ID   PTN9_HUMAN              Reviewed;         593 AA.
AC   P43378; Q53XR9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 221.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 9;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase MEG2;
DE            Short=PTPase MEG2;
GN   Name=PTPN9;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=1557404; DOI=10.1073/pnas.89.7.2980;
RA   Gu M., Warshawsky I., Majerus P.W.;
RT   "Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-
RT   phosphatase with sequence homology to retinaldehyde-binding protein and
RT   yeast SEC14p.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2980-2984(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 277-582, AND FUNCTION.
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 tyrosine
RT   phosphatome.";
RL   Cell 136:352-363(2009).
CC   -!- FUNCTION: Protein-tyrosine phosphatase that could participate in the
CC       transfer of hydrophobic ligands or in functions of the Golgi apparatus.
CC       {ECO:0000269|PubMed:19167335}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- INTERACTION:
CC       P43378; Q6RW13: AGTRAP; NbExp=5; IntAct=EBI-742898, EBI-741181;
CC       P43378; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-742898, EBI-11522760;
CC       P43378; Q13520: AQP6; NbExp=3; IntAct=EBI-742898, EBI-13059134;
CC       P43378; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-742898, EBI-11343438;
CC       P43378; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-742898, EBI-714543;
CC       P43378; P18859: ATP5PF; NbExp=3; IntAct=EBI-742898, EBI-2606700;
CC       P43378; Q8WZ55: BSND; NbExp=3; IntAct=EBI-742898, EBI-7996695;
CC       P43378; P51861: CDR1; NbExp=3; IntAct=EBI-742898, EBI-2836538;
CC       P43378; Q9HA82: CERS4; NbExp=3; IntAct=EBI-742898, EBI-2622997;
CC       P43378; Q8IZR5-2: CMTM4; NbExp=3; IntAct=EBI-742898, EBI-17278014;
CC       P43378; Q96DZ9: CMTM5; NbExp=4; IntAct=EBI-742898, EBI-2548702;
CC       P43378; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-742898, EBI-11522780;
CC       P43378; Q9NZJ6: COQ3; NbExp=3; IntAct=EBI-742898, EBI-10897372;
CC       P43378; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-742898, EBI-18013275;
CC       P43378; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-742898, EBI-6942903;
CC       P43378; Q9GZP9: DERL2; NbExp=3; IntAct=EBI-742898, EBI-7962814;
CC       P43378; Q15125: EBP; NbExp=3; IntAct=EBI-742898, EBI-3915253;
CC       P43378; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-742898, EBI-10973142;
CC       P43378; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-742898, EBI-3918971;
CC       P43378; O00258: GET1; NbExp=3; IntAct=EBI-742898, EBI-18908258;
CC       P43378; P10912: GHR; NbExp=2; IntAct=EBI-742898, EBI-286316;
CC       P43378; P08034: GJB1; NbExp=3; IntAct=EBI-742898, EBI-17565645;
CC       P43378; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-742898, EBI-3917143;
CC       P43378; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-742898, EBI-1052304;
CC       P43378; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-742898, EBI-18053395;
CC       P43378; Q9H400: LIME1; NbExp=3; IntAct=EBI-742898, EBI-2830566;
CC       P43378; Q969L2: MAL2; NbExp=4; IntAct=EBI-742898, EBI-944295;
CC       P43378; P46459: NSF; NbExp=2; IntAct=EBI-742898, EBI-712251;
CC       P43378; Q96AL5: PBX3; NbExp=3; IntAct=EBI-742898, EBI-741171;
CC       P43378; O00623: PEX12; NbExp=3; IntAct=EBI-742898, EBI-594836;
CC       P43378; O60664: PLIN3; NbExp=3; IntAct=EBI-742898, EBI-725795;
CC       P43378; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-742898, EBI-14065960;
CC       P43378; O95197: RTN3; NbExp=5; IntAct=EBI-742898, EBI-740467;
CC       P43378; O95197-3: RTN3; NbExp=3; IntAct=EBI-742898, EBI-11525735;
CC       P43378; O15126: SCAMP1; NbExp=3; IntAct=EBI-742898, EBI-954338;
CC       P43378; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-742898, EBI-12243266;
CC       P43378; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-742898, EBI-10262251;
CC       P43378; P30825: SLC7A1; NbExp=3; IntAct=EBI-742898, EBI-4289564;
CC       P43378; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-742898, EBI-10819434;
CC       P43378; P08247: SYP; NbExp=3; IntAct=EBI-742898, EBI-9071725;
CC       P43378; Q7Z6W1: TMCO2; NbExp=3; IntAct=EBI-742898, EBI-12807858;
CC       P43378; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-742898, EBI-11742770;
CC       P43378; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-742898, EBI-2548832;
CC       P43378; Q9Y320: TMX2; NbExp=3; IntAct=EBI-742898, EBI-6447886;
CC       P43378; O95070: YIF1A; NbExp=3; IntAct=EBI-742898, EBI-2799703;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class 3 subfamily. {ECO:0000305}.
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DR   EMBL; M83738; AAA60226.1; -; mRNA.
DR   EMBL; BT007405; AAP36073.1; -; mRNA.
DR   EMBL; BC010863; AAH10863.1; -; mRNA.
DR   CCDS; CCDS10280.1; -.
DR   PIR; A42690; A42690.
DR   RefSeq; NP_002824.1; NM_002833.4.
DR   PDB; 2PA5; X-ray; 1.60 A; A/B=277-582.
DR   PDB; 4GE2; X-ray; 1.80 A; A/B=277-582.
DR   PDB; 4GE5; X-ray; 2.00 A; A/B=277-582.
DR   PDB; 4GE6; X-ray; 1.40 A; A/B=277-582.
DR   PDB; 4ICZ; X-ray; 1.90 A; A=277-582.
DR   PDB; 6KZQ; X-ray; 1.70 A; A=277-583.
DR   PDB; 6L03; X-ray; 2.08 A; A=277-583.
DR   AlphaFoldDB; P43378; -.
DR   MDRepo; P43378; -.
DR   SMR; P43378; -.
DR   BioGRID; 111744; 118.
DR   FunCoup; P43378; 3092.
DR   IntAct; P43378; 59.
DR   MINT; P43378; -.
DR   NDEx; IQUERY-CP-PTPN9; 3 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000482732; -.
DR   BindingDB; P43378; -.
DR   ChEMBL; CHEMBL6117; -.
DR   DEPOD; PTPN9; -.
DR   iPTMnet; P43378; -.
DR   MetOSite; P43378; -.
DR   PhosphoSitePlus; P43378; -.
DR   BioMuta; PTPN9; -.
DR   DMDM; 1172724; -.
DR   jPOST; P43378; -.
DR   MassIVE; P43378; -.
DR   PaxDb; 9606-ENSP00000482732; -.
DR   PeptideAtlas; P43378; -.
DR   ProteomicsDB; 55630; -.
DR   Pumba; P43378; -.
DR   Antibodypedia; 27331; 129 antibodies from 29 providers.
DR   DNASU; 5780; -.
DR   Ensembl; ENST00000618819.5; ENSP00000482732.1; ENSG00000169410.12.
DR   GeneID; 5780; -.
DR   KEGG; hsa:5780; -.
DR   MANE-Select; ENST00000618819.5; ENSP00000482732.1; NM_002833.4; NP_002824.1.
DR   UCSC; uc002bal.5; human.
DR   AGR; HGNC:9661; -.
DR   ClinPGx; PA34005; -.
DR   CTD; 5780; -.
DR   DisGeNET; 5780; -.
DR   GeneCards; PTPN9; -.
DR   HGNC; HGNC:9661; PTPN9.
DR   HPA; ENSG00000169410; Low tissue specificity.
DR   MIM; 600768; gene.
DR   OpenTargets; ENSG00000169410; -.
DR   VEuPathDB; HostDB:ENSG00000169410; -.
DR   eggNOG; ENOG502QR81; Eukaryota.
DR   GeneTree; ENSGT00940000157447; -.
DR   InParanoid; P43378; -.
DR   OMA; DLASWNF; -.
DR   OrthoDB; 10051650at2759; -.
DR   PAN-GO; P43378; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; P43378; -.
DR   BRENDA; 3.1.3.48; 2681.
DR   PathwayCommons; P43378; -.
DR   Reactome; R-HSA-9008059; Interleukin-37 signaling.
DR   SignaLink; P43378; -.
DR   SIGNOR; P43378; -.
DR   Agora; ENSG00000169410; -.
DR   BioGRID-ORCS; 5780; 21 hits in 1174 CRISPR screens.
DR   CD-CODE; 91857CE7; Nucleolus.
DR   ChiTaRS; PTPN9; human.
DR   EvolutionaryTrace; P43378; -.
DR   GeneWiki; PTPN9; -.
DR   GenomeRNAi; 5780; -.
DR   Pharos; P43378; Tchem.
DR   PRO; PR:P43378; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P43378; protein.
DR   Bgee; ENSG00000169410; Expressed in ventricular zone and 165 other cell types or tissues.
DR   ExpressionAtlas; P43378; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:ProtInc.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IDA:MGI.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:MGI.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd14543; PTPc-N9; 1.
DR   CDD; cd00170; SEC14; 1.
DR   FunFam; 3.40.525.10:FF:000005; Tyrosine-protein phosphatase non-receptor type 9; 1.
DR   FunFam; 3.90.190.10:FF:000026; tyrosine-protein phosphatase non-receptor type 9; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR011074; CRAL/TRIO_N_dom.
DR   InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR050348; Protein-Tyr_Phosphatase.
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:SF285; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 9; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
DR   PDBsum; 2PA5; -.
DR   PDBsum; 4GE2; -.
DR   PDBsum; 4GE5; -.
DR   PDBsum; 4GE6; -.
DR   PDBsum; 4ICZ; -.
DR   PDBsum; 6KZQ; -.
DR   PDBsum; 6L03; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Hydrolase; Protein phosphatase;
KW   Proteomics identification; Reference proteome.
FT   CHAIN           1..593
FT                   /note="Tyrosine-protein phosphatase non-receptor type 9"
FT                   /id="PRO_0000094764"
FT   DOMAIN          84..243
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   DOMAIN          303..574
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        515
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         470
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         515..521
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         559
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   HELIX           288..312
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   HELIX           320..323
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   TURN            325..327
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   HELIX           328..330
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   TURN            340..342
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   HELIX           344..346
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          359..365
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          368..375
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   HELIX           376..379
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   HELIX           380..382
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   HELIX           383..392
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          397..400
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          404..406
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          423..426
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          429..438
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          440..451
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   TURN            452..455
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          456..465
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          470..472
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   HELIX           478..497
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   HELIX           508..510
FT                   /evidence="ECO:0007829|PDB:6L03"
FT   STRAND          511..514
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          516..519
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   HELIX           520..538
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   STRAND          539..541
FT                   /evidence="ECO:0007829|PDB:6KZQ"
FT   HELIX           543..550
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   TURN            551..553
FT                   /evidence="ECO:0007829|PDB:4GE6"
FT   HELIX           561..577
FT                   /evidence="ECO:0007829|PDB:4GE6"
SQ   SEQUENCE   593 AA;  68020 MW;  9BD75A5A986DDA0B CRC64;
     MEPATAPRPD MAPELTPEEE QATKQFLEEI NKWTVQYNVS PLSWNVAVKF LMARKFDVLR
     AIELFHSYRE TRRKEGIVKL KPHEEPLRSE ILSGKFTILN VRDPTGASIA LFTARLHHPH
     KSVQHVVLQA LFYLLDRAVD SFETQRNGLV FIYDMCGSNY ANFELDLGKK VLNLLKGAFP
     ARLKKVLIVG APIWFRVPYS IISLLLKDKV RERIQILKTS EVTQHLPREC LPENLGGYVK
     IDLATWNFQF LPQVNGHPDP FDEIILFSLP PALDWDSVHV PGPHAMTIQE LVDYVNARQK
     QGIYEEYEDI RRENPVGTFH CSMSPGNLEK NRYGDVPCLD QTRVKLTKRS GHTQTDYINA
     SFMDGYKQKN AYIGTQGPLE NTYRDFWLMV WEQKVLVIVM TTRFEEGGRR KCGQYWPLEK
     DSRIRFGFLT VTNLGVENMN HYKKTTLEIH NTEERQKRQV THFQFLSWPD YGVPSSAASL
     IDFLRVVRNQ QSLAVSNMGA RSKGQCPEPP IVVHCSAGIG RTGTFCSLDI CLAQLEELGT
     LNVFQTVSRM RTQRAFSIQT PEQYYFCYKA ILEFAEKEGM VSSGQNLLAV ESQ
//