ID   PTPRQ_HUMAN             Reviewed;        2332 AA.
AC   Q9UMZ3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   11-NOV-2015, entry version 103.
DE   RecName: Full=Phosphatidylinositol phosphatase PTPRQ;
DE            EC=3.1.3.-;
DE   AltName: Full=Receptor-type tyrosine-protein phosphatase Q;
DE            Short=PTP-RQ;
DE            Short=R-PTP-Q;
DE            EC=3.1.3.48;
DE   Flags: Precursor;
GN   Name=PTPRQ;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2133-2266.
RA   Dayton M.A., Blanchard K.L.;
RT   "Differential expression of PTPase RNAs resulting from K562
RT   differentiation induced by PMA.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12837292; DOI=10.1016/S0014-4827(03)00121-6;
RA   Seifert R.A., Coats S.A., Oganesian A., Wright M.B., Dishmon M.,
RA   Booth C.J., Johnson R.J., Alpers C.E., Bowen-Pope D.F.;
RT   "PTPRQ is a novel phosphatidylinositol phosphatase that can be
RT   expressed as a cytoplasmic protein or as a subcellularly localized
RT   receptor-like protein.";
RL   Exp. Cell Res. 287:374-386(2003).
RN   [4]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=19351528; DOI=10.1016/j.bbrc.2009.04.001;
RA   Jung H., Kim W.K., Kim do H., Cho Y.S., Kim S.J., Park S.G.,
RA   Park B.C., Lim H.M., Bae K.H., Lee S.C.;
RT   "Involvement of PTP-RQ in differentiation during adipogenesis of human
RT   mesenchymal stem cells.";
RL   Biochem. Biophys. Res. Commun. 383:252-257(2009).
RN   [5]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND VARIANT DFNB84A GLY-281.
RX   PubMed=20346435; DOI=10.1016/j.ajhg.2010.02.015;
RA   Schraders M., Oostrik J., Huygen P.L., Strom T.M., van Wijk E.,
RA   Kunst H.P., Hoefsloot L.H., Cremers C.W., Admiraal R.J., Kremer H.;
RT   "Mutations in PTPRQ are a cause of autosomal-recessive nonsyndromic
RT   hearing impairment DFNB84 and associated with vestibular
RT   dysfunction.";
RL   Am. J. Hum. Genet. 86:604-610(2010).
RN   [6]
RP   INVOLVEMENT IN DFNB84A, AND VARIANT GLU-471.
RX   PubMed=20472657; DOI=10.1136/jmg.2009.075697;
RA   Shahin H., Rahil M., Abu Rayan A., Avraham K.B., King M.C., Kanaan M.,
RA   Walsh T.;
RT   "Nonsense mutation of the stereociliar membrane protein gene PTPRQ in
RT   human hearing loss DFNB84.";
RL   J. Med. Genet. 47:643-645(2010).
CC   -!- FUNCTION: Phosphatidylinositol phosphatase required for auditory
CC       function. May act by regulating the level of phosphatidylinositol
CC       4,5-bisphosphate (PIP2) level in the basal region of hair bundles.
CC       Can dephosphorylate a broad range of phosphatidylinositol
CC       phosphates, including phosphatidylinositol 3,4,5-trisphosphate and
CC       most phosphatidylinositol monophosphates and diphosphates.
CC       Phosphate can be hydrolyzed from the D3 and D5 positions in the
CC       inositol ring. Has low tyrosine-protein phosphatase activity;
CC       however, the relevance of such activity in vivo is unclear. Plays
CC       an important role in adipogenesis of mesenchymal stem cells
CC       (MSCs). Regulates the phosphorylation state of AKT1 by suppressing
CC       the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs
CC       and preadipocyte cells. {ECO:0000269|PubMed:19351528}.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12837292};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:12837292}.
CC   -!- TISSUE SPECIFICITY: In developing kidney, it localizes to the
CC       basal membrane of podocytes, beginning when podocyte progenitors
CC       can first be identified in the embryonic kidney (at protein
CC       level). Expressed in lung and kidney.
CC       {ECO:0000269|PubMed:12837292, ECO:0000269|PubMed:20346435}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at highest levels in fetal kidney,
CC       followed by fetal lung and fetal cochlea.
CC       {ECO:0000269|PubMed:20346435}.
CC   -!- INDUCTION: Down-regulated during adipogenesis of mesenchymal stem
CC       cells. {ECO:0000269|PubMed:19351528}.
CC   -!- DISEASE: Deafness, autosomal recessive, 84A (DFNB84A)
CC       [MIM:613391]: A form of non-syndromic deafness characterized by
CC       progressive, sensorineural hearing loss and vestibular
CC       dysfunction. {ECO:0000269|PubMed:20346435,
CC       ECO:0000269|PubMed:20472657}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 18 fibronectin type-III domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00160}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC083812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC074031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF169351; AAD50277.1; -; mRNA.
DR   UniGene; Hs.539284; -.
DR   PDB; 4IKC; X-ray; 1.56 A; A=2015-2293.
DR   PDBsum; 4IKC; -.
DR   ProteinModelPortal; Q9UMZ3; -.
DR   SMR; Q9UMZ3; 2015-2293.
DR   DEPOD; Q9UMZ3; -.
DR   PhosphoSite; Q9UMZ3; -.
DR   DMDM; 158563998; -.
DR   PRIDE; Q9UMZ3; -.
DR   Ensembl; ENST00000266688; ENSP00000266688; ENSG00000139304.
DR   UCSC; uc001sze.2; human.
DR   GeneCards; PTPRQ; -.
DR   H-InvDB; HIX0201920; -.
DR   HGNC; HGNC:9679; PTPRQ.
DR   HPA; HPA053245; -.
DR   MIM; 603317; gene.
DR   MIM; 613391; phenotype.
DR   neXtProt; NX_Q9UMZ3; -.
DR   Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR   HOGENOM; HOG000115793; -.
DR   HOVERGEN; HBG108308; -.
DR   InParanoid; Q9UMZ3; -.
DR   PhylomeDB; Q9UMZ3; -.
DR   TreeFam; TF351926; -.
DR   BRENDA; 3.1.3.48; 2681.
DR   ChiTaRS; PTPRQ; human.
DR   PRO; PR:Q9UMZ3; -.
DR   Proteomes; UP000005640; Unplaced.
DR   Bgee; Q9UMZ3; -.
DR   CleanEx; HS_PTPRQ; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045598; P:regulation of fat cell differentiation; IDA:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 19.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTPase_domain.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; TYR_PHOSPHATASE_dom.
DR   Pfam; PF00041; fn3; 13.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 17.
DR   SMART; SM00194; PTPc; 1.
DR   SUPFAM; SSF49265; SSF49265; 11.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50853; FN3; 17.
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; Complete proteome; Deafness; Disease mutation;
KW   Glycoprotein; Hydrolase; Membrane; Non-syndromic deafness;
KW   Polymorphism; Protein phosphatase; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     35       {ECO:0000255}.
FT   CHAIN        36   2332       Phosphatidylinositol phosphatase PTPRQ.
FT                                /FTId=PRO_0000302850.
FT   TOPO_DOM     36   1947       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1948   1968       Helical. {ECO:0000255}.
FT   TOPO_DOM   1969   2332       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       36     99       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      100    195       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      199    294       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      350    438       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      441    539       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      514    606       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      610    705       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      710    799       Fibronectin type-III 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      804    894       Fibronectin type-III 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      899    988       Fibronectin type-III 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      993   1093       Fibronectin type-III 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1098   1190       Fibronectin type-III 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1192   1282       Fibronectin type-III 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1287   1380       Fibronectin type-III 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1384   1470       Fibronectin type-III 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1474   1578       Fibronectin type-III 16.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1583   1681       Fibronectin type-III 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1686   1787       Fibronectin type-III 18.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2036   2292       Tyrosine-protein phosphatase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   ACT_SITE   2233   2233       Phosphocysteine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160,
FT                                ECO:0000255|PROSITE-ProRule:PRU10044}.
FT   CARBOHYD     18     18       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     94     94       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    202    202       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    394    394       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    944    944       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1038   1038       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1080   1080       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1101   1101       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1290   1290       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1295   1295       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1844   1844       N-linked (GlcNAc...). {ECO:0000255}.
FT   VARIANT     281    281       R -> G (in DFNB84A).
FT                                {ECO:0000269|PubMed:20346435}.
FT                                /FTId=VAR_063526.
FT   VARIANT     471    471       Q -> E (in dbSNP:rs61729287).
FT                                {ECO:0000269|PubMed:20472657}.
FT                                /FTId=VAR_069041.
FT   VARIANT    1040   1040       T -> I (in dbSNP:rs12316867).
FT                                /FTId=VAR_034970.
FT   VARIANT    1098   1098       F -> L (in dbSNP:rs6539524).
FT                                /FTId=VAR_034971.
FT   VARIANT    1120   1120       A -> P (in dbSNP:rs7975340).
FT                                /FTId=VAR_034972.
FT   VARIANT    1244   1244       N -> D (in dbSNP:rs17713202).
FT                                /FTId=VAR_034973.
FT   VARIANT    1734   1734       I -> T (in dbSNP:rs7963963).
FT                                /FTId=VAR_034974.
FT   VARIANT    2121   2121       R -> K (in dbSNP:rs1163042).
FT                                /FTId=VAR_034975.
FT   TURN       2018   2020       {ECO:0000244|PDB:4IKC}.
FT   HELIX      2021   2042       {ECO:0000244|PDB:4IKC}.
FT   HELIX      2053   2056       {ECO:0000244|PDB:4IKC}.
FT   HELIX      2058   2063       {ECO:0000244|PDB:4IKC}.
FT   TURN       2073   2075       {ECO:0000244|PDB:4IKC}.
FT   TURN       2086   2089       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2092   2096       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2099   2101       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2105   2109       {ECO:0000244|PDB:4IKC}.
FT   HELIX      2113   2115       {ECO:0000244|PDB:4IKC}.
FT   HELIX      2116   2126       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2130   2133       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2156   2159       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2162   2171       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2173   2184       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2187   2196       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2201   2204       {ECO:0000244|PDB:4IKC}.
FT   HELIX      2209   2221       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2224   2226       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2229   2238       {ECO:0000244|PDB:4IKC}.
FT   HELIX      2239   2255       {ECO:0000244|PDB:4IKC}.
FT   STRAND     2257   2259       {ECO:0000244|PDB:4IKC}.
FT   HELIX      2261   2271       {ECO:0000244|PDB:4IKC}.
FT   HELIX      2279   2292       {ECO:0000244|PDB:4IKC}.
SQ   SEQUENCE   2332 AA;  260924 MW;  999D87AA00BA04C2 CRC64;
     MKKVPIKPEQ PEKLRAFNIS THSFSLHWSL PSGHVERYQV DLVPDSGFVT IRDLGGGEYQ
     VDVSNVVPGT RYDITISSIS TTYTSPVTRI VTTNVTKPGP PVFLAGERVG SAGILLSWNT
     PPNPNGRIIS YIVKYKEVCP WMQTVYTQVR SKPDSLEVLL TNLNPGTTYE IKVAAENSAG
     IGVFSDPFLF QTAESAPGKV VNLTVEAYNA SAVKLIWYLP RQPNGKITSF KISVKHARSG
     IVVKDVSIRV EDILTGKLPE CNENSESFLW STASPSPTLG RVTPPSRTTH SSSTLTQNEI
     SSVWKEPISF VVTHLRPYTT YLFEVSAVTT EAGYIDSTIV RTPESVPEGP PQNCVTGNIT
     GKSFSILWDP PTIVTGKFSY RVELYGPSGR ILDNSTKDLK FAFTNLTPFT MYDVYIAAET
     SAGTGPKSNI SVFTPPDVPG AVFDLQLAEV ESTQVRITWK KPRQPNGIIN QYRVKVLVPE
     TGIILENTLL TGNNEYINDP MAPEIVNIVE PMVGLYEGSA EMSSDLHSLA TFIYNSHPDK
     NFPARNRAED QTSPVVTTRN QYITDIAAEQ LSYVIRRLVP FTEHMISVSA FTIMGEGPPT
     VLSVRTRQQV PSSIKIINYK NISSSSILLY WDPPEYPNGK ITHYTIYAME LDTNRAFQIT
     TIDNSFLITG LKKYTKYKMR VAASTHVGES SLSEENDIFV RTSEDEPESS PQDVEVIDVT
     ADEIRLKWSP PEKPNGIIIA YEVLYKNIDT LYMKNTSTTD IILRNLRPHT LYNISVRSYT
     RFGHGNQVSS LLSVRTSETV PDSAPENITY KNISSGEIEL SFLPPSSPNG IIKKYTIYLK
     RSNGNEERTI NTTSLTQNIK VLKKYTQYII EVSASTLKGE GVRSAPISIL TEEDAPDSPP
     QDFSVKQLSG VTVKLSWQPP LEPNGIILYY TVYVWNRSSL KTINVTETSL ELSDLDYNVE
     YSAYVTASTR FGDGKTRSNI ISFQTPEGAP SDPPKDVYYA NLSSSSIILF WTPPSKPNGI
     IQYYSVYYRN TSGTFMQNFT LHEVTNDFDN MTVSTIIDKL TIFSYYTFWL TASTSVGNGN
     KSSDIIEVYT DQDIPEGFVG NLTYESISST AINVSWVPPA QPNGLVFYYV SLILQQTPRH
     VRPPLVTYER SIYFDNLEKY TDYILKITPS TEKGFSDTYT AQLYIKTEED VPETSPIINT
     FKNLSSTSVL LSWDPPVKPN GAIISYDLTL QGPNENYSFI TSDNYIILEE LSPFTLYSFF
     AAARTRKGLG PSSILFFYTD ESVPLAPPQN LTLINCTSDF VWLKWSPSPL PGGIVKVYSF
     KIHEHETDTI YYKNISGFKT EAKLVGLEPV STYSIRVSAF TKVGNGNQFS NVVKFTTQES
     VPDVVQNMQC MATSWQSVLV KWDPPKKANG IITQYMVTVE RNSTKVSPQD HMYTFIKLLA
     NTSYVFKVRA STSAGEGDES TCHVSTLPET VPSVPTNIAF SDVQSTSATL TWIRPDTILG
     YFQNYKITTQ LRAQKCKEWE SEECVEYQKI QYLYEAHLTE ETVYGLKKFR WYRFQVAAST
     NAGYGNASNW ISTKTLPGPP DGPPENVHVV ATSPFSISIS WSEPAVITGP TCYLIDVKSV
     DNDEFNISFI KSNEENKTIE IKDLEIFTRY SVVITAFTGN ISAAYVEGKS SAEMIVTTLE
     SAPKDPPNNM TFQKIPDEVT KFQLTFLPPS QPNGNIQVYQ ALVYREDDPT AVQIHNLSII
     QKTNTFVIAM LEGLKGGHTY NISVYAVNSA GAGPKVPMRI TMDIKAPARP KTKPTPIYDA
     TGKLLVTSTT ITIRMPICYY SDDHGPIKNV QVLVTETGAQ HDGNVTKWYD AYFNKARPYF
     TNEGFPNPPC TEGKTKFSGN EEIYIIGADN ACMIPGNEDK ICNGPLKPKK QYLFKFRATN
     IMGQFTDSDY SDPVKTLGEG LSERTVEIIL SVTLCILSII LLGTAIFAFA RIRQKQKEGG
     TYSPQDAEII DTKLKLDQLI TVADLELKDE RLTRPISKKS FLQHVEELCT NNNLKFQEEF
     SELPKFLQDL SSTDADLPWN RAKNRFPNIK PYNNNRVKLI ADASVPGSDY INASYISGYL
     CPNEFIATQG PLPGTVGDFW RMVWETRAKT LVMLTQCFEK GRIRCHQYWP EDNKPVTVFG
     DIVITKLMED VQIDWTIRDL KIERHGDCMT VRQCNFTAWP EHGVPENSAP LIHFVKLVRA
     SRAHDTTPMI VHCSAGVGRT GVFIALDHLT QHINDHDFVD IYGLVAELRS ERMCMVQNLA
     QYIFLHQCIL DLLSNKGSNQ PICFVNYSAL QKMDSLDAME GDVELEWEET TM
//