ROS1_CHICK
ID ROS1_CHICK Reviewed; 2311 AA.
AC P08941;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Proto-oncogene tyrosine-protein kinase ROS;
DE EC=2.7.10.1;
DE AltName: Full=Proto-oncogene c-Ros;
DE AltName: Full=Proto-oncogene c-Ros-1;
DE AltName: Full=Receptor tyrosine kinase c-ros oncogene 1;
DE AltName: Full=c-Ros receptor tyrosine kinase;
DE Flags: Precursor;
GN Name=ROS1;
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], AND TISSUE SPECIFICITY.
RX PubMed=1900358;
RA Chen J.M., Heller D., Poon B., Kang L., Wang L.-H.;
RT "The proto-oncogene c-ros codes for a transmembrane tyrosine protein kinase
RT sharing sequence and structural homology with sevenless protein of
RT Drosophila melanogaster.";
RL Oncogene 6:257-264(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1805-1867.
RX PubMed=3023956; DOI=10.1128/mcb.6.8.3000-3004.1986;
RA Matsushime H., Wang L.-H., Shibuya M.;
RT "Human c-ros-1 gene homologous to the v-ros sequence of UR2 sarcoma virus
RT encodes for a transmembrane receptorlike molecule.";
RL Mol. Cell. Biol. 6:3000-3004(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1868-2292.
RX PubMed=3023892; DOI=10.1128/mcb.6.5.1478-1486.1986;
RA Neckameyer W.S., Shibuya M., Hsu M.-T., Wang L.-H.;
RT "Proto-oncogene c-ros codes for a molecule with structural features common
RT to those of growth factor receptors and displays tissue specific and
RT developmentally regulated expression.";
RL Mol. Cell. Biol. 6:1478-1486(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2010-2311.
RC TISSUE=Kidney;
RX PubMed=3325887;
RA Podell S.B., Sefton B.M.;
RT "Chicken proto-oncogene c-ros cDNA clones: identification of a c-ros RNA
RT transcript and deduction of the amino acid sequence of the carboxyl
RT terminus of the c-ros product.";
RL Oncogene 2:9-14(1987).
RN [5]
RP FUNCTION IN CELL PROLIFERATION, AND SUBCELLULAR LOCATION.
RX PubMed=8657124; DOI=10.1128/mcb.16.4.1509;
RA Xiong Q., Chan J.L., Zong C.S., Wang L.H.;
RT "Two chimeric receptors of epidermal growth factor receptor and c-Ros that
RT differ in their transmembrane domains have opposite effects on cell
RT growth.";
RL Mol. Cell. Biol. 16:1509-1518(1996).
RN [6]
RP FUNCTION IN STAT3 ACTIVATION.
RX PubMed=9774423; DOI=10.1074/jbc.273.43.28065;
RA Zong C.S., Zeng L., Jiang Y., Sadowski H.B., Wang L.H.;
RT "Stat3 plays an important role in oncogenic Ros- and insulin-like growth
RT factor I receptor-induced anchorage-independent growth.";
RL J. Biol. Chem. 273:28065-28072(1998).
RN [7]
RP FUNCTION IN VAV3 ACTIVATION, AND INTERACTION WITH VAV3.
RX PubMed=11094073; DOI=10.1128/mcb.20.24.9212-9224.2000;
RA Zeng L., Sachdev P., Yan L., Chan J.L., Trenkle T., McClelland M.,
RA Welsh J., Wang L.H.;
RT "Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase
RT activity, modulates cell morphology, and induces cell transformation.";
RL Mol. Cell. Biol. 20:9212-9224(2000).
RN [8]
RP FUNCTION IN PI3 KINASE AND STAT3 ACTIVATION.
RX PubMed=11799110; DOI=10.1074/jbc.m108166200;
RA Nguyen K.T., Zong C.S., Uttamsingh S., Sachdev P., Bhanot M., Le M.T.,
RA Chan J.L., Wang L.H.;
RT "The role of phosphatidylinositol 3-kinase, rho family GTPases, and STAT3
RT in Ros-induced cell transformation.";
RL J. Biol. Chem. 277:11107-11115(2002).
CC -!- FUNCTION: Orphan receptor tyrosine kinase (RTK) that may activate
CC several downstream signaling pathways related to cell differentiation,
CC proliferation, growth and survival including the PI3 kinase-mTOR
CC signaling pathway. Mediates the phosphorylation of PTPN11, an activator
CC of this pathway. May also phosphorylate and activate the transcription
CC factor STAT3 to control anchorage-independent cell growth. Mediates the
CC phosphorylation and the activation of VAV3, a guanine nucleotide
CC exchange factor regulating cell morphology. May activate other
CC downstream signaling proteins including AKT1, MAPK1, MAPK3, IRS1, and
CC PLCG2. {ECO:0000269|PubMed:11094073, ECO:0000269|PubMed:11799110,
CC ECO:0000269|PubMed:8657124, ECO:0000269|PubMed:9774423}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Interacts with VAV3; constitutive interaction mediating VAV3
CC phosphorylation. {ECO:0000269|PubMed:11094073}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8657124};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:8657124}.
CC -!- TISSUE SPECIFICITY: Highest expression in kidney. Also expressed in
CC gonad, thymus, bursa, brain and kidney. {ECO:0000269|PubMed:1900358}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; M13013; AAA49058.1; -; Genomic_DNA.
DR EMBL; X06770; CAA29938.1; -; mRNA.
DR PIR; A60197; TVCHSR.
DR AlphaFoldDB; P08941; -.
DR SMR; P08941; -.
DR STRING; 9031.ENSGALP00000036566; -.
DR iPTMnet; P08941; -.
DR PaxDb; P08941; -.
DR PRIDE; P08941; -.
DR VEuPathDB; HostDB:geneid_396192; -.
DR eggNOG; KOG1095; Eukaryota.
DR InParanoid; P08941; -.
DR PhylomeDB; P08941; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR GO; GO:0002066; P:columnar/cuboidal epithelial cell development; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0032006; P:regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 7.
DR Gene3D; 2.120.10.30; -; 3.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 9.
DR SMART; SM00135; LY; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 9.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..2311
FT /note="Proto-oncogene tyrosine-protein kinase ROS"
FT /id="PRO_0000016723"
FT TOPO_DOM 25..1873
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1874..1898
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1899..2311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 110..202
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 203..294
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 571..671
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 952..1047
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1051..1158
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1459..1569
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1570..1669
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1671..1766
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1767..1868
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1961..2240
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1754..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2095
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 1967..1975
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1996
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2131
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 962
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 971
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1827
FT /note="N -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 2140..2141
FT /note="IN -> LP (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 2255..2292
FT /note="FINQAFEDIDVPPADSDSILSTTLMEARDQEGLNYLVV -> SSTKLLRVSL
FT GSAVPTAFAQTCNSVNVESQNGLGWKGP (in Ref. 3; AAA49058)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2311 AA; 260961 MW; CF9680E5B0491417 CRC64;
MRNACLLLNR LGAFYFIWIS AAYCSFSKNC QDLCTSNLEG ELGIANLCNV SDINVACTQG
CQFWNATEQV NCPLKCNKTY TRECETVSCK FGCSRAEDAY GVEAQNCLNK PGAPFASSIG
SHNITLGWKP ANISEVKYII QWKFHQLPGD WRYTEVVSET SYTVKDLQAF TEYEFRVVWI
ITSQLQLHSP PSPSYRTHAS GVPTTAPIIK DIQSSSPNTV EVSWFPPLFP NGLIVGYNLV
LTSENHELLR ASRGHSFQFY STFPNSTYRF SIVAVNEAGA GPPAEANITT PESKVKEKAK
WLFLSRNQSL RKRYMEHFLE AAHCLQNGII HHNITGISVN VYQQVVYFSE GNSIWVKGVV
DMSDVSDLTL FYTGWGNITS ISVDWLYQRM YFVMNEKIHV CQLENCTAAE DITPPYETSP
RKIVADPYNG YIFCLLEDGI YRANLPLFPD TASAASLVVK SHTLRDFMIN FQSKRLIFFN
KTEQAFVSGF LDGSEFHTLR AHVPLDDMES FVYEDNIFTV TDGRAVFHEE ISQVGSSSFN
EYVVDCSLEY PEYFGFGNLL FYAASTQPYP LPTLPRLVTV LFGSDQAVIS WSPPEYTIGT
SRSAWQNWTY DVKVSSQSTF EEEWVVSNIT DTRFAVKNLV SFTEYEMSVR AVSPAGEGPW
SEPFRGMTFE EAEEEPYILA VGAEGLWKQR LDSYGPGEFL YPHIRNISDL DWYNDTLYWS
NSMGKVQTWS MNKKEGTTEN SYVPDIKNAR MLAFDWLGQC LYWAGKANTI YRKSLLGDHM
DVVAHVVYVV KDLAVDSVNG YLYWATTYTV ESARLNGEEY LILQEHLQFS GKQVVGLALD
LTSGFLYWLV QDGLCLNLYR ISICKESCGN IMVTEISAWS VSEVSQNALQ YYSGRLFWIN
RLKFITTQEL NQSISIPFSE PAEFAAFTLV HTSLKPLPGN FSFTPKVIPS SVPESSFKIK
GNSSSFHIIW NASTDVQWGT VFYCVGSNAL QMRTLESERC LHPHDLTVPS YKVDWLEPFT
LFDFSVTPYT YWGKAPTTSV YLRAPEGVPS APANPRIYVL HSNTHEGEEK VLVELRWDKP
ERDNGVLTQF RVYYQLLYES GAADTLMEWN VSDVKPTALL FSIRDEHPRL TVRFQVQAFT
SVGPGPMSDV AQRNSSDIFP VPTLITFSSN KLFLTDIDSN HTIWEVLTNR NIKDICYTAD
DDKVYYILED SLFLLNVQST SESQLFEDVF LRNVTAITVD WIARHLFVAM KTSWNETQVF
FIDLELKTKS LKALNIQLGK RNSTISSLLS YPFLSRLYWI EELDYGSRMF YYDILNNTMY
HILGYESVEE KMRNYCNCNV AEAELGRPIS IDVTDIKKPQ LLFIRGRDEI WASDVDACHC
WRITKIPSFQ GTKIGSLTVD KQFIYWTIEK KEYTEICLAD KESTRHSLQR KANHELKILA
YSSAMQSYPD KKCLTPLLDT EKPTILDTTN TSFTLSLPSV TTQQLCPSIS QPTPTYLVFF
REITSNHENS TYHFSTLLQK TLEIQEPIAV INNLKPFSTY AIQVAVKNYY SNQNQLAVGR
EAISTTLYGV PEGVDSIKTV VLSDTTINIS WSEPLEPNGP LESIRYQISV NLLSLFPEAP
LRKSEFPNGT LSWSVSDLQS GTNNLFKVLA FHPNENWFSE SVPVIAKTFE TPLSPSNIIP
RNTSFQLEWR APLHINGTSF WFELSKWQTR SDWFSPASTT CTVGPVYTCN LTGTLPSANY
LVRATVVYVT GMKSTSSPTS FKTTAGVPSK PGTPKRAEDS KNSVQWEKAE DNGSNLTYYI
LESRKQSGNT NKVKSLWVVV YNGSCDNICT WKAENLEGTF QFRAAAANML GLGEYSDTSK
DIVLAKDTVT SPDITAIVAV IGAVVLGLTI IILFGFVWHQ RWKSRKPAST GQIVLVKEDK
ELAQLRGMAE TVGLANACYA VSTLPSQAEI ESLPAFPRDK LNLHKLLGSG AFGEVYEGTA
LDILADGSGE SRVAVKTLKR GATDQEKSEF LKEAHLMSKF DHPHILKLLG VCLLNEPQYL
ILELMEGGDL LSYLRGARKQ KFQSPLLTLT DLLDICLDIC KGCVYLEKMR FIHRDLAARN
CLVSEKQYGS CSRVVKIGDF GLARDIYKND YYRKRGEGLI NVRWMAPESL IDGVFTNHSD
VWAFGVLVWE TLTLGQQPYP GLSNIEVLHH VRSGGRLESP NNCPDDIRDL MTRCWAQDPH
NRPTFFYIQH KLQEIRHSPL CFSYFLGDKE SVAGFINQAF EDIDVPPADS DSILSTTLME
ARDQEGLNYL VVVKESNQDQ GSISSAELTS V
