GenomeNet

Database: UniProt
Entry: P26045
LinkDB: P26045
Original site: P26045 
ID   PTN3_HUMAN              Reviewed;         913 AA.
AC   P26045; A0AUW9; E7EN99; E9PGU7;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   29-OCT-2014, entry version 147.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 3;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase H1;
DE            Short=PTP-H1;
GN   Name=PTPN3; Synonyms=PTPH1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-90.
RX   PubMed=1648725; DOI=10.1073/pnas.88.14.5949;
RA   Yang Q., Tonks N.K.;
RT   "Isolation of a cDNA clone encoding a human protein-tyrosine
RT   phosphatase with homology to the cytoskeletal-associated proteins band
RT   4.1, ezrin, and talin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5949-5953(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Fetal kidney, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 194-896 (ISOFORM 1).
RC   TISSUE=Colon;
RX   PubMed=1626183;
RA   Arimura Y., Hinoda Y., Itoh F., Takekawa M., Tsujisaki M., Adachi M.,
RA   Imai K., Yachi A.;
RT   "cDNA cloning of new protein tyrosine phosphatases in the human
RT   colon.";
RL   Tumor Biol. 13:180-186(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 899-913 (ISOFORM 1).
RX   PubMed=7874267; DOI=10.1007/BF02349278;
RA   Ikuta S., Itoh F., Hinoda Y., Toyota M., Makiguchi Y., Imai K.,
RA   Yachi A.;
RT   "Expression of cytoskeletal-associated protein tyrosine phosphatase
RT   PTPH1 mRNA in human hepatocellular carcinoma.";
RL   J. Gastroenterol. 29:727-732(1994).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359; SER-367; THR-376
RP   AND SER-381, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 628-913.
RX   PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
RA   Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
RA   Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
RT   "Large-scale structural analysis of the classical human protein
RT   tyrosine phosphatome.";
RL   Cell 136:352-363(2009).
CC   -!- FUNCTION: May act at junctions between the membrane and the
CC       cytoskeleton. Possesses tyrosine phosphatase activity.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
CC   -!- INTERACTION:
CC       P06463:E6 (xeno); NbExp=4; IntAct=EBI-1047946, EBI-1186926;
CC       P10912:GHR; NbExp=4; IntAct=EBI-1047946, EBI-286316;
CC       Q14524:SCN5A; NbExp=2; IntAct=EBI-1047946, EBI-726858;
CC       P55072:VCP; NbExp=2; IntAct=EBI-1047946, EBI-355164;
CC       P11473:VDR; NbExp=4; IntAct=EBI-1047946, EBI-286357;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P26045-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P26045-2; Sequence=VSP_046309;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=P26045-3; Sequence=VSP_046309, VSP_046310;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 FERM domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00084}.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00143}.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00160}.
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DR   EMBL; M64572; AAA35647.1; -; mRNA.
DR   EMBL; BX648253; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BX648735; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL359963; CAH71094.1; -; Genomic_DNA.
DR   EMBL; AL162733; CAH71094.1; JOINED; Genomic_DNA.
DR   EMBL; AL450025; CAH71094.1; JOINED; Genomic_DNA.
DR   EMBL; AL450025; CAH73252.1; -; Genomic_DNA.
DR   EMBL; AL162733; CAH73252.1; JOINED; Genomic_DNA.
DR   EMBL; AL359963; CAH73252.1; JOINED; Genomic_DNA.
DR   EMBL; AL162733; CAH73386.1; -; Genomic_DNA.
DR   EMBL; AL359963; CAH73386.1; JOINED; Genomic_DNA.
DR   EMBL; AL450025; CAH73386.1; JOINED; Genomic_DNA.
DR   EMBL; CH471105; EAW59046.1; -; Genomic_DNA.
DR   EMBL; BC126117; AAI26118.1; -; mRNA.
DR   EMBL; S39392; AAB22439.2; -; mRNA.
DR   EMBL; S76309; AAB33583.1; -; mRNA.
DR   CCDS; CCDS48000.1; -. [P26045-3]
DR   CCDS; CCDS48001.1; -. [P26045-2]
DR   CCDS; CCDS6776.1; -. [P26045-1]
DR   PIR; A41109; A41109.
DR   RefSeq; NP_001138840.1; NM_001145368.1.
DR   RefSeq; NP_001138841.1; NM_001145369.1. [P26045-2]
DR   RefSeq; NP_001138842.1; NM_001145370.1. [P26045-3]
DR   RefSeq; NP_001138843.1; NM_001145371.1.
DR   RefSeq; NP_002820.3; NM_002829.3. [P26045-1]
DR   RefSeq; XP_006717261.1; XM_006717198.1. [P26045-1]
DR   RefSeq; XP_006717262.1; XM_006717199.1. [P26045-1]
DR   RefSeq; XP_006717267.1; XM_006717204.1. [P26045-2]
DR   RefSeq; XP_006717269.1; XM_006717206.1. [P26045-3]
DR   UniGene; Hs.436429; -.
DR   PDB; 2B49; X-ray; 1.54 A; A=628-913.
DR   PDBsum; 2B49; -.
DR   ProteinModelPortal; P26045; -.
DR   SMR; P26045; 31-309, 508-595, 646-904.
DR   BioGrid; 111740; 7.
DR   IntAct; P26045; 15.
DR   MINT; MINT-246110; -.
DR   STRING; 9606.ENSP00000262539; -.
DR   ChEMBL; CHEMBL2396509; -.
DR   PhosphoSite; P26045; -.
DR   DMDM; 229462761; -.
DR   MaxQB; P26045; -.
DR   PaxDb; P26045; -.
DR   PRIDE; P26045; -.
DR   DNASU; 5774; -.
DR   Ensembl; ENST00000374541; ENSP00000363667; ENSG00000070159. [P26045-1]
DR   Ensembl; ENST00000412145; ENSP00000416654; ENSG00000070159. [P26045-2]
DR   Ensembl; ENST00000446349; ENSP00000395384; ENSG00000070159. [P26045-3]
DR   GeneID; 5774; -.
DR   KEGG; hsa:5774; -.
DR   UCSC; uc004beb.2; human. [P26045-1]
DR   CTD; 5774; -.
DR   GeneCards; GC09M112138; -.
DR   H-InvDB; HIX0025742; -.
DR   HGNC; HGNC:9655; PTPN3.
DR   HPA; HPA038343; -.
DR   MIM; 176877; gene.
DR   neXtProt; NX_P26045; -.
DR   Orphanet; 70567; Cholangiocarcinoma.
DR   PharmGKB; PA33999; -.
DR   eggNOG; COG5599; -.
DR   GeneTree; ENSGT00760000118823; -.
DR   HOGENOM; HOG000007048; -.
DR   HOVERGEN; HBG008322; -.
DR   InParanoid; P26045; -.
DR   KO; K18027; -.
DR   OMA; HFGDYNS; -.
DR   OrthoDB; EOG76HQ1B; -.
DR   PhylomeDB; P26045; -.
DR   TreeFam; TF315900; -.
DR   ChiTaRS; PTPN3; human.
DR   EvolutionaryTrace; P26045; -.
DR   GeneWiki; PTPN3; -.
DR   GenomeRNAi; 5774; -.
DR   NextBio; 22458; -.
DR   PRO; PR:P26045; -.
DR   Bgee; P26045; -.
DR   CleanEx; HS_PTPN3; -.
DR   ExpressionAtlas; P26045; baseline and differential.
DR   Genevestigator; P26045; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR   GO; GO:0001784; F:phosphotyrosine binding; IPI:BHF-UCL.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL.
DR   GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IMP:BHF-UCL.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:BHF-UCL.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:GOC.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:BHF-UCL.
DR   GO; GO:0098902; P:regulation of membrane depolarization during action potential; IDA:BHF-UCL.
DR   GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SUPFAM; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50106; PDZ; 1.
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; Cell membrane; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Hydrolase; Membrane; Phosphoprotein;
KW   Polymorphism; Protein phosphatase; Reference proteome.
FT   CHAIN         1    913       Tyrosine-protein phosphatase non-receptor
FT                                type 3.
FT                                /FTId=PRO_0000219433.
FT   DOMAIN       29    312       FERM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00084}.
FT   DOMAIN      510    582       PDZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      646    901       Tyrosine-protein phosphatase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   REGION      842    848       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    842    842       Phosphocysteine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160,
FT                                ECO:0000255|PROSITE-ProRule:PRU10044}.
FT   BINDING     811    811       Substrate. {ECO:0000250}.
FT   BINDING     886    886       Substrate. {ECO:0000250}.
FT   MOD_RES     359    359       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648}.
FT   MOD_RES     367    367       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648}.
FT   MOD_RES     376    376       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18669648}.
FT   MOD_RES     381    381       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648}.
FT   VAR_SEQ       1    131       Missing (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_046309.
FT   VAR_SEQ     335    379       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_046310.
FT   VARIANT      77     77       D -> N (in dbSNP:rs35285139).
FT                                /FTId=VAR_055252.
FT   VARIANT      90     90       A -> P (in dbSNP:rs3793524).
FT                                {ECO:0000269|PubMed:1648725}.
FT                                /FTId=VAR_055253.
FT   VARIANT     409    409       T -> A (in dbSNP:rs10979858).
FT                                /FTId=VAR_055254.
FT   VARIANT     605    605       F -> L (in dbSNP:rs7859962).
FT                                /FTId=VAR_055255.
FT   VARIANT     763    763       D -> N (in dbSNP:rs10116806).
FT                                /FTId=VAR_055256.
FT   CONFLICT    814    814       V -> I (in Ref. 1; AAA35647 and 6;
FT                                AAB22439). {ECO:0000305}.
FT   HELIX       649    652
FT   HELIX       664    666
FT   HELIX       668    673
FT   TURN        683    685
FT   STRAND      686    688
FT   STRAND      690    692
FT   STRAND      695    705
FT   HELIX       706    708
FT   STRAND      710    717
FT   TURN        722    724
FT   HELIX       725    734
FT   STRAND      739    742
FT   STRAND      746    748
FT   STRAND      764    767
FT   STRAND      770    779
FT   STRAND      781    792
FT   TURN        793    795
FT   STRAND      798    806
FT   STRAND      811    813
FT   HELIX       819    831
FT   STRAND      838    841
FT   STRAND      843    846
FT   HELIX       847    863
FT   HELIX       870    878
FT   HELIX       888    903
SQ   SEQUENCE   913 AA;  103990 MW;  44FBBFA35A5F2AFF CRC64;
     MTSRLRALGG RINNIRTSEL PKEKTRSEVI CSIHFLDGVV QTFKVTKQDT GQVLLDMVHN
     HLGVTEKEYF GLQHDDDSVD SPRWLEASKA IRKQLKGGFP CTLHFRVRFF IPDPNTLQQE
     QTRHLYFLQL KMDICEGRLT CPLNSAVVLA SYAVQSHFGD YNSSIHHPGY LSDSHFIPDQ
     NEDFLTKVES LHEQHSGLKQ SEAESCYINI ARTLDFYGVE LHSGRDLHNL DLMIGIASAG
     VAVYRKYICT SFYPWVNILK ISFKRKKFFI HQRQKQAESR EHIVAFNMLN YRSCKNLWKS
     CVEHHTFFQA KKLLPQEKNV LSQYWTMGSR NTKKSVNNQY CKKVIGGMVW NPAMRRSLSV
     EHLETKSLPS RSPPITPNWR SPRLRHEIRK PRHSSADNLA NEMTYITETE DVFYTYKGSL
     APQDSDSEVS QNRSPHQESL SENNPAQSYL TQKSSSSVSP SSNAPGSCSP DGVDQQLLDD
     FHRVTKGGST EDASQYYCDK NDNGDSYLVL IRITPDEDGK FGFNLKGGVD QKMPLVVSRI
     NPESPADTCI PKLNEGDQIV LINGRDISEH THDQVVMFIK ASRESHSREL ALVIRRRAVR
     SFADFKSEDE LNQLFPEAIF PMCPEGGDTL EGSMAQLKKG LESGTVLIQF EQLYRKKPGL
     AITFAKLPQN LDKNRYKDVL PYDTTRVLLQ GNEDYINASY VNMEIPAANL VNKYIATQGP
     LPHTCAQFWQ VVWDQKLSLI VMLTTLTERG RTKCHQYWPD PPDVMNHGGF HIQCQSEDCT
     IAYVSREMLV TNTQTGEEHT VTHLQYVAWP DHGVPDDSSD FLEFVNYVRS LRVDSEPVLV
     HCSAGIGRTG VLVTMETAMC LTERNLPIYP LDIVRKMRDQ RAMMVQTSSQ YKFVCEAILR
     VYEEGLVQML DPS
//
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