGTWAE THIVDSPNYK LWHLDPDVEY
     EIRVLLTRPG EGGTGPPGPP LTTRTKCADP VHGPQNVEIV DIRARQLTLQ WEPFGYAVTR
     CHSYNLTVQY QYVFNQQQYE AEEVIQTSSH YTLRGLRPFM TIRLRLLLSN PEGRMESEEL
     VVQTEEDVPG AVPLESIQGG PFEEKIYIQW KPPNETNGVI TLYEINYKAV GSLDPSADLS
     SQRGKVFKLR NETHHLFVGL YPGTTYSFTI KASTAKGFGP PVTTRIATKI SAPSMPEYDA
     DTPLNETDTT ITVMLKPAQS RGAPVSVYQL VVKEERLQKS RRAADIIECF SVPVSYRNAS
     NLDSLHYFAA ELKPSNLPVT QPFTVGDNKT YNGYWNPPLS PLKSYSIYFQ ALSKANGETK
     INCVRLATKG APMGSAQVTP GTPLCLLTTA STQNSNTVEP EKQVDNTVKM AGVIAGLLMF
     IIILLGVMLT IKRRKLAKKQ KETQSGAQRE MGPVASTDKP TAKLGTNRND EGFSSSSQDV
     NGFTDGSRGE LSQPTLTIQT HPYRTCDPVE MSYPRDQFQP AIRVADLLQH ITQMKRGQGY
     GFKEEYEALP EGQTASWDTA KEDENRNKNR YGNIISYDHS RVRLLVLDGD PHSDYINANY
     IDGYHRPRHY IATQGPMQET VKDFWRMIWQ ENSASIVMVT NLVEVGRVKC VRYWPDDTEV
     YGDIKVTLIE TEPLAEYVIR TFTVQKKGYH EIRELRLFHF TSWPDHGVPC YATGLLGFVR
     QVKFLNPPEA GPIVVHCSAG AGRTGCFIAI DTMLDMAENE GVVDIFNCVR ELRAQRVNLV
     QTEEQYVFVH DAILEACLCG NTAIPVCEFR SLYYNISRLD PQTNSSQIKD EFQTLNIVTP
     RVRPEDCSIG LLPRNHDKNR SMDVLPLDRC LPFLISVDGE SSNYINAALM DSHKQPAAFV
     VTQHPLPNTV ADFWRLVFDY NCSSVVMLNE MDTAQLCMQY WPEKTSGCYG PIQVEFVSAD
     IDEDIIHRIF RICNMARPQD GYRIVQHLQY IGWPAYRDTP PSKRSLLKVV RRLEKWQEQY
     DGREGRTVVH CLNGGGRSGT FCAICSVCEM IQQQNIIDVF HIVKTLRNNK SNMVETLEQY
     KFVYEVALEY LSSF
//