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Database: UniProt
Entry: P35992
LinkDB: P35992
Original site: P35992 
ID   PTP10_DROME             Reviewed;        1631 AA.
AC   P35992; A4V4B4; B7Z142; Q0KHT5; Q86NN9; Q8IR87; Q9VYW1;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 3.
DT   09-JUL-2014, entry version 131.
DE   RecName: Full=Tyrosine-protein phosphatase 10D;
DE            EC=3.1.3.48;
DE   AltName: Full=Receptor-linked protein-tyrosine phosphatase 10D;
DE            Short=DPTP10D;
DE   Flags: Precursor;
GN   Name=Ptp10D; ORFNames=CG1817;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND E), FUNCTION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=1657401; DOI=10.1016/0092-8674(91)90062-4;
RA   Yang X., Seow K.T., Bahri S.M., Oon S.H., Chia W.;
RT   "Two Drosophila receptor-like tyrosine phosphatase genes are expressed
RT   in a subset of developing axons and pioneer neurons in the embryonic
RT   CNS.";
RL   Cell 67:661-673(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=1657402; DOI=10.1016/0092-8674(91)90063-5;
RA   Tian S.-S., Tsoulfas P., Zinn K.;
RT   "Three receptor-linked protein-tyrosine phosphatases are selectively
RT   expressed on central nervous system axons in the Drosophila embryo.";
RL   Cell 67:675-685(1991).
RN   [3]
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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May have a role in axon outgrowth and guidance.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=B; Synonyms=Long;
CC         IsoId=P35992-1; Sequence=Displayed;
CC       Name=A; Synonyms=D;
CC         IsoId=P35992-3; Sequence=VSP_015266;
CC         Note=No experimental confirmation available;
CC       Name=E; Synonyms=Short;
CC         IsoId=P35992-2; Sequence=VSP_005143, VSP_005144;
CC   -!- TISSUE SPECIFICITY: In 9-12 hour embryos, expression is
CC       specifically seen in the anterior commissure and its junctions
CC       with the longitudinal tracts.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed throughout development to adulthood, lowest expression
CC       is during second and third larval instars.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class subfamily.
CC   -!- SIMILARITY: Contains 12 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR   EMBL; M80465; AAA28484.1; -; mRNA.
DR   EMBL; M80538; AAA28952.1; -; mRNA.
DR   EMBL; AE014298; AAF48072.3; -; Genomic_DNA.
DR   EMBL; AE014298; AAS65319.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAS65320.1; -; Genomic_DNA.
DR   EMBL; AE014298; ACL82919.1; -; Genomic_DNA.
DR   EMBL; BT004474; AAO42638.1; -; mRNA.
DR   PIR; C41214; C41214.
DR   PIR; D41214; D41214.
DR   RefSeq; NP_001138187.1; NM_001144715.2. [P35992-2]
DR   RefSeq; NP_001259454.1; NM_001272525.1. [P35992-2]
DR   RefSeq; NP_727544.2; NM_167292.3. [P35992-1]
DR   RefSeq; NP_996413.2; NM_206690.2.
DR   RefSeq; NP_996414.2; NM_206691.3.
DR   UniGene; Dm.7386; -.
DR   PDB; 3S3E; X-ray; 2.40 A; A/B=1250-1533.
DR   PDB; 3S3F; X-ray; 2.70 A; A/B=1250-1533.
DR   PDB; 3S3H; X-ray; 2.80 A; A/B=1250-1533.
DR   PDB; 3S3K; X-ray; 3.20 A; A/B=1250-1533.
DR   PDBsum; 3S3E; -.
DR   PDBsum; 3S3F; -.
DR   PDBsum; 3S3H; -.
DR   PDBsum; 3S3K; -.
DR   ProteinModelPortal; P35992; -.
DR   SMR; P35992; 1249-1531.
DR   BioGrid; 58524; 4.
DR   IntAct; P35992; 2.
DR   PaxDb; P35992; -.
DR   PRIDE; P35992; -.
DR   EnsemblMetazoa; FBtr0073522; FBpp0073369; FBgn0004370. [P35992-1]
DR   GeneID; 32115; -.
DR   KEGG; dme:Dmel_CG1817; -.
DR   CTD; 32115; -.
DR   FlyBase; FBgn0004370; Ptp10D.
DR   eggNOG; COG5599; -.
DR   GeneTree; ENSGT00750000117631; -.
DR   InParanoid; P35992; -.
DR   KO; K05694; -.
DR   OrthoDB; EOG7PCJFZ; -.
DR   PhylomeDB; P35992; -.
DR   ChiTaRS; Ptp10D; drosophila.
DR   GenomeRNAi; 32115; -.
DR   NextBio; 776913; -.
DR   PRO; PR:P35992; -.
DR   Bgee; P35992; -.
DR   GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR   GO; GO:0030424; C:axon; IDA:FlyBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:FlyBase.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:FlyBase.
DR   GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISS:FlyBase.
DR   GO; GO:0007411; P:axon guidance; IGI:FlyBase.
DR   GO; GO:0007417; P:central nervous system development; IGI:FlyBase.
DR   GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR   GO; GO:0008045; P:motor neuron axon guidance; IGI:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; IGI:FlyBase.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:GOC.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
DR   Gene3D; 2.60.40.10; -; 9.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Pfam; PF00041; fn3; 10.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 11.
DR   SMART; SM00194; PTPc; 1.
DR   SUPFAM; SSF49265; SSF49265; 6.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50853; FN3; 9.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome;
KW   Developmental protein; Differentiation; Glycoprotein; Hydrolase;
KW   Membrane; Neurogenesis; Protein phosphatase; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     42       Potential.
FT   CHAIN        43   1631       Tyrosine-protein phosphatase 10D.
FT                                /FTId=PRO_0000025427.
FT   TOPO_DOM     43   1197       Extracellular (Potential).
FT   TRANSMEM   1198   1218       Helical; (Potential).
FT   TOPO_DOM   1219   1631       Cytoplasmic (Potential).
FT   DOMAIN       43    119       Fibronectin type-III 1.
FT   DOMAIN      125    218       Fibronectin type-III 2.
FT   DOMAIN      219    314       Fibronectin type-III 3.
FT   DOMAIN      309    402       Fibronectin type-III 4.
FT   DOMAIN      407    498       Fibronectin type-III 5.
FT   DOMAIN      499    584       Fibronectin type-III 6.
FT   DOMAIN      585    674       Fibronectin type-III 7.
FT   DOMAIN      675    771       Fibronectin type-III 8.
FT   DOMAIN      775    865       Fibronectin type-III 9.
FT   DOMAIN      866    956       Fibronectin type-III 10.
FT   DOMAIN      957   1057       Fibronectin type-III 11.
FT   DOMAIN     1049   1190       Fibronectin type-III 12.
FT   DOMAIN     1272   1527       Tyrosine-protein phosphatase.
FT   REGION     1468   1474       Substrate binding (By similarity).
FT   ACT_SITE   1468   1468       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING    1436   1436       Substrate (By similarity).
FT   BINDING    1512   1512       Substrate (By similarity).
FT   CARBOHYD     75     75       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    106    106       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    128    128       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    169    169       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    212    212       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    229    229       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    259    259       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    289    289       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    317    317       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    471    471       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    486    486       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    512    512       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    533    533       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    588    588       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    668    668       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    687    687       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    719    719       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    723    723       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    823    823       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    841    841       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    874    874       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    908    908       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    925    925       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1001   1001       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1104   1104       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1136   1136       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1195   1195       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ    1549   1558       GQQVQLDENG -> DDEGIAESGM (in isoform E).
FT                                /FTId=VSP_005143.
FT   VAR_SEQ    1559   1631       Missing (in isoform E).
FT                                /FTId=VSP_005144.
FT   VAR_SEQ    1626   1631       VDAPDR -> PSSMICKDSKGGNIDVLESQQQQQQQQQQQP
FT                                NQGGHNITTISAINGYNTLQHRRKSQLITFSSSSCDIKNSL
FT                                SHEYINGSNGSAANGPPSSGSGSGSGPGSNRASRANVRLSF
FT                                AEEDVMILPQNHSQQSNHQDDEVFTRRRSLLEVEIGVEVGE
FT                                DGELAPHEMEEDLEEEDEDEELYMHDEFETHIDTKSNNAND
FT                                DSGGGSYEDSHALHSSLGGSNRNSLEKDDDDIEVDVISTDV
FT                                SCYDQLLGSSCNTRNGDDDDIATLVGDGDYSTTKLSKASRL
FT                                SGAGVGGLVVSGGGGGTAIGGGIAVNGGGVLGNGVGSEAGG
FT                                GIIYANPFMDDEGIAESGM (in isoform A).
FT                                /FTId=VSP_015266.
FT   CONFLICT    124    124       D -> I (in Ref. 1; AAA28484).
FT   CONFLICT    127    127       S -> L (in Ref. 1; AAA28484).
FT   CONFLICT    188    188       P -> L (in Ref. 5; AAO42638).
FT   CONFLICT    369    369       F -> S (in Ref. 1; AAA28484 and 2;
FT                                AAA28952).
FT   CONFLICT    558    558       G -> A (in Ref. 1; AAA28484 and 2;
FT                                AAA28952).
FT   CONFLICT    810    810       L -> S (in Ref. 1; AAA28484 and 2;
FT                                AAA28952).
FT   CONFLICT   1403   1403       N -> S (in Ref. 5; AAO42638).
FT   HELIX      1254   1256
FT   HELIX      1257   1277
FT   TURN       1278   1285
FT   HELIX      1290   1292
FT   TURN       1294   1296
FT   HELIX      1297   1299
FT   HELIX      1309   1311
FT   STRAND     1312   1314
FT   TURN       1319   1321
FT   TURN       1322   1325
FT   STRAND     1326   1332
FT   STRAND     1340   1344
FT   HELIX      1349   1351
FT   HELIX      1352   1361
FT   STRAND     1366   1369
FT   STRAND     1373   1375
FT   STRAND     1387   1390
FT   STRAND     1392   1394
FT   STRAND     1397   1406
FT   STRAND     1408   1419
FT   STRAND     1422   1431
FT   STRAND     1436   1438
FT   HELIX      1444   1457
FT   STRAND     1464   1467
FT   STRAND     1469   1472
FT   HELIX      1473   1487
FT   TURN       1488   1490
FT   STRAND     1492   1494
FT   HELIX      1496   1506
FT   HELIX      1514   1528
SQ   SEQUENCE   1631 AA;  185081 MW;  22A59AB61665875D CRC64;
     MLYQLSKATT RIRLKRQKAV PQHRWLWSLA FLAAFTLKDV RCADLAISIP NNPGLDDGAS
     YRLDYSPPFG YPEPNTTIAS REIGDEIQFS RALPGTKYNF WLYYTNFTHH DWLTWTVTIT
     TAPDPPSNLS VQVRSGKNAI ILWSPPTQGS YTAFKIKVLG LSEASSSYNR TFQVNDNTFQ
     HSVKELTPGA TYQVQAYTIY DGKESVAYTS RNFTTKPNTP GKFIVWFRNE TTLLVLWQPP
     YPAGIYTHYK VSIEPPDAND SVLYVEKEGE PPGPAQAAFK GLVPGRAYNI SVQTMSEDEI
     SLPTTAQYRT VPLRPLNVTF DRDFITSNSF RVLWEAPKGI SEFDKYQVSV ATTRRQSTVP
     RSNEPVAFFD FRDIAEPGKT FNVIVKTVSG KVTSWPATGD VTLRPLPVRN LRSINDDKTN
     TMIITWEADP ASTQDEYRIV YHELETFNGD TSTLTTDRTR FTLESLLPGR NYSLSVQAVS
     KKMESNETSI FVVTRPSSPI IEDLKSIRMG LNISWKSDVN SKQEQYEVLY SRNGTSDLRT
     QKTKESRLVI KNLQPGAGYE LKVFAVSHDL RSEPHAYFQA VYPNPPRNMT IETVRSNSVL
     VHWSPPESGE FTEYSIRYRT DSEQQWVRLP SVRSTEADIT DMTKGEKYTI QVNTVSFGVE
     SPVPQEVNTT VPPNPVSNII QLVDSRNITL EWPKPEGRVE SYILKWWPSD NPGRVQTKNV
     SENKSADDLS TVRVLIGELM PGVQYKFDIQ TTSYGILSGI TSLYPRTMPL IQSDVVVANG
     EKEDERDTIT LSYTPTPQSS SKFDIYRFSL GDAEIRDKEK LANDTDRKVT FTGLVPGRLY
     NITVWTVSGG VASLPIQRQD RLYPEPITQL HATNITDTEI SLRWDLPKGE YNDFDIAYLT
     ADNLLAQNMT TRNEITISDL RPHRNYTFTV VVRSGTESSV LRSSSPLSAS FTTNEAVPGR
     VERFHPTDVQ PSEINFEWSL PSSEANGVIR QFSIAYTNIN NLTDAGMQDF ESEEAFGVIK
     NLKPGETYVF KIQAKTAIGF GPEREYRQTM PILAPPRPAT QVVPTEVYRS SSTIQIRFRK
     NYFSDQNGQV RMYTIIVAED DAKNASGLEM PSWLDVQSYS VWLPYQAIDP YYPFENRSVE
     DFTIGTENCD NHKIGYCNGP LKSGTTYRVK VRAFTGADKF TDTAYSFPIQ TDQDNTSLIV
     AITVPLTIIL VLLVTLLFYK RRRNNCRKTT KDSRANDNMS LPDSVIEQNR PILIKNFAEH
     YRLMSADSDF RFSEEFEELK HVGRDQPCTF ADLPCNRPKN RFTNILPYDH SRFKLQPVDD
     DEGSDYINAN YVPGHNSPRE FIVTQGPLHS TRDDFWRMCW ESNSRAIVML TRCFEKGREK
     CDQYWPNDTV PVFYGDIKVQ ILNDSHYADW VMTEFMLCRG SEQRILRHFH FTTWPDFGVP
     NPPQTLVRFV RAFRDRIGAE QRPIVVHCSA GVGRSGTFIT LDRILQQINT SDYVDIFGIV
     YAMRKERVWM VQTEQQYICI HQCLLAVLEG KENIVGPARE MHDNEGYEGQ QVQLDENGDV
     VATIEGHLSH HDLQQAEAEA IDDENAAILH DDQQPLTSSF TGHHTHMPPT TSMSSFGGGG
     GGHTNVDAPD R
//
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