PTPRT_MOUSE
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 03-AUG-2022, entry version 164.
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.ENSMUSP00000105071; -.
DR GlyGen; Q99M80; 10 sites.
DR iPTMnet; Q99M80; -.
DR PhosphoSitePlus; Q99M80; -.
DR MaxQB; Q99M80; -.
DR PaxDb; Q99M80; -.
DR PRIDE; Q99M80; -.
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; 110 antibodies from 32 providers.
DR DNASU; 19281; -.
DR Ensembl; ENSMUST00000109441; ENSMUSP00000105067; ENSMUSG00000053141. [Q99M80-2]
DR Ensembl; ENSMUST00000109443; ENSMUSP00000105069; ENSMUSG00000053141. [Q99M80-3]
DR Ensembl; ENSMUST00000109445; ENSMUSP00000105071; ENSMUSG00000053141. [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 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; IVECFSV; -.
DR OrthoDB; 411281at2759; -.
DR TreeFam; TF312900; -.
DR BioGRID-ORCS; 19281; 1 hit in 71 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 114 other tissues.
DR ExpressionAtlas; Q99M80; baseline and differential.
DR Genevisible; Q99M80; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma 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: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:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:MGI.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA: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 Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.90.190.10; -; 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 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; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
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.
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
