LIFR_HUMAN
ID LIFR_HUMAN Reviewed; 1097 AA.
AC P42702; Q6LCD9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Leukemia inhibitory factor receptor;
DE Short=LIF receptor;
DE Short=LIF-R;
DE AltName: CD_antigen=CD118;
DE Flags: Precursor;
GN Name=LIFR;
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).
RC TISSUE=Placenta;
RX PubMed=1915266; DOI=10.1002/j.1460-2075.1991.tb07833.x;
RA Gearing D.P., Thut C.J., Vanden Bos T., Gimpel S.D., Delaney P.B., King J.,
RA Price V., Cosman D., Beckmann M.P.;
RT "Leukemia inhibitory factor receptor is structurally related to the IL-6
RT signal transducer, gp130.";
RL EMBO J. 10:2839-2848(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 942-1097.
RA Wang Z., Melmed S.;
RT "Human LIF receptor 3' non-coding region.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHROMOSOMAL TRANSLOCATION WITH PLAG1.
RX PubMed=9525740; DOI=10.1038/sj.onc.1201660;
RA Voz M.L., Astrom A.-K., Kas K., Mark J., Stenman G., Van de Ven W.J.M.;
RT "The recurrent translocation t(5;8)(p13;q12) in pleomorphic adenomas
RT results in upregulation of PLAG1 gene expression under control of the LIFR
RT promoter.";
RL Oncogene 16:1409-1416(1998).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927, AND IDENTIFICATION BY
RP 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 X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 52-534, IDENTIFICATION IN A
RP COMPLEX WITH IL6ST; CNTF AND CNTFR, GLYCOSYLATION AT ASN-131; ASN-303;
RP ASN-407 AND ASN-426, DISULFIDE BONDS, ELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=18775332; DOI=10.1016/j.molcel.2008.08.011;
RA Skiniotis G., Lupardus P.J., Martick M., Walz T., Garcia K.C.;
RT "Structural organization of a full-length gp130/LIF-R cytokine receptor
RT transmembrane complex.";
RL Mol. Cell 31:737-748(2008).
RN [6]
RP VARIANT STWS PRO-279.
RX PubMed=14740318; DOI=10.1086/381715;
RA Dagoneau N., Scheffer D., Huber C., Al-Gazali L.I., Di Rocco M., Godard A.,
RA Martinovic J., Raas-Rothschild A., Sigaudy S., Unger S., Nicole S.,
RA Fontaine B., Taupin J.-L., Moreau J.-F., Superti-Furga A., Le Merrer M.,
RA Bonaventure J., Munnich A., Legeai-Mallet L., Cormier-Daire V.;
RT "Null leukemia inhibitory factor receptor (LIFR) mutations in Stueve-
RT Wiedemann/Schwartz-Jampel type 2 syndrome.";
RL Am. J. Hum. Genet. 74:298-305(2004).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-1068.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Signal-transducing molecule. May have a common pathway with
CC IL6ST. The soluble form inhibits the biological activity of LIF by
CC blocking its binding to receptors on target cells.
CC -!- SUBUNIT: Heterodimer composed of LIFR and IL6ST. The heterodimer formed
CC by LIFR and IL6ST interacts with the complex formed by CNTF and CNTFR.
CC {ECO:0000269|PubMed:18775332}.
CC -!- INTERACTION:
CC P42702; P26441: CNTF; NbExp=9; IntAct=EBI-7702162, EBI-1050897;
CC P42702; Q99523: SORT1; NbExp=3; IntAct=EBI-7702162, EBI-1057058;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Membrane;
CC IsoId=P42702-1; Sequence=Displayed;
CC Name=2; Synonyms=Secreted;
CC IsoId=P42702-2; Sequence=Not described;
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.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- DISEASE: Stuve-Wiedemann syndrome (STWS) [MIM:601559]: A form of Stuve-
CC Wiedemann syndrome, an autosomal recessive disease characterized by
CC bowing of tubular bones and other skeletal and craniofacial
CC abnormalities, respiratory distress, feeding difficulties, and
CC hyperthermic episodes. Most patients do not survive past infancy.
CC {ECO:0000269|PubMed:14740318}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving LIFR is found in
CC salivary gland pleiomorphic adenomas, the most common benign epithelial
CC tumors of the salivary gland. Translocation t(5;8)(p13;q12) with PLAG1.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LIFRID410ch5p13.html";
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DR EMBL; X61615; CAA43805.1; -; mRNA.
DR EMBL; U66563; AAB61897.1; -; mRNA.
DR CCDS; CCDS3927.1; -. [P42702-1]
DR PIR; S17308; S17308.
DR RefSeq; NP_001121143.1; NM_001127671.1. [P42702-1]
DR RefSeq; NP_002301.1; NM_002310.5. [P42702-1]
DR RefSeq; XP_011512342.1; XM_011514040.2.
DR RefSeq; XP_011512344.1; XM_011514042.2. [P42702-1]
DR RefSeq; XP_016864952.1; XM_017009463.1. [P42702-1]
DR PDB; 3E0G; X-ray; 3.10 A; A=52-534.
DR PDBsum; 3E0G; -.
DR AlphaFoldDB; P42702; -.
DR SMR; P42702; -.
DR BioGRID; 110165; 39.
DR CORUM; P42702; -.
DR DIP; DIP-5770N; -.
DR IntAct; P42702; 15.
DR MINT; P42702; -.
DR STRING; 9606.ENSP00000263409; -.
DR GlyGen; P42702; 19 sites.
DR iPTMnet; P42702; -.
DR PhosphoSitePlus; P42702; -.
DR BioMuta; LIFR; -.
DR DMDM; 1170784; -.
DR EPD; P42702; -.
DR jPOST; P42702; -.
DR MassIVE; P42702; -.
DR MaxQB; P42702; -.
DR PaxDb; P42702; -.
DR PeptideAtlas; P42702; -.
DR PRIDE; P42702; -.
DR ProteomicsDB; 55546; -. [P42702-1]
DR Antibodypedia; 4137; 472 antibodies from 31 providers.
DR DNASU; 3977; -.
DR Ensembl; ENST00000263409.8; ENSP00000263409.4; ENSG00000113594.10. [P42702-1]
DR Ensembl; ENST00000453190.7; ENSP00000398368.2; ENSG00000113594.10. [P42702-1]
DR GeneID; 3977; -.
DR KEGG; hsa:3977; -.
DR MANE-Select; ENST00000453190.7; ENSP00000398368.2; NM_001127671.2; NP_001121143.1.
DR UCSC; uc003jli.3; human. [P42702-1]
DR CTD; 3977; -.
DR DisGeNET; 3977; -.
DR GeneCards; LIFR; -.
DR HGNC; HGNC:6597; LIFR.
DR HPA; ENSG00000113594; Low tissue specificity.
DR MalaCards; LIFR; -.
DR MIM; 151443; gene.
DR MIM; 601559; phenotype.
DR neXtProt; NX_P42702; -.
DR OpenTargets; ENSG00000113594; -.
DR Orphanet; 3206; Stueve-Wiedemann syndrome.
DR PharmGKB; PA30371; -.
DR VEuPathDB; HostDB:ENSG00000113594; -.
DR eggNOG; ENOG502QQF6; Eukaryota.
DR GeneTree; ENSGT00940000155776; -.
DR HOGENOM; CLU_283805_0_0_1; -.
DR InParanoid; P42702; -.
DR OMA; HYVKIRC; -.
DR OrthoDB; 331447at2759; -.
DR PhylomeDB; P42702; -.
DR TreeFam; TF338122; -.
DR PathwayCommons; P42702; -.
DR Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions.
DR Reactome; R-HSA-8939247; RUNX1 regulates transcription of genes involved in interleukin signaling.
DR SignaLink; P42702; -.
DR SIGNOR; P42702; -.
DR BioGRID-ORCS; 3977; 15 hits in 1083 CRISPR screens.
DR ChiTaRS; LIFR; human.
DR EvolutionaryTrace; P42702; -.
DR GeneWiki; Leukemia_inhibitory_factor_receptor; -.
DR GenomeRNAi; 3977; -.
DR Pharos; P42702; Tbio.
DR PRO; PR:P42702; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P42702; protein.
DR Bgee; ENSG00000113594; Expressed in medial globus pallidus and 186 other tissues.
DR ExpressionAtlas; P42702; baseline and differential.
DR Genevisible; P42702; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; IPI:BHF-UCL.
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; IDA:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 8.
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 InterPro; IPR040901; LIFR_N.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF17971; LIFR_D2; 1.
DR Pfam; PF18207; LIFR_N; 1.
DR SMART; SM00060; FN3; 5.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Chromosomal rearrangement; Disease variant; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..1097
FT /note="Leukemia inhibitory factor receptor"
FT /id="PRO_0000010902"
FT TOPO_DOM 45..833
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 834..858
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 859..1097
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..138
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 335..434
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 435..534
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 538..629
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 627..719
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 724..833
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 983..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 519..523
FT /note="WSXWS motif"
FT MOTIF 869..877
FT /note="Box 1 motif"
FT COMPBIAS 1081..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42703"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18775332"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18775332"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18775332"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18775332"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..65
FT /evidence="ECO:0000269|PubMed:18775332"
FT DISULFID 82..90
FT /evidence="ECO:0000269|PubMed:18775332"
FT DISULFID 213..270
FT /evidence="ECO:0000269|PubMed:18775332"
FT DISULFID 341..351
FT /evidence="ECO:0000269|PubMed:18775332"
FT DISULFID 466..511
FT /evidence="ECO:0000269|PubMed:18775332"
FT VARIANT 116
FT /note="H -> Y (in dbSNP:rs3729734)"
FT /id="VAR_029109"
FT VARIANT 279
FT /note="S -> P (in STWS)"
FT /evidence="ECO:0000269|PubMed:14740318"
FT /id="VAR_025666"
FT VARIANT 578
FT /note="D -> N (in dbSNP:rs3729740)"
FT /id="VAR_029110"
FT VARIANT 633
FT /note="I -> M (in dbSNP:rs2303743)"
FT /id="VAR_021996"
FT VARIANT 664
FT /note="S -> L (in dbSNP:rs3729744)"
FT /id="VAR_038626"
FT VARIANT 785
FT /note="V -> I (in dbSNP:rs3110234)"
FT /id="VAR_029111"
FT VARIANT 1068
FT /note="F -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036166"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3E0G"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:3E0G"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 169..181
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:3E0G"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:3E0G"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:3E0G"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 418..425
FT /evidence="ECO:0007829|PDB:3E0G"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:3E0G"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:3E0G"
SQ SEQUENCE 1097 AA; 123743 MW; C8602897E359FCE5 CRC64;
MMDIYVCLKR PSWMVDNKRM RTASNFQWLL STFILLYLMN QVNSQKKGAP HDLKCVTNNL
QVWNCSWKAP SGTGRGTDYE VCIENRSRSC YQLEKTSIKI PALSHGDYEI TINSLHDFGS
STSKFTLNEQ NVSLIPDTPE ILNLSADFST STLYLKWNDR GSVFPHRSNV IWEIKVLRKE
SMELVKLVTH NTTLNGKDTL HHWSWASDMP LECAIHFVEI RCYIDNLHFS GLEEWSDWSP
VKNISWIPDS QTKVFPQDKV ILVGSDITFC CVSQEKVLSA LIGHTNCPLI HLDGENVAIK
IRNISVSASS GTNVVFTTED NIFGTVIFAG YPPDTPQQLN CETHDLKEII CSWNPGRVTA
LVGPRATSYT LVESFSGKYV RLKRAEAPTN ESYQLLFQML PNQEIYNFTL NAHNPLGRSQ
STILVNITEK VYPHTPTSFK VKDINSTAVK LSWHLPGNFA KINFLCEIEI KKSNSVQEQR
NVTIKGVENS SYLVALDKLN PYTLYTFRIR CSTETFWKWS KWSNKKQHLT TEASPSKGPD
TWREWSSDGK NLIIYWKPLP INEANGKILS YNVSCSSDEE TQSLSEIPDP QHKAEIRLDK
NDYIISVVAK NSVGSSPPSK IASMEIPNDD LKIEQVVGMG KGILLTWHYD PNMTCDYVIK
WCNSSRSEPC LMDWRKVPSN STETVIESDE FRPGIRYNFF LYGCRNQGYQ LLRSMIGYIE
ELAPIVAPNF TVEDTSADSI LVKWEDIPVE ELRGFLRGYL FYFGKGERDT SKMRVLESGR
SDIKVKNITD ISQKTLRIAD LQGKTSYHLV LRAYTDGGVG PEKSMYVVTK ENSVGLIIAI
LIPVAVAVIV GVVTSILCYR KREWIKETFY PDIPNPENCK ALQFQKSVCE GSSALKTLEM
NPCTPNNVEV LETRSAFPKI EDTEIISPVA ERPEDRSDAE PENHVVVSYC PPIIEEEIPN
PAADEAGGTA QVIYIDVQSM YQPQAKPEEE QENDPVGGAG YKPQMHLPIN STVEDIAAEE
DLDKTAGYRP QANVNTWNLV SPDSPRSIDS NSEIVSFGSP CSINSRQFLI PPKDEDSPKS
NGGGWSFTNF FQNKPND
