ID   PTP69_DROME             Reviewed;        1462 AA.
AC   P16620; Q8IGY3; Q9VU03;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Tyrosine-protein phosphatase 69D;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine-phosphate phosphohydrolase;
DE            Short=DPTP;
DE   Flags: Precursor;
GN   Name=Ptp69D; Synonyms=DPTP; ORFNames=CG10975;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), POSSIBLE FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=2554325; DOI=10.1073/pnas.86.22.8698;
RA   Streuli M., Krueger N.X., Tsai A.Y.M., Saito H.;
RT   "A family of receptor-linked protein tyrosine phosphatases in humans and
RT   Drosophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-58; ASN-613 AND ASN-701, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Possible cell adhesion receptor.
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:2554325};
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P16620-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P16620-2; Sequence=VSP_015257;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class subfamily. {ECO:0000305}.
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DR   EMBL; M27699; AAA28842.1; -; mRNA.
DR   EMBL; AE014296; AAF49892.2; -; Genomic_DNA.
DR   EMBL; AE014296; AAO41254.1; -; Genomic_DNA.
DR   EMBL; BT001531; AAN71286.1; -; mRNA.
DR   PIR; B36182; B36182.
DR   RefSeq; NP_524048.2; NM_079324.3. [P16620-1]
DR   RefSeq; NP_788502.1; NM_176324.2. [P16620-2]
DR   AlphaFoldDB; P16620; -.
DR   SMR; P16620; -.
DR   BioGRID; 64791; 12.
DR   IntAct; P16620; 9.
DR   MINT; P16620; -.
DR   STRING; 7227.FBpp0075645; -.
DR   GlyCosmos; P16620; 20 sites, No reported glycans.
DR   GlyGen; P16620; 20 sites.
DR   iPTMnet; P16620; -.
DR   PaxDb; 7227-FBpp0075645; -.
DR   EnsemblMetazoa; FBtr0075913; FBpp0075645; FBgn0014007. [P16620-1]
DR   EnsemblMetazoa; FBtr0075914; FBpp0075646; FBgn0014007. [P16620-2]
DR   GeneID; 39443; -.
DR   KEGG; dme:Dmel_CG10975; -.
DR   AGR; FB:FBgn0014007; -.
DR   CTD; 39443; -.
DR   FlyBase; FBgn0014007; Ptp69D.
DR   VEuPathDB; VectorBase:FBgn0014007; -.
DR   eggNOG; KOG4228; Eukaryota.
DR   GeneTree; ENSGT00940000174163; -.
DR   InParanoid; P16620; -.
DR   OMA; YSVQRGP; -.
DR   OrthoDB; 2875525at2759; -.
DR   PhylomeDB; P16620; -.
DR   SignaLink; P16620; -.
DR   BioGRID-ORCS; 39443; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 39443; -.
DR   PRO; PR:P16620; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0014007; Expressed in wing disc and 33 other cell types or tissues.
DR   ExpressionAtlas; P16620; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:FlyBase.
DR   GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IDA:FlyBase.
DR   GO; GO:0007411; P:axon guidance; IGI:FlyBase.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007415; P:defasciculation of motor neuron axon; IMP:FlyBase.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR   GO; GO:0097155; P:fasciculation of sensory neuron axon; IMP:FlyBase.
DR   GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:FlyBase.
DR   GO; GO:0016201; P:synaptic target inhibition; IMP:FlyBase.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd00047; PTPc; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
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; 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; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF495; TYROSINE-PROTEIN PHOSPHATASE 69D; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
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; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
DR   Genevisible; P16620; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW   Hydrolase; Immunoglobulin domain; Membrane; Protein phosphatase; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..1462
FT                   /note="Tyrosine-protein phosphatase 69D"
FT                   /id="PRO_0000025428"
FT   TOPO_DOM        29..805
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        806..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        824..1462
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..125
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          131..230
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          237..332
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          334..435
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          439..547
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          893..1156
FT                   /note="Tyrosine-protein phosphatase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   DOMAIN          1187..1450
FT                   /note="Tyrosine-protein phosphatase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
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   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        442
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        516
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        613
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        701
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        755
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        45..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        154..214
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         845
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_015257"
FT   CONFLICT        91
FT                   /note="I -> M (in Ref. 1; AAA28842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="A -> T (in Ref. 1; AAA28842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="K -> N (in Ref. 1; AAA28842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="R -> K (in Ref. 1; AAA28842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        638
FT                   /note="D -> A (in Ref. 1; AAA28842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        651
FT                   /note="D -> G (in Ref. 1; AAA28842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        990
FT                   /note="M -> I (in Ref. 1; AAA28842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1189
FT                   /note="V -> M (in Ref. 1; AAA28842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1265
FT                   /note="L -> F (in Ref. 1; AAA28842)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1462 AA;  167460 MW;  61214ADC778D319A CRC64;
     MALLYRRMSM LLNIILAYIF LCAICVQGSV KQEWAEIGKN VSLECASENE AVAWKLGNQT
     INKNHTRYKI RTEPLKSNDD GSENNDSQDF IKYKNVLALL DVNIKDSGNY TCTAQTGQNH
     STEFQVRPYL PSKVLQSTPD RIKRKIKQDV MLYCLIEMYP QNETTNRNLK WLKDGSQFEF
     LDTFSSISKL NDTHLNFTLE FTEVYKKENG TYKCTVFDDT GLEITSKEIT LFVMEVPQVS
     IDFAKAVGAN KIYLNWTVND GNDPIQKFFI TLQEAGTPTF TYHKDFINGS HTSYILDHFK
     PNTTYFLRIV GKNSIGNGQP TQYPQGITTL SYDPIFIPKV ETTGSTASTI TIGWNPPPPD
     LIDYIQYYEL IVSESGEVPK VIEEAIYQQN SRNLPYMFDK LKTATDYEFR VRACSDLTKT
     CGPWSENVNG TTMDGVATKP TNLSIQCHHD NVTRGNSIAI NWDVPKTPNG KVVSYLIHLL
     GNPMSTVDRE MWGPKIRRID EPHHKTLYES VSPNTNYTVT VSAITRHKKN GEPATGSCLM
     PVSTPDAIGR TMWSKVNLDS KYVLKLYLPK ISERNGPICC YRLYLVRINN DNKELPDPEK
     LNIATYQEVH SDNVTRSSAY IAEMISSKYF RPEIFLGDEK RFSENNDIIR DNDEICRKCL
     EGTPFLRKPE IIHIPPQGSL SNSDSELPIL SEKDNLIKGA NLTEHALKIL ESKLRDKRNA
     VTSDENPILS AVNPNVPLHD SSRDVFDGEI DINSNYTGFL EIIVRDRNNA LMAYSKYFDI
     ITPATEAEPI QSLNNMDYYL SIGVKAGAVL LGVILVFIVL WVFHHKKTKN ELQGEDTLTL
     RDSLSRALFG RRNHNHSHFI TSGNHKGFDA GPIHRLDLEN AYKNRHKDTD YGFLREYEML
     PNRFSDRTTK NSDLKENACK NRYPDIKAYD QTRVKLAVIN GLQTTDYINA NFVIGYKERK
     KFICAQGPME STIDDFWRMI WEQHLEIIVM LTNLEEYNKA KCAKYWPEKV FDTKQFGDIL
     VKFAQERKTG DYIERTLNVS KNKANVGEEE DRRQITQYHY LTWKDFMAPE HPHGIIKFIR
     QINSVYSLQR GPILVHCSAG VGRTGTLVAL DSLIQQLEEE DSVSIYNTVC DLRHQRNFLV
     QSLKQYIFLY RALLDTGTFG NTDICIDTMA SAIESLKRKP NEGKCKLEVE FEKLLATADE
     ISKSCSVGEN EENNMKNRSQ EIIPYDRNRV ILTPLPMREN STYINASFIE GYDNSETFII
     AQDPLENTIG DFWRMISEQS VTTLVMISEI GDGPRKCPRY WADDEVQYDH ILVKYVHSES
     CPYYTRREFY VTNCKIDDTL KVTQFQYNGW PTVDGEVPEV CRGIIELVDQ AYNHYKNNKN
     SGCRSPLTVH CSLGTDRSSI FVAMCILVQH LRLEKCVDIC ATTRKLRSQR TGLINSYAQY
     EFLHRAIINY SDLHHIAEST LD
//