OSMR_HUMAN
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 03-AUG-2022, entry version 175.
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; 115.
DR IntAct; Q99650; 25.
DR MINT; Q99650; -.
DR STRING; 9606.ENSP00000274276; -.
DR ChEMBL; CHEMBL4630885; -.
DR GlyConnect; 1965; 16 N-Linked glycans (8 sites).
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; Q99650; -.
DR PeptideAtlas; Q99650; -.
DR PRIDE; Q99650; -.
DR ProteomicsDB; 78379; -. [Q99650-1]
DR ProteomicsDB; 78380; -. [Q99650-2]
DR Antibodypedia; 2731; 441 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 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; SGSCGHV; -.
DR OrthoDB; 331447at2759; -.
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 1069 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 166 other tissues.
DR ExpressionAtlas; Q99650; baseline and differential.
DR Genevisible; Q99650; HS.
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:0004923; F:leukemia inhibitory factor receptor activity; IBA:GO_Central.
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; -; 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; IPR040817; LIFR_D2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF17971; LIFR_D2; 1.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
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
