ROS1_MOUSE
ID ROS1_MOUSE Reviewed; 2340 AA.
AC Q78DX7; Q60705;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 152.
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; Synonyms=Ros, Ros-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NMRI; TISSUE=Intestine;
RX PubMed=7970722;
RA Riethmacher D., Langholz O., Godecke S., Sachs M., Birchmeier C.;
RT "Biochemical and functional characterization of the murine ros
RT protooncogene.";
RL Oncogene 9:3617-3626(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Kidney;
RX PubMed=8544427; DOI=10.1038/ki.1995.460;
RA Kanwar Y.S., Liu Z.Z., Kumar A., Wada J., Carone F.A.;
RT "Cloning of mouse c-ros renal cDNA, its role in development and
RT relationship to extracellular matrix glycoproteins.";
RL Kidney Int. 48:1646-1659(1995).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION IN EPITHELIUM DIFFERENTIATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8675006; DOI=10.1101/gad.10.10.1184;
RA Sonnenberg-Riethmacher E., Walter B., Riethmacher D., Goedecke S.,
RA Birchmeier C.;
RT "The c-ros tyrosine kinase receptor controls regionalization and
RT differentiation of epithelial cells in the epididymis.";
RL Genes Dev. 10:1184-1193(1996).
RN [4]
RP FUNCTION IN CELL PROLIFERATION.
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 [5]
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 [6]
RP FUNCTION IN CELL PROLIFERATION, INTERACTION WITH PTPN6, ACTIVITY
RP REGULATION, PHOSPHORYLATION AT TYR-2267, AND MUTAGENESIS OF TYR-2267.
RX PubMed=11266449; DOI=10.1083/jcb.152.2.325;
RA Keilhack H., Mueller M., Boehmer S.A., Frank C., Weidner K.M.,
RA Birchmeier W., Ligensa T., Berndt A., Kosmehl H., Guenther B., Mueller T.,
RA Birchmeier C., Boehmer F.D.;
RT "Negative regulation of Ros receptor tyrosine kinase signaling. An
RT epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1.";
RL J. Cell Biol. 152:325-334(2001).
RN [7]
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 plays a role in
CC epithelial cell differentiation and regionalization of the proximal
CC epididymal epithelium. May activate several downstream signaling
CC pathways related to cell differentiation, proliferation, growth and
CC survival including the PI3 kinase-mTOR signaling pathway. Mediates the
CC phosphorylation of PTPN11, an activator of this pathway. May also
CC phosphorylate and activate the transcription factor STAT3 to control
CC anchorage-independent cell growth. Mediates the phosphorylation and the
CC activation of VAV3, a guanine nucleotide exchange factor regulating
CC cell morphology. May activate other downstream signaling proteins
CC including AKT1, MAPK1, MAPK3, IRS1, and PLCG2.
CC {ECO:0000269|PubMed:11266449, ECO:0000269|PubMed:11799110,
CC ECO:0000269|PubMed:8657124, ECO:0000269|PubMed:8675006,
CC 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 -!- ACTIVITY REGULATION: Inhibited by dephosphorylation by PTPN6.
CC {ECO:0000269|PubMed:11266449}.
CC -!- SUBUNIT: Interacts with PTPN11; may activate the PI3 kinase-mTOR
CC signaling pathway. Interacts with VAV3; constitutive interaction
CC mediating VAV3 phosphorylation (By similarity). Interacts with PTPN6
CC (via SH2 1 domain); the interaction is direct and promotes ROS1
CC dephosphorylation. {ECO:0000250, ECO:0000269|PubMed:11266449}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by epithelial cells of the caput
CC epididymis (at protein level). {ECO:0000269|PubMed:8675006}.
CC -!- PTM: Phosphorylated. Probably autophosphorylates. Phosphorylation at
CC Tyr-2267 and/or Tyr-2327 recruits PTPN11 (By similarity).
CC Phosphorylation at Tyr-2267 is required for the interaction with PTPN6
CC that mediates ROS1 dephosphorylation. Phosphorylation at Tyr-2267
CC stimulates the kinase activity and the activation of the ERK1 signaling
CC cascade. {ECO:0000250, ECO:0000269|PubMed:11266449}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and healthy. Females display
CC normal fertility while males are sterile due a non-cell autonomous
CC defect in sperm maturation. It is associated with the absence of tall
CC columnar epithelial cells with long microvilli in the proximal part of
CC the caput epididymidis. {ECO:0000269|PubMed:8675006}.
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; X81650; CAA57310.1; -; mRNA.
DR EMBL; U15443; AAA50600.1; -; mRNA.
DR CCDS; CCDS23838.1; -.
DR RefSeq; NP_035412.2; NM_011282.2.
DR AlphaFoldDB; Q78DX7; -.
DR SMR; Q78DX7; -.
DR IntAct; Q78DX7; 2.
DR MINT; Q78DX7; -.
DR STRING; 10090.ENSMUSP00000020045; -.
DR BindingDB; Q78DX7; -.
DR ChEMBL; CHEMBL2034802; -.
DR GlyGen; Q78DX7; 7 sites.
DR iPTMnet; Q78DX7; -.
DR PhosphoSitePlus; Q78DX7; -.
DR PaxDb; Q78DX7; -.
DR PRIDE; Q78DX7; -.
DR ProteomicsDB; 300468; -.
DR Antibodypedia; 32541; 683 antibodies from 36 providers.
DR DNASU; 19886; -.
DR Ensembl; ENSMUST00000020045; ENSMUSP00000020045; ENSMUSG00000019893.
DR GeneID; 19886; -.
DR KEGG; mmu:19886; -.
DR UCSC; uc007fbb.1; mouse.
DR CTD; 6098; -.
DR MGI; MGI:97999; Ros1.
DR VEuPathDB; HostDB:ENSMUSG00000019893; -.
DR eggNOG; KOG1095; Eukaryota.
DR GeneTree; ENSGT00940000160831; -.
DR HOGENOM; CLU_000798_0_0_1; -.
DR InParanoid; Q78DX7; -.
DR OMA; SCKFGCS; -.
DR OrthoDB; 203310at2759; -.
DR PhylomeDB; Q78DX7; -.
DR TreeFam; TF351636; -.
DR BioGRID-ORCS; 19886; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Ros1; mouse.
DR PRO; PR:Q78DX7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q78DX7; protein.
DR Bgee; ENSMUSG00000019893; Expressed in semen and 32 other tissues.
DR ExpressionAtlas; Q78DX7; baseline and differential.
DR Genevisible; Q78DX7; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
DR GO; GO:0002066; P:columnar/cuboidal epithelial cell development; IMP:UniProtKB.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0010966; P:regulation of phosphate transport; IMP:MGI.
DR GO; GO:0032006; P:regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00063; FN3; 8.
DR Gene3D; 2.120.10.30; -; 3.
DR Gene3D; 2.60.40.10; -; 8.
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 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.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..2340
FT /note="Proto-oncogene tyrosine-protein kinase ROS"
FT /id="PRO_0000278115"
FT TOPO_DOM 29..1854
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1855..1875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1876..2340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 111..206
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 207..295
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 567..667
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 943..1038
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1039..1146
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1442..1549
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1550..1649
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1651..1744
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1745..1846
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1938..2216
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 2072
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 1944..1952
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1973
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2267
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11266449"
FT MOD_RES 2327
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P08922"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 935
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 2267
FT /note="Y->F: Abrogates interaction with PTPN6."
FT /evidence="ECO:0000269|PubMed:11266449"
FT CONFLICT 27
FT /note="Q -> L (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..111
FT /note="TEL -> QAI (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="D -> Y (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="I -> V (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="A -> P (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="G -> P (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 631..632
FT /note="NV -> KL (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 642..645
FT /note="TVSV -> PFSC (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="W -> G (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 671..672
FT /note="PP -> LL (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="I -> V (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1050
FT /note="S -> R (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1066
FT /note="N -> D (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1085
FT /note="S -> F (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1235
FT /note="Y -> C (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276
FT /note="I -> T (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1371
FT /note="V -> L (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1428..1429
FT /note="SA -> FR (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1486..1487
FT /note="ME -> IK (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1541..1545
FT /note="EIQGQ -> RFKDK (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1585..1592
FT /note="RYQLVMSY -> AISWLMSD (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1669
FT /note="W -> R (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1778
FT /note="T -> S (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1893
FT /note="N -> S (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1917..1918
FT /note="AV -> GI (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 2087
FT /note="S -> N (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 2118
FT /note="V -> A (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 2270..2272
FT /note="LAT -> VPQ (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
FT CONFLICT 2333
FT /note="S -> R (in Ref. 2; AAA50600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2340 AA; 261967 MW; A3A670B0C4151D7C CRC64;
MKNICWLTLK LVKFVVLGCI IWISVAQSTV LSSCLTSCVT NLGRQLDSGT RYNLSEACIH
GCQFWNSVDQ ETCALKCNDT YATICERESC EVGCSNAEGS YEEEVLESTE LPTAPFASSI
GSHGVTLRWN PANISGVKYI IQWKYAQLPG SWTFTETVSK LSYTVEPLHP FTEYIFRVVW
IFTAQLHLYS PPSPSYRTHP YGVPETAPLI LNMESWSPDT VEVSWAPPHF PGGPILGYNL
RLISKNQKLD SGTQRTSFQF YSTLPNTTYR FSIAAVNEVG EGPEAESTVT TPSPSVQEEE
QWLFLSRKTS LRKRSLKYLV DEAHCLWSDA IHHNITGISV YAQQQVVYFS EGTVIWMKGA
ANMSDVSDLR IFYQGSGLVS SISIDWLYQR MYFIMDKLVY VCELKNCSNL EEITPFSLIA
PQKVVVDSYN GYLFYLLRDG IYRVNLPLPS GRDTKAVRIV ESGTLKDFAV KPQSKRIIYF
NDTMQLFMST FLDGSAFHRV LPWVPLVTVK SFACENNDFL ITDGKAIFQQ DSLSFNEFIV
GCDLSHIEEF GFGNLVIFGS SVQSYPLPGH PQEVSVLFGS REALIQWTPP ALAIGASPSA
WQNWTYEVKV YSQDILEITQ VFSNISGTML NVPELQSSTK YTVSVRASSP KGPGPWSAPS
VGTTLVPATE PPFIMAVKED GLWSKPLCSF GPGEFLSSDV GNVSDMDWYN NSLYYSDTKG
NVYVRPLNGM DISENYHIPS IVGAGALAFE WLGHFLYWAG KTYVIQRQSV LTGHTDIVTH
VKLLVNDMAV DSVGGYLYWT TLYSVESTRL NGESSLVLQA QPWLSGKKVI ALTLDLSDGL
LYWLVQDNQC IHLYTAVLRG WSGGDATITE FAAWSTSEIS QNALMYYSGR LFWINGFRII
TAQEIGQRTS VSVSEPAKFN QFTIIQTSLK PLPGNFSSTP KVIPDPVQES SFRIEGHTSS
FQILWNEPPA VDWGIVFYSV EFSTHSKFLI IEQQSLPIFT VEGLEPYTLF NLSVTPYTYW
GKGQKTSLSF RAPESVPSAP ENPRIFILSS GRYTKKNEVV VEFRWNKPKH ENGVLTKFEI
FYHISKQSGT NRSTEDWMSA SVIPPVMSFQ LEAVSPEYTV AFQVRVFTSK GPGPFSDIVM
SKTSEIKPCP YLISLLGNKI VFLDMDQNQV LWTFSLEGDV STVGYTTDDE MGYFAQGDTL
FLLNLRNHSS SKLFQDALVS DIRVIAVDWI ARHLYFALKA SQNGTQIFNV DLEHKVKSPR
EVKTCKAHTT IISFSIYPLL SRLYWTEVSD LGHQMFYCNI SNHTSQHVLQ PKASNQHGRS
QCSCNVTESE LSGAMTVDTS DPDRPWIYFT KRQEIWAMDL EGCQCWKVIM VPTIPGKRII
SLTVDGEFIY WIMKTKDDAQ IYQAKKGSGA ILSQVKASRS KHILAYSSAL QPFPDKAYLS
LASDMVEATI LYATNTSLTL KLPPVKTNLT WHGITHPTST YLIYYMEANR ANSSDRRHKM
LESQENVARI EGLQPFSMYM IQIAVKNYYS EPLEHLPLGK EIQGQTKSGV PGAVCHINAT
VLSDTSLHVF WTESHKPNGP KESVRYQLVM SYLAPIPETP LRQGEFPSAK LSLLITKLSG
GQLYVMKVLA CHPEEMWCTE SHPVSVNMFD TPEKPSALVP ENTSLQLDWK ARSNVNLTGF
WFELQKWKYN EFYHVKASCS QGPVYVCNIT DLQPYTSYNI RVVVVYTTGE NSSSIPESFK
TKAGVPSKPG IPKLLEGSKN SIQWEKAEDN GSRLMYYTLE VRKGISNDSQ NQSSRWKVVF
NGSCSSICTW RSKNLKGTFQ FRAVAANEIG LGEYSEISED ITLVEDGVWI TETSFILTII
VGIFLVATVP LTFVWHRSLK SHKASKEGLS VLNDNDKELA ELRGLAAGVG LANACYAVHT
VPTQEEIENL PAFPREKLSL RLLLGSGAFG EVYEGTAIDI LGVGSGEIKV AVKTLKKGST
DQEKIEFLKE AHLMSKFNHP NILKQLGVCL LGEPQYIILE LMEGGDLLSY LRKARGTTFH
GPSLTLLDLV ELCVDISKGC VYLEQMHFIH RDLAARNCLV SVKDYTSPRV VKIGDFGLAR
EIYKNDYYRK RGEGLLPVRW MAPENLMDGI FTSQSDVWSF GILVWEILTL GHQPYPAHSN
LDVLNYVQAG GRLEPPRNCP DDLWNLMSQC WAQEPDQRPT FHNIQNQLQL FRNVFLNNVS
HCGEAAPTGG VINKGFEGED DEMVTLNSDD TMPVALMETK NQEGLNYMVL ATKCSQGEGS
YEGPLGPKEL GSCDLKKDKK QPQADKDFCQ EPQVAYGSPG LSEGLNYACL AHSEHGDVSE
