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   27-MAR-2024, entry version 200.
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,
GN   ECO:0000303|PubMed:3018519, 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   GlyCosmos; P04426; 4 sites, No reported glycans.
DR   GlyGen; P04426; 4 sites.
DR   iPTMnet; P04426; -.
DR   PhosphoSitePlus; P04426; -.
DR   SwissPalm; P04426; -.
DR   PaxDb; 10090-ENSMUSP00000023734; -.
DR   Antibodypedia; 13738; 622 antibodies from 40 providers.
DR   DNASU; 22408; -.
DR   Ensembl; ENSMUST00000023734.8; ENSMUSP00000023734.8; ENSMUSG00000022997.10.
DR   GeneID; 22408; -.
DR   KEGG; mmu:22408; -.
DR   UCSC; uc007xnx.1; mouse.
DR   AGR; MGI:98953; -.
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; 2874082at2759; -.
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 79 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 58 other cell types or tissues.
DR   ExpressionAtlas; P04426; baseline and differential.
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; IPI:BHF-UCL.
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: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; IDA: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:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; 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:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
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:0006355; P:regulation of DNA-templated transcription; 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:0016055; P:Wnt signaling pathway; IDA:ParkinsonsUK-UCL.
DR   CDD; cd19333; Wnt_Wnt1; 1.
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:SF91; PROTO-ONCOGENE WNT-1; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01841; WNT1PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
DR   Genevisible; P04426; MM.
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
//