ID   OSMR_HUMAN              Reviewed;         979 AA.
AC   Q99650; Q6P4E8; Q96QJ6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Oncostatin-M-specific receptor subunit beta;
DE   AltName: Full=Interleukin-31 receptor subunit beta;
DE            Short=IL-31 receptor subunit beta;
DE            Short=IL-31R subunit beta;
DE            Short=IL-31R-beta;
DE            Short=IL-31RB;
DE   Flags: Precursor;
GN   Name=OSMR; Synonyms=OSMRB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, INDUCTION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=8999038; DOI=10.1074/jbc.271.51.32635;
RA   Mosley B., De Imus C., Friend D., Boiani N., Thoma B., Park L.S.,
RA   Cosman D.;
RT   "Dual oncostatin M (OSM) receptors. Cloning and characterization of an
RT   alternative signaling subunit conferring OSM-specific receptor
RT   activation.";
RL   J. Biol. Chem. 271:32635-32643(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   TRP-210.
RC   TISSUE=Colon, and Placenta;
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   [3]
RP   FUNCTION, OLIGOMERIZATION, AND INDUCTION.
RX   PubMed=15184896; DOI=10.1038/ni1084;
RA   Dillon S.R., Sprecher C., Hammond A., Bilsborough J.,
RA   Rosenfeld-Franklin M., Presnell S.R., Haugen H.S., Maurer M., Harder B.,
RA   Johnston J., Bort S., Mudri S., Kuijper J.L., Bukowski T., Shea P.,
RA   Dong D.L., Dasovich M., Grant F.J., Lockwood L., Levin S.D., LeCiel C.,
RA   Waggie K., Day H., Topouzis S., Kramer J., Kuestner R., Chen Z., Foster D.,
RA   Parrish-Novak J., Gross J.A.;
RT   "Interleukin 31, a cytokine produced by activated T cells, induces
RT   dermatitis in mice.";
RL   Nat. Immunol. 5:752-760(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826 AND SER-889, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [6]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=21261663; DOI=10.1111/j.1398-9995.2011.02545.x;
RA   Kasraie S., Niebuhr M., Baumert K., Werfel T.;
RT   "Functional effects of interleukin 31 in human primary keratinocytes.";
RL   Allergy 66:845-852(2011).
RN   [7]
RP   VARIANTS PLCA1 ALA-618 AND THR-691.
RX   PubMed=18179886; DOI=10.1016/j.ajhg.2007.09.002;
RA   Arita K., South A.P., Hans-Filho G., Sakuma T.H., Lai-Cheong J.,
RA   Clements S., Odashiro M., Odashiro D.N., Hans-Neto G., Hans N.R.,
RA   Holder M.V., Bhogal B.S., Hartshorne S.T., Akiyama M., Shimizu H.,
RA   McGrath J.A.;
RT   "Oncostatin M receptor-beta mutations underlie familial primary localized
RT   cutaneous amyloidosis.";
RL   Am. J. Hum. Genet. 82:73-80(2008).
RN   [8]
RP   VARIANTS PLCA1 VAL-647; LEU-694 AND THR-697.
RX   PubMed=19690585; DOI=10.1038/ejhg.2009.135;
RA   Lin M.W., Lee D.D., Liu T.T., Lin Y.F., Chen S.Y., Huang C.C., Weng H.Y.,
RA   Liu Y.F., Tanaka A., Arita K., Lai-Cheong J., Palisson F., Chang Y.T.,
RA   Wong C.K., Matsuura I., McGrath J.A., Tsai S.F.;
RT   "Novel IL31RA gene mutation and ancestral OSMR mutant allele in familial
RT   primary cutaneous amyloidosis.";
RL   Eur. J. Hum. Genet. 18:26-32(2010).
CC   -!- FUNCTION: Associates with IL31RA to form the IL31 receptor. Binds IL31
CC       to activate STAT3 and possibly STAT1 and STAT5. Capable of transducing
CC       OSM-specific signaling events. {ECO:0000269|PubMed:15184896,
CC       ECO:0000269|PubMed:8999038}.
CC   -!- SUBUNIT: Heterodimer composed of OSMR and IL6ST (type II OSM receptor).
CC       Heterodimer with IL31RA to form the IL31 receptor.
CC       {ECO:0000269|PubMed:8999038}.
CC   -!- INTERACTION:
CC       Q99650; Q9UII2: ATP5IF1; NbExp=4; IntAct=EBI-2804080, EBI-718459;
CC       Q99650; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-2804080, EBI-13067820;
CC       Q99650; P38646: HSPA9; NbExp=4; IntAct=EBI-2804080, EBI-354932;
CC       Q99650; P40189: IL6ST; NbExp=2; IntAct=EBI-2804080, EBI-1030834;
CC       Q99650; P50458: LHX2; NbExp=3; IntAct=EBI-2804080, EBI-12179869;
CC       Q99650; P28331: NDUFS1; NbExp=4; IntAct=EBI-2804080, EBI-1043922;
CC       Q99650; O75306: NDUFS2; NbExp=4; IntAct=EBI-2804080, EBI-1224806;
CC       Q99650; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2804080, EBI-744081;
CC       Q99650; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2804080, EBI-18159983;
CC       Q99650; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2804080, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99650-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99650-2; Sequence=VSP_021527, VSP_021528;
CC   -!- TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level)
CC       (PubMed:21261663). Expressed at relatively high levels in all neural
CC       cells as well as fibroblast and epithelial cells (PubMed:8999038).
CC       {ECO:0000269|PubMed:21261663, ECO:0000269|PubMed:8999038}.
CC   -!- INDUCTION: Activated by oncostatin-M (PubMed:8999038). Up-regulated by
CC       IFNG/IFN-gamma (PubMed:15184896, PubMed:21261663). Up-regulated by
CC       bacterial lipopolysaccharides (LPS) (PubMed:15184896). Up-regulated by
CC       triacylated lipoprotein (Pam3Cys) (PubMed:21261663).
CC       {ECO:0000269|PubMed:15184896, ECO:0000269|PubMed:21261663,
CC       ECO:0000269|PubMed:8999038}.
CC   -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC       folding and thereby efficient intracellular transport and cell-surface
CC       receptor binding. {ECO:0000250}.
CC   -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC       activation. {ECO:0000250}.
CC   -!- DISEASE: Amyloidosis, primary localized cutaneous, 1 (PLCA1)
CC       [MIM:105250]: A primary amyloidosis characterized by localized
CC       cutaneous amyloid deposition. This condition usually presents with
CC       itching (especially on the lower legs) and visible changes of skin
CC       hyperpigmentation and thickening that may be exacerbated by chronic
CC       scratching and rubbing. Primary localized cutaneous amyloidosis is
CC       often divided into macular and lichen subtypes although many affected
CC       individuals often show both variants coexisting. Lichen amyloidosis
CC       characteristically presents as a pruritic eruption of grouped
CC       hyperkeratotic papules with a predilection for the shins, calves,
CC       ankles and dorsa of feet and thighs. Papules may coalesce to form
CC       hyperkeratotic plaques that can resemble lichen planus, lichen simplex
CC       or nodular prurigo. Macular amyloidosis is characterized by small
CC       pigmented macules that may merge to produce macular hyperpigmentation,
CC       sometimes with a reticulate or rippled pattern. In macular and lichen
CC       amyloidosis, amyloid is deposited in the papillary dermis in
CC       association with grouped colloid bodies, thought to represent
CC       degenerate basal keratinocytes. The amyloid deposits probably reflect a
CC       combination of degenerate keratin filaments, serum amyloid P component,
CC       and deposition of immunoglobulins. {ECO:0000269|PubMed:18179886,
CC       ECO:0000269|PubMed:19690585}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH63468.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH63468.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U60805; AAC50946.1; -; mRNA.
DR   EMBL; BC010943; AAH10943.1; -; mRNA.
DR   EMBL; BC063468; AAH63468.1; ALT_SEQ; mRNA.
DR   EMBL; BC125209; AAI25210.1; -; mRNA.
DR   EMBL; BC125210; AAI25211.1; -; mRNA.
DR   CCDS; CCDS3928.1; -. [Q99650-1]
DR   CCDS; CCDS54847.1; -. [Q99650-2]
DR   RefSeq; NP_001161827.1; NM_001168355.2. [Q99650-2]
DR   RefSeq; NP_001310433.1; NM_001323504.1. [Q99650-2]
DR   RefSeq; NP_001310434.1; NM_001323505.1. [Q99650-1]
DR   RefSeq; NP_001310435.1; NM_001323506.1.
DR   RefSeq; NP_001310436.1; NM_001323507.1.
DR   RefSeq; NP_003990.1; NM_003999.2. [Q99650-1]
DR   AlphaFoldDB; Q99650; -.
DR   SMR; Q99650; -.
DR   BioGRID; 114617; 116.
DR   IntAct; Q99650; 26.
DR   MINT; Q99650; -.
DR   STRING; 9606.ENSP00000274276; -.
DR   ChEMBL; CHEMBL4630885; -.
DR   GlyConnect; 1965; 16 N-Linked glycans (8 sites).
DR   GlyCosmos; Q99650; 12 sites, 18 glycans.
DR   GlyGen; Q99650; 12 sites, 17 N-linked glycans (8 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q99650; -.
DR   PhosphoSitePlus; Q99650; -.
DR   SwissPalm; Q99650; -.
DR   BioMuta; OSMR; -.
DR   DMDM; 74724833; -.
DR   EPD; Q99650; -.
DR   jPOST; Q99650; -.
DR   MassIVE; Q99650; -.
DR   MaxQB; Q99650; -.
DR   PaxDb; 9606-ENSP00000274276; -.
DR   PeptideAtlas; Q99650; -.
DR   ProteomicsDB; 78379; -. [Q99650-1]
DR   ProteomicsDB; 78380; -. [Q99650-2]
DR   Pumba; Q99650; -.
DR   Antibodypedia; 2731; 475 antibodies from 35 providers.
DR   DNASU; 9180; -.
DR   Ensembl; ENST00000274276.8; ENSP00000274276.3; ENSG00000145623.13. [Q99650-1]
DR   Ensembl; ENST00000502536.5; ENSP00000422023.1; ENSG00000145623.13. [Q99650-2]
DR   GeneID; 9180; -.
DR   KEGG; hsa:9180; -.
DR   MANE-Select; ENST00000274276.8; ENSP00000274276.3; NM_003999.3; NP_003990.1.
DR   UCSC; uc003jlm.2; human. [Q99650-1]
DR   AGR; HGNC:8507; -.
DR   CTD; 9180; -.
DR   DisGeNET; 9180; -.
DR   GeneCards; OSMR; -.
DR   HGNC; HGNC:8507; OSMR.
DR   HPA; ENSG00000145623; Low tissue specificity.
DR   MalaCards; OSMR; -.
DR   MIM; 105250; phenotype.
DR   MIM; 601743; gene.
DR   neXtProt; NX_Q99650; -.
DR   OpenTargets; ENSG00000145623; -.
DR   Orphanet; 353220; Familial primary localized cutaneous amyloidosis.
DR   PharmGKB; PA32837; -.
DR   VEuPathDB; HostDB:ENSG00000145623; -.
DR   eggNOG; ENOG502QWRV; Eukaryota.
DR   GeneTree; ENSGT00940000160851; -.
DR   HOGENOM; CLU_046956_0_0_1; -.
DR   InParanoid; Q99650; -.
DR   OMA; GKMMQYN; -.
DR   OrthoDB; 5347052at2759; -.
DR   PhylomeDB; Q99650; -.
DR   TreeFam; TF338122; -.
DR   PathwayCommons; Q99650; -.
DR   Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions.
DR   SignaLink; Q99650; -.
DR   SIGNOR; Q99650; -.
DR   BioGRID-ORCS; 9180; 9 hits in 1149 CRISPR screens.
DR   ChiTaRS; OSMR; human.
DR   GeneWiki; Oncostatin_M_receptor; -.
DR   GenomeRNAi; 9180; -.
DR   Pharos; Q99650; Tbio.
DR   PRO; PR:Q99650; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q99650; Protein.
DR   Bgee; ENSG00000145623; Expressed in pericardium and 168 other cell types or tissues.
DR   ExpressionAtlas; Q99650; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:CACAO.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005900; C:oncostatin-M receptor complex; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; IBA:GO_Central.
DR   GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0019838; F:growth factor binding; IPI:BHF-UCL.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0002675; P:positive regulation of acute inflammatory response; IC:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:BHF-UCL.
DR   GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL.
DR   CDD; cd00063; FN3; 4.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR048497; LIF-R-like_Ig-like.
DR   InterPro; IPR040817; LIFR_D2.
DR   PANTHER; PTHR23036; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR23036:SF95; ONCOSTATIN-M-SPECIFIC RECEPTOR SUBUNIT BETA; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF21177; LIF-R_Ig-like; 1.
DR   Pfam; PF17971; LIFR_D2; 1.
DR   SMART; SM00060; FN3; 4.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
DR   Genevisible; Q99650; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amyloidosis; Disease variant; Disulfide bond;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..979
FT                   /note="Oncostatin-M-specific receptor subunit beta"
FT                   /id="PRO_0000259759"
FT   TOPO_DOM        28..740
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        741..761
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        762..979
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          335..428
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          433..528
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          529..623
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          625..736
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   MOTIF           415..419
FT                   /note="WSXWS motif"
FT   MOTIF           770..778
FT                   /note="Box 1 motif"
FT   MOD_RES         826
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         889
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        380
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        245..255
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         331..342
FT                   /note="VYLMNPFSVNFE -> GETRVVTAHRGH (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021527"
FT   VAR_SEQ         343..979
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021528"
FT   VARIANT         187
FT                   /note="H -> Q (in dbSNP:rs34675408)"
FT                   /id="VAR_043512"
FT   VARIANT         210
FT                   /note="G -> W (in dbSNP:rs17855841)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_028972"
FT   VARIANT         527
FT                   /note="E -> K (in dbSNP:rs10941412)"
FT                   /id="VAR_028973"
FT   VARIANT         553
FT                   /note="D -> N (in dbSNP:rs2278329)"
FT                   /id="VAR_028974"
FT   VARIANT         618
FT                   /note="G -> A (in PLCA1; dbSNP:rs63750560)"
FT                   /evidence="ECO:0000269|PubMed:18179886"
FT                   /id="VAR_043513"
FT   VARIANT         647
FT                   /note="D -> V (in PLCA1; dbSNP:rs387906821)"
FT                   /evidence="ECO:0000269|PubMed:19690585"
FT                   /id="VAR_065810"
FT   VARIANT         691
FT                   /note="I -> T (in PLCA1; dbSNP:rs63750567)"
FT                   /evidence="ECO:0000269|PubMed:18179886"
FT                   /id="VAR_043514"
FT   VARIANT         694
FT                   /note="P -> L (in PLCA1; dbSNP:rs387906822)"
FT                   /evidence="ECO:0000269|PubMed:19690585"
FT                   /id="VAR_065811"
FT   VARIANT         697
FT                   /note="K -> T (in PLCA1; dbSNP:rs387906823)"
FT                   /evidence="ECO:0000269|PubMed:19690585"
FT                   /id="VAR_065812"
FT   VARIANT         936
FT                   /note="P -> S (in dbSNP:rs3749737)"
FT                   /id="VAR_028975"
FT   VARIANT         959
FT                   /note="P -> R (in dbSNP:rs34080825)"
FT                   /id="VAR_043515"
SQ   SEQUENCE   979 AA;  110509 MW;  179852CA3D90D9EF CRC64;
     MALFAVFQTT FFLTLLSLRT YQSEVLAERL PLTPVSLKVS TNSTRQSLHL QWTVHNLPYH
     QELKMVFQIQ ISRIETSNVI WVGNYSTTVK WNQVLHWSWE SELPLECATH FVRIKSLVDD
     AKFPEPNFWS NWSSWEEVSV QDSTGQDILF VFPKDKLVEE GTNVTICYVS RNIQNNVSCY
     LEGKQIHGEQ LDPHVTAFNL NSVPFIRNKG TNIYCEASQG NVSEGMKGIV LFVSKVLEEP
     KDFSCETEDF KTLHCTWDPG TDTALGWSKQ PSQSYTLFES FSGEKKLCTH KNWCNWQITQ
     DSQETYNFTL IAENYLRKRS VNILFNLTHR VYLMNPFSVN FENVNATNAI MTWKVHSIRN
     NFTYLCQIEL HGEGKMMQYN VSIKVNGEYF LSELEPATEY MARVRCADAS HFWKWSEWSG
     QNFTTLEAAP SEAPDVWRIV SLEPGNHTVT LFWKPLSKLH ANGKILFYNV VVENLDKPSS
     SELHSIPAPA NSTKLILDRC SYQICVIANN SVGASPASVI VISADPENKE VEEERIAGTE
     GGFSLSWKPQ PGDVIGYVVD WCDHTQDVLG DFQWKNVGPN TTSTVISTDA FRPGVRYDFR
     IYGLSTKRIA CLLEKKTGYS QELAPSDNPH VLVDTLTSHS FTLSWKDYST ESQPGFIQGY
     HVYLKSKARQ CHPRFEKAVL SDGSECCKYK IDNPEEKALI VDNLKPESFY EFFITPFTSA
     GEGPSATFTK VTTPDEHSSM LIHILLPMVF CVLLIMVMCY LKSQWIKETC YPDIPDPYKS
     SILSLIKFKE NPHLIIMNVS DCIPDAIEVV SKPEGTKIQF LGTRKSLTET ELTKPNYLYL
     LPTEKNHSGP GPCICFENLT YNQAASDSGS CGHVPVSPKA PSMLGLMTSP ENVLKALEKN
     YMNSLGEIPA GETSLNYVSQ LASPMFGDKD SLPTNPVEAP HCSEYKMQMA VSLRLALPPP
     TENSSLSSIT LLDPGEHYC
//