WNT1_MOUSE
ID WNT1_MOUSE Reviewed; 370 AA.
AC P04426;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Proto-oncogene Wnt-1;
DE AltName: Full=Proto-oncogene Int-1 {ECO:0000303|PubMed:2202907, ECO:0000303|PubMed:6091914};
DE Flags: Precursor;
GN Name=Wnt1;
GN Synonyms=Int-1 {ECO:0000303|PubMed:2202907, ECO:0000303|PubMed:3018519,
GN ECO:0000303|PubMed:6091914}, Wnt-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 [GENOMIC DNA].
RC STRAIN=C3H/HeJ;
RX PubMed=6091914; DOI=10.1016/0092-8674(84)90209-5;
RA Ooyen A.V., Nusse R.;
RT "Structure and nucleotide sequence of the putative mammary oncogene int-1;
RT proviral insertions leave the protein-encoding domain intact.";
RL Cell 39:233-240(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3018519; DOI=10.1128/mcb.5.12.3337-3344.1985;
RA Fung Y.-K.T., Shackleford G.M., Brown A.M.C., Sanders G.S., Varmus H.E.;
RT "Nucleotide sequence and expression in vitro of cDNA derived from mRNA of
RT int-1, a provirally activated mouse mammary oncogene.";
RL Mol. Cell. Biol. 5:3337-3344(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2279700; DOI=10.1101/gad.4.12b.2319;
RA Gavin B.J., McMahon J.A., McMahon A.P.;
RT "Expression of multiple novel Wnt-1/int-1-related genes during fetal and
RT adult mouse development.";
RL Genes Dev. 4:2319-2332(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II;
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=2202907; DOI=10.1038/346847a0;
RA Thomas K.R., Capecchi M.R.;
RT "Targeted disruption of the murine int-1 proto-oncogene resulting in severe
RT abnormalities in midbrain and cerebellar development.";
RL Nature 346:847-850(1990).
RN [6]
RP DEVELOPMENTAL STAGE.
RC STRAIN=CBA/CaJ; TISSUE=Embryo;
RX PubMed=3594565; DOI=10.1016/0092-8674(87)90664-7;
RA Wilkinson D.G., Bailes J.A., McMahon A.P.;
RT "Expression of the proto-oncogene int-1 is restricted to specific neural
RT cells in the developing mouse embryo.";
RL Cell 50:79-88(1987).
RN [7]
RP TISSUE SPECIFICITY.
RC STRAIN=ICR;
RX PubMed=3594566; DOI=10.1016/0092-8674(87)90665-9;
RA Shackleford G.M., Varmus H.E.;
RT "Expression of the proto-oncogene int-1 is restricted to postmeiotic male
RT germ cells and the neural tube of mid-gestational embryos.";
RL Cell 50:89-95(1987).
RN [8]
RP INTERACTION WITH PORCN.
RX PubMed=10866835; DOI=10.1046/j.1432-1033.2000.01478.x;
RA Tanaka K., Okabayashi H., Asashima M., Perrimon N., Kadowaki T.;
RT "The evolutionarily conserved porcupine gene family is involved in the
RT processing of the Wnt family.";
RL Eur. J. Biochem. 267:4300-4311(2000).
RN [9]
RP FUNCTION.
RX PubMed=15454084; DOI=10.1016/j.cell.2004.09.019;
RA Lu W., Yamamoto V., Ortega B., Baltimore D.;
RT "Mammalian Ryk is a Wnt coreceptor required for stimulation of neurite
RT outgrowth.";
RL Cell 119:97-108(2004).
RN [10]
RP FUNCTION.
RX PubMed=16116452; DOI=10.1038/nn1520;
RA Liu Y., Shi J., Lu C.C., Wang Z.B., Lyuksyutova A.I., Song X.J., Zou Y.;
RT "Ryk-mediated Wnt repulsion regulates posterior-directed growth of
RT corticospinal tract.";
RL Nat. Neurosci. 8:1151-1159(2005).
RN [11]
RP INTERACTION WITH RSPO1; RSPO2 AND RSPO3.
RX PubMed=16543246; DOI=10.1074/jbc.m508324200;
RA Nam J.-S., Turcotte T.J., Smith P.F., Choi S., Yoon J.K.;
RT "Mouse cristin/R-spondin family proteins are novel ligands for the Frizzled
RT 8 and LRP6 receptors and activate beta-catenin-dependent gene expression.";
RL J. Biol. Chem. 281:13247-13257(2006).
RN [12]
RP INTERACTION WITH WLS.
RX PubMed=19841259; DOI=10.1073/pnas.0904894106;
RA Fu J., Jiang M., Mirando A.J., Yu H.-M., Hsu W.;
RT "Reciprocal regulation of Wnt and Gpr177/mouse Wntless is required for
RT embryonic axis formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18598-18603(2009).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=23499309; DOI=10.1016/j.ajhg.2013.02.010;
RA Keupp K., Beleggia F., Kayserili H., Barnes A.M., Steiner M., Semler O.,
RA Fischer B., Yigit G., Janda C.Y., Becker J., Breer S., Altunoglu U.,
RA Gruenhagen J., Krawitz P., Hecht J., Schinke T., Makareeva E., Lausch E.,
RA Cankaya T., Caparros-Martin J.A., Lapunzina P., Temtamy S., Aglan M.,
RA Zabel B., Eysel P., Koerber F., Leikin S., Garcia K.C., Netzer C.,
RA Schoenau E., Ruiz-Perez V.L., Mundlos S., Amling M., Kornak U., Marini J.,
RA Wollnik B.;
RT "Mutations in WNT1 cause different forms of bone fragility.";
RL Am. J. Hum. Genet. 92:565-574(2013).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=23656646; DOI=10.1056/nejmoa1215458;
RA Laine C.M., Joeng K.S., Campeau P.M., Kiviranta R., Tarkkonen K.,
RA Grover M., Lu J.T., Pekkinen M., Wessman M., Heino T.J.,
RA Nieminen-Pihala V., Aronen M., Laine T., Kroeger H., Cole W.G.,
RA Lehesjoki A.E., Nevarez L., Krakow D., Curry C.J., Cohn D.H., Gibbs R.A.,
RA Lee B.H., Maekitie O.;
RT "WNT1 mutations in early-onset osteoporosis and osteogenesis imperfecta.";
RL N. Engl. J. Med. 368:1809-1816(2013).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Acts in the canonical Wnt signaling pathway by
CC promoting beta-catenin-dependent transcriptional activation (By
CC similarity). In some developmental processes, is also a ligand for the
CC coreceptor RYK, thus triggering Wnt signaling (PubMed:15454084,
CC PubMed:16116452). Plays an essential role in the development of the
CC embryonic brain and central nervous system (CNS) (PubMed:2202907,
CC PubMed:16116452). Has a role in osteoblast function, bone development
CC and bone homeostasis (By similarity). {ECO:0000250|UniProtKB:P04628,
CC ECO:0000269|PubMed:15454084, ECO:0000269|PubMed:16116452,
CC ECO:0000269|PubMed:2202907}.
CC -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC oligomerization and is required for prolonged biological activity. The
CC complex with AFM may represent the physiological form in body fluids
CC (By similarity). Interacts with PORCN (PubMed:10866835). Interacts with
CC RSPO1, RSPO2 and RSPO3 (PubMed:16543246). Interacts with WLS
CC (PubMed:19841259). {ECO:0000250|UniProtKB:P04628,
CC ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:16543246,
CC ECO:0000269|PubMed:19841259}.
CC -!- INTERACTION:
CC P04426; O35082: Kl; NbExp=2; IntAct=EBI-1570911, EBI-1570828;
CC P04426; Q6DID7-1: Wls; NbExp=2; IntAct=EBI-1570911, EBI-15811068;
CC P04426; O75581: LRP6; Xeno; NbExp=2; IntAct=EBI-1570911, EBI-910915;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P04628}. Secreted
CC {ECO:0000250|UniProtKB:P04628}.
CC -!- TISSUE SPECIFICITY: Testis and mid-gestational embryos. In the testis,
CC detected only in postmeiotic germ cells undergoing differentiation from
CC round spermatids into mature spermatozoa. In the embryos, expression is
CC restricted to the developing CNS in regions of the neural tube other
CC than the telencephalon. Expressed in osteoblast; expression levels
CC increase with advancing osteoblast differentiation. Expressed in the
CC brain, femur, spleen, and hematopoietic bone marrow.
CC {ECO:0000269|PubMed:23499309, ECO:0000269|PubMed:23656646,
CC ECO:0000269|PubMed:3594566}.
CC -!- DEVELOPMENTAL STAGE: Accumulates throughout the neural plate at the
CC anterior head folds of the 9 day embryo but only at its lateral tips in
CC more posterior regions. Following neural tube closure, expression is
CC restricted to specific regions of the dorsal wall of the brain
CC ventricles and spinal cord, the ventral wall of the midbrain and the
CC diencephalon, and the lateral walls of the neuroepithelium at the
CC midbrain-hindbrain junction. {ECO:0000269|PubMed:3594565}.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors. Palmitoleoylation is necessary for proper trafficking to
CC cell surface (By similarity). Depalmitoleoylated by NOTUM, leading to
CC inhibit Wnt signaling pathway (By similarity).
CC {ECO:0000250|UniProtKB:P56704, ECO:0000250|UniProtKB:Q91029}.
CC -!- DISRUPTION PHENOTYPE: Important perinatal lethality, due to defects in
CC brain development. After 14.5 dpc, embryos display dramatic
CC malformations of the mesencephalon and metencephalon, and especially
CC the cerebellum. They show mild midbrain hydrocephaly by 17.5 dpc. Only
CC one out of ten live-born pups survives more than 30 days; these mice
CC respond normally to light, sound, smell and touch, but display severe
CC ataxia. {ECO:0000269|PubMed:2202907}.
CC -!- MISCELLANEOUS: Many mouse mammary tumors induced by mouse mammary tumor
CC virus (MMTV) contain a provirus integrated into a host cell region
CC which has been named INT-1 (now Wnt1). {ECO:0000269|PubMed:6091914}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC -!- CAUTION: A palmitoylation site was proposed at Cys-93, but it was later
CC shown that this cysteine is engaged in a disulfide bond.
CC {ECO:0000250|UniProtKB:P04628}.
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DR EMBL; K02593; AAA39321.1; -; Genomic_DNA.
DR EMBL; M11943; AAA39322.1; -; mRNA.
DR EMBL; BC005449; AAH05449.1; -; mRNA.
DR CCDS; CCDS27807.1; -.
DR PIR; A23447; TVMST1.
DR RefSeq; NP_067254.1; NM_021279.4.
DR AlphaFoldDB; P04426; -.
DR SMR; P04426; -.
DR BioGRID; 204567; 9.
DR CORUM; P04426; -.
DR DIP; DIP-39896N; -.
DR IntAct; P04426; 4.
DR STRING; 10090.ENSMUSP00000023734; -.
DR GlyGen; P04426; 4 sites.
DR iPTMnet; P04426; -.
DR PhosphoSitePlus; P04426; -.
DR SwissPalm; P04426; -.
DR PaxDb; P04426; -.
DR PRIDE; P04426; -.
DR Antibodypedia; 13738; 563 antibodies from 40 providers.
DR DNASU; 22408; -.
DR Ensembl; ENSMUST00000023734; ENSMUSP00000023734; ENSMUSG00000022997.
DR GeneID; 22408; -.
DR KEGG; mmu:22408; -.
DR UCSC; uc007xnx.1; mouse.
DR CTD; 7471; -.
DR MGI; MGI:98953; Wnt1.
DR VEuPathDB; HostDB:ENSMUSG00000022997; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000160329; -.
DR HOGENOM; CLU_033039_1_1_1; -.
DR InParanoid; P04426; -.
DR OMA; NDHMPDI; -.
DR OrthoDB; 624528at2759; -.
DR PhylomeDB; P04426; -.
DR TreeFam; TF105310; -.
DR Reactome; R-MMU-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR BioGRID-ORCS; 22408; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Wnt1; mouse.
DR PRO; PR:P04426; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P04426; protein.
DR Bgee; ENSMUSG00000022997; Expressed in presumptive midbrain and 56 other tissues.
DR ExpressionAtlas; P04426; baseline and differential.
DR Genevisible; P04426; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1990909; C:Wnt signalosome; IC:ParkinsonsUK-UCL.
DR GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0048018; F:receptor ligand activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005102; F:signaling receptor binding; TAS:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
DR GO; GO:0031100; P:animal organ regeneration; ISO:MGI.
DR GO; GO:0036520; P:astrocyte-dopaminergic neuron signaling; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:MGI.
DR GO; GO:0060348; P:bone development; ISS:UniProtKB.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:1904954; P:canonical Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0033278; P:cell proliferation in midbrain; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007267; P:cell-cell signaling; IDA:BHF-UCL.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
DR GO; GO:0021551; P:central nervous system morphogenesis; IMP:BHF-UCL.
DR GO; GO:0021549; P:cerebellum development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021588; P:cerebellum formation; IMP:BHF-UCL.
DR GO; GO:0021536; P:diencephalon development; IGI:MGI.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IMP:CACAO.
DR GO; GO:0000578; P:embryonic axis specification; IMP:BHF-UCL.
DR GO; GO:1990403; P:embryonic brain development; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR GO; GO:0021797; P:forebrain anterior/posterior pattern specification; IGI:MGI.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:MGI.
DR GO; GO:0070365; P:hepatocyte differentiation; ISO:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IGI:MGI.
DR GO; GO:0022037; P:metencephalon development; IMP:MGI.
DR GO; GO:0030901; P:midbrain development; IDA:ParkinsonsUK-UCL.
DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030917; P:midbrain-hindbrain boundary development; IMP:MGI.
DR GO; GO:0022004; P:midbrain-hindbrain boundary maturation during brain development; IMP:MGI.
DR GO; GO:0007520; P:myoblast fusion; IDA:MGI.
DR GO; GO:0014902; P:myotube differentiation; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IMP:AgBase.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISO:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:MGI.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0022008; P:neurogenesis; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
DR GO; GO:0048664; P:neuron fate determination; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0061184; P:positive regulation of dermatome development; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IDA:MGI.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ParkinsonsUK-UCL.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; ISO:MGI.
DR GO; GO:0060061; P:Spemann organizer formation; IMP:BHF-UCL.
DR GO; GO:0021527; P:spinal cord association neuron differentiation; IGI:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IDA:MGI.
DR GO; GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; IDA:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:ParkinsonsUK-UCL.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR009139; Wnt1.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01841; WNT1PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Proto-oncogene; Reference proteome; Secreted; Signal;
KW Wnt signaling pathway.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..370
FT /note="Proto-oncogene Wnt-1"
FT /id="PRO_0000041406"
FT LIPID 224
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:Q91029"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..104
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 143..151
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 153..170
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 218..232
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 220..227
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 299..330
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 315..325
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 329..369
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 345..360
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 347..357
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 352..353
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 370 AA; 41086 MW; 02EEB23109231A40 CRC64;
MGLWALLPSW VSTTLLLALT ALPAALAANS SGRWWGIVNI ASSTNLLTDS KSLQLVLEPS
LQLLSRKQRR LIRQNPGILH SVSGGLQSAV RECKWQFRNR RWNCPTAPGP HLFGKIVNRG
CRETAFIFAI TSAGVTHSVA RSCSEGSIES CTCDYRRRGP GGPDWHWGGC SDNIDFGRLF
GREFVDSGEK GRDLRFLMNL HNNEAGRTTV FSEMRQECKC HGMSGSCTVR TCWMRLPTLR
AVGDVLRDRF DGASRVLYGN RGSNRASRAE LLRLEPEDPA HKPPSPHDLV YFEKSPNFCT
YSGRLGTAGT AGRACNSSSP ALDGCELLCC GRGHRTRTQR VTERCNCTFH WCCHVSCRNC
THTRVLHECL
