ID   TENS1_CHICK             Reviewed;        1744 AA.
AC   Q04205; A0A1L1RRE9; Q91007; Q92011;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2022, sequence version 3.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Tensin-1;
DE            EC=3.1.3.- {ECO:0000305};
GN   Name=TNS1; Synonyms=TNS;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=8071358; DOI=10.1016/s0021-9258(17)31791-x;
RA   Lo S.H., An Q., Bao S., Wong W.K., Liu Y., Janmey P.A., Hartwig J.H.,
RA   Chen L.B.;
RT   "Molecular cloning of chick cardiac muscle tensin. Full-length cDNA
RT   sequence, expression, and characterization.";
RL   J. Biol. Chem. 269:22310-22319(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=7896874; DOI=10.1083/jcb.128.6.1095;
RA   Chuang J.Z., Lin D.C., Lin S.;
RT   "Molecular cloning, expression, and mapping of the high affinity actin-
RT   capping domain of chicken cardiac tensin.";
RL   J. Cell Biol. 128:1095-1109(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen L.B.;
RL   Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|Proteomes:UP000000539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 888-1239, DOMAIN SH2, AND PHOSPHORYLATION.
RX   PubMed=1708917; DOI=10.1126/science.1708917;
RA   Davis S., Lu M.L., Lo S.H., Lin S., Butler J.A., Druker B.J., Roberts T.M.,
RA   An Q., Chen L.B.;
RT   "Presence of an SH2 domain in the actin-binding protein tensin.";
RL   Science 252:712-715(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1469-1744.
RC   TISSUE=Embryonic chondrocyte, and Embryonic heart;
RX   PubMed=8223621; DOI=10.1111/j.1432-1033.1993.tb18306.x;
RA   van de Werken R., Gennari M., Tavella S., Bet P., Molina F., Lin S.,
RA   Cancedda R., Castagnola P.;
RT   "Modulation of tensin and vimentin expression in chick embryo developing
RT   cartilage and cultured differentiating chondrocytes.";
RL   Eur. J. Biochem. 217:781-790(1993).
CC   -!- FUNCTION: May act as a protein phosphatase and/or a lipid phosphatase.
CC       Involved in fibrillar adhesion formation. Plays a role in cell
CC       polarization and migration. May be involved in cartilage development
CC       and in linking signal transduction pathways to the cytoskeleton.
CC       {ECO:0000250|UniProtKB:Q9HBL0}.
CC   -!- SUBUNIT: Binds to actin filaments. Interacts with phosphotyrosine-
CC       containing proteins (PubMed:1708917). {ECO:0000269|PubMed:1708917}.
CC   -!- INTERACTION:
CC       Q04205; P56945: BCAR1; Xeno; NbExp=2; IntAct=EBI-2607590, EBI-702093;
CC       Q04205; Q96QB1-1: DLC1; Xeno; NbExp=7; IntAct=EBI-2607590, EBI-15638708;
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:Q9HBL0}. Cell
CC       junction, focal adhesion {ECO:0000250|UniProtKB:Q9HBL0}. Cytoplasm,
CC       cytoskeleton {ECO:0000250|UniProtKB:Q9HBL0}.
CC   -!- TISSUE SPECIFICITY: Heart, gizzard, lung and skeletal muscle.
CC   -!- PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:1708917}.
CC   -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA73949.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA79215.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=M63606; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; M96625; AAA59053.1; -; mRNA.
DR   EMBL; L06662; AAA73949.1; ALT_INIT; mRNA.
DR   EMBL; Z18529; CAA79215.1; ALT_INIT; mRNA.
DR   EMBL; M74165; AAA49087.1; -; mRNA.
DR   EMBL; AADN05000350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M63606; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; X66286; CAA46992.1; -; mRNA.
DR   PIR; A54970; A54970.
DR   PIR; A57075; A57075.
DR   PIR; S27939; S27939.
DR   RefSeq; NP_990786.1; NM_205455.1.
DR   PDB; 1WVH; X-ray; 1.50 A; A=1605-1738.
DR   PDB; 2GJY; NMR; -; A=1605-1744.
DR   PDBsum; 1WVH; -.
DR   PDBsum; 2GJY; -.
DR   AlphaFoldDB; Q04205; -.
DR   BMRB; Q04205; -.
DR   SMR; Q04205; -.
DR   DIP; DIP-56927N; -.
DR   IntAct; Q04205; 4.
DR   STRING; 9031.ENSGALP00000061378; -.
DR   DNASU; 396439; -.
DR   KEGG; gga:396439; -.
DR   VEuPathDB; HostDB:geneid_396439; -.
DR   InParanoid; Q04205; -.
DR   PhylomeDB; Q04205; -.
DR   EvolutionaryTrace; Q04205; -.
DR   PRO; PR:Q04205; -.
DR   Proteomes; UP000000539; Chromosome 7.
DR   Bgee; ENSGALG00000041013; Expressed in heart and 13 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010761; P:fibroblast migration; IBA:GO_Central.
DR   CDD; cd01213; PTB_tensin; 1.
DR   CDD; cd14560; PTP_tensin-1; 1.
DR   CDD; cd09927; SH2_Tensin_like; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR035012; Tensin-like_SH2.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   InterPro; IPR033929; Tensin_PTB.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   PANTHER; PTHR45734; TENSIN; 1.
DR   PANTHER; PTHR45734:SF3; TENSIN-1; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Cell junction; Cytoplasm; Cytoskeleton;
KW   Hydrolase; Phosphoprotein; Protein phosphatase; Reference proteome;
KW   SH2 domain.
FT   CHAIN           1..1744
FT                   /note="Tensin-1"
FT                   /id="PRO_0000215901"
FT   DOMAIN          58..230
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT   DOMAIN          235..361
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT   DOMAIN          1472..1581
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          1607..1743
FT                   /note="PTB"
FT                   /evidence="ECO:0000255"
FT   REGION          15..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1156..1437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..753
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..789
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..954
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1010
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1156..1170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1199..1227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1340..1357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1364..1388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1405..1437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        49
FT                   /note="R -> C (in Ref. 1; AAA59053 and 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="M -> T (in Ref. 2; AAA73949/CAA79215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="Q -> PR (in Ref. 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        404
FT                   /note="T -> A (in Ref. 1; AAA59053 and 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        452
FT                   /note="A -> T (in Ref. 1; AAA59053 and 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        508..509
FT                   /note="EL -> DV (in Ref. 1; AAA59053 and 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        522
FT                   /note="P -> A (in Ref. 1; AAA59053 and 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        664
FT                   /note="A -> R (in Ref. 1; AAA59053 and 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        666
FT                   /note="A -> T (in Ref. 2; AAA73949/CAA79215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        681
FT                   /note="T -> A (in Ref. 1; AAA59053, 2; AAA73949/CAA79215
FT                   and 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        845
FT                   /note="P -> R (in Ref. 1; AAA59053, 2; AAA73949/CAA79215
FT                   and 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        875
FT                   /note="A -> P (in Ref. 1; AAA59053 and 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        909
FT                   /note="P -> T (in Ref. 2; AAA73949/CAA79215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1102..1113
FT                   /note="Missing (in Ref. 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1240
FT                   /note="A -> G (in Ref. 1; AAA59053 and 3; AAA49087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1480
FT                   /note="E -> D (in Ref. 2; AAA73949/CAA79215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1711
FT                   /note="D -> E (in Ref. 2; AAA73949/CAA79215)"
FT                   /evidence="ECO:0000305"
FT   STRAND          1607..1619
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   HELIX           1623..1635
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   STRAND          1644..1651
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   STRAND          1654..1662
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   STRAND          1667..1671
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   HELIX           1672..1674
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   STRAND          1675..1680
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   STRAND          1686..1688
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   STRAND          1690..1693
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   STRAND          1695..1703
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   STRAND          1706..1709
FT                   /evidence="ECO:0007829|PDB:2GJY"
FT   STRAND          1712..1719
FT                   /evidence="ECO:0007829|PDB:1WVH"
FT   HELIX           1726..1737
FT                   /evidence="ECO:0007829|PDB:1WVH"
SQ   SEQUENCE   1744 AA;  187195 MW;  74064257D8F4BB44 CRC64;
     MDFGSVMNQA ATPCSPAVNY ELPSPGQSIT KQVDTPDATR SPRGGQAHRK ASRSMSVTAA
     MESSCELDLV YITERIIAVS YPSTAEEQSF RSNLREVAHM LKSKHGDNYV LFNLSERRHD
     ISKLHPKVLD FGWPDLHTPA LEKICSICKA MDTWLNAAAH NVVVLHNKGN RGRLGVVVAA
     YMHYSNISAS ADQALDRFAM KRFYEDKVVP VGQPSQKRYI HYFSGLLSGS IKMNNKPLFL
     HHVIMHGIPN FESKGGCRPF LKIYQAMQPV YTSGIYNVQG DSQTGICITI EPGLLLKGDI
     LLKCYHKKFR SPTRDVIFRV QFHTCAVHDL DIVFGKEDLD EAFRDERFPE YGKVEFVFSY
     GPEKIQGMEH LENGPSVSVD YNTSDPLIRW DSYENFNIQR EDSTEGTWAE PALPGKHLEK
     EVGHTQGPLD GSLYAKVKKK DSLHGSIGAV NAARLPLSAA PNHVEHTLSV SSDSGNSTAS
     TKTDRTDEPG APGAPTGHAV LSPEEKRELD RLLVGFGLES APPMHNHAPG PAPARLPAGP
     GRHVVPAQVH VNGAGTPLLA ERETDILDDE LPNQDGHSVG SLGTLSSLDG TTTASEAGFH
     EAPRVGSLSS LPNGPASYNG AEKMLKEGLY EAEPLSNGAY PYSNQNTLMG HHLRDPLAHL
     RPSASAQEHL AGYPQRQPAS TSPAWLQPPV PQPYLYGYDL PSAHRSQSFP AVGTAKYEAN
     LALPQAPARS TSSREAVQRG LNSWQQQGGS RPPSQLHDGG LESHSPSLSS CSPQPSPLQP
     MPPHSHSMPE FPRAPSRREI EQSIEALDVL MLDLAPSVHK SQSVPSAATR QDKPAAMLSS
     LSAQPLSGHY AQPTPQVVQP RSFGTSVGTD PLAKAYSPGP LVPAARSTAE PDYTVHEYRE
     TYTPYSYQPV PEPRSYGSAP ASILPLSASY SPAGSQQLLV SSPPSPTAPA QSQLPHKGLE
     SYEDLSRSGE EPLNLEGLVA HRVAGVQSRE KSPEESTVPA RRRTPSDSHY EKSSPEPGSP
     RSPTVLSPEV VSTIAANPGG RPKEPHLHSY KEAFEEMESA SPSSLTSGGV RSPPGLAKTP
     LSALGLKPHN PADILLHPVG ELEGEAGADS EEEPRSYVES VARTATTGRA GNLPAAQPVG
     LEVPARNGAF GNSFTVPSPV STSSPIHSVD GASLRSYPSE GSPHGTVTPP HAVAETAYRS
     PMVSQTPSAH SSYQTSSPSS FQAGTLGSPY ASPDYPDGRA GFQPDPQARQ QPQVSVVGVH
     ALPGSPRTLH RTVATNTPPS PGFGRRAANP AVASVPGSPG LGRHTVSPHA PPGSPSLARH
     QMAAVPPGSP MYGYSSPEER RPTLSRQSSA SGYQPPSTPS FPVSPAYYPG TSTPHSSSPD
     SAAYRQGSPT PQPALPEKRR MSAGERSNSL PNYATVNGKA SSPLSSGMSS PSSGSAVAFS
     HTLPDFSKFS MPDISPETRA NVKFVQDTSK YWYKPDISRE QAIALLKDRE PGAFIIRDSH
     SFRGAYGLAM KVASPPPTVM QQNKKGDITN ELVRHFLIET SPRGVKLKGC PNEPNFGCLS
     ALVYQHSIMP LALPCKLVIP DRDPMEEKKD AASTTNSATD LLKQGAACNV LFINSVEMES
     LTGPQAISKA VAETLVADPT PTATIVHFKV SAQGITLTDN QRKLFFRRHY PLNTVTFCDL
     DPQERKWTKT DGSGPAKLFG FVARKQGSTT DNVCHLFAEL DPDQPAAAIV NFVSRVMLGS
     GQKR
//