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 28-JAN-2026, entry version 216. 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 STWS1 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 1 (STWS1) [MIM:601559]: A form of CC Stuve-Wiedemann syndrome, an autosomal recessive disease characterized CC by 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="https://atlasgeneticsoncology.org/gene/410/LIFR"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001127671.2. [P42702-1] DR RefSeq; NP_001351226.1; NM_001364297.2. [P42702-1] DR RefSeq; NP_002301.1; NM_002310.6. [P42702-1] DR RefSeq; XP_011512344.1; XM_011514042.4. [P42702-1] DR RefSeq; XP_016864952.1; XM_017009463.2. [P42702-1] DR PDB; 3E0G; X-ray; 3.10 A; A=52-534. DR PDB; 8D6A; EM; 3.54 A; B=45-833. DR PDB; 8D74; EM; 3.03 A; B=45-833. DR PDB; 8D7R; EM; 3.90 A; B=45-833. DR PDB; 8V29; EM; 3.99 A; C=45-833. DR PDB; 8V2A; EM; 3.59 A; C=45-833. DR PDBsum; 3E0G; -. DR PDBsum; 8D6A; -. DR PDBsum; 8D74; -. DR PDBsum; 8D7R; -. DR PDBsum; 8V29; -. DR PDBsum; 8V2A; -. DR AlphaFoldDB; P42702; -. DR EMDB; EMD-27221; -. DR EMDB; EMD-27227; -. DR EMDB; EMD-27229; -. DR EMDB; EMD-27231; -. DR EMDB; EMD-42902; -. DR EMDB; EMD-42903; -. DR SMR; P42702; -. DR BioGRID; 110165; 49. DR CORUM; P42702; -. DR DIP; DIP-5770N; -. DR FunCoup; P42702; 741. DR IntAct; P42702; 32. DR MINT; P42702; -. DR STRING; 9606.ENSP00000398368; -. DR GlyCosmos; P42702; 19 sites, No reported glycans. DR GlyGen; P42702; 22 sites, 10 N-linked glycans (11 sites), 2 O-linked glycans (3 sites). DR iPTMnet; P42702; -. DR PhosphoSitePlus; P42702; -. DR SwissPalm; P42702; -. DR BioMuta; LIFR; -. DR DMDM; 1170784; -. DR jPOST; P42702; -. DR MassIVE; P42702; -. DR PaxDb; 9606-ENSP00000263409; -. DR PeptideAtlas; P42702; -. DR ProteomicsDB; 55546; -. [P42702-1] DR Pumba; P42702; -. DR Antibodypedia; 4137; 461 antibodies from 31 providers. DR DNASU; 3977; -. DR Ensembl; ENST00000263409.8; ENSP00000263409.4; ENSG00000113594.11. DR Ensembl; ENST00000453190.7; ENSP00000398368.2; ENSG00000113594.11. 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 AGR; HGNC:6597; -. DR ClinPGx; PA30371; -. 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 OpenTargets; ENSG00000113594; -. DR Orphanet; 3206; Stueve-Wiedemann syndrome. DR VEuPathDB; HostDB:ENSG00000113594; -. DR eggNOG; ENOG502QQF6; Eukaryota. DR GeneTree; ENSGT00940000155776; -. DR HOGENOM; CLU_283805_0_0_1; -. DR InParanoid; P42702; -. DR OMA; FFLYGCK; -. DR OrthoDB; 6382334at2759; -. DR PAN-GO; P42702; 8 GO annotations based on evolutionary models. DR PhylomeDB; P42702; -. 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 Agora; ENSG00000113594; -. DR BioGRID-ORCS; 3977; 17 hits in 1164 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 188 other cell types or tissues. DR ExpressionAtlas; P42702; baseline and differential. 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: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:MGI. DR GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL. DR CDD; cd00063; FN3; 3. DR FunFam; 2.60.40.10:FF:000578; Leukemia inhibitory factor receptor; 1. DR FunFam; 2.60.40.10:FF:000607; Leukemia inhibitory factor receptor; 1. DR FunFam; 2.60.40.10:FF:000657; Leukemia inhibitory factor receptor; 1. DR FunFam; 2.60.40.10:FF:000738; Leukemia inhibitory factor receptor; 1. DR FunFam; 2.60.40.10:FF:000808; Leukemia inhibitory factor receptor; 1. DR FunFam; 2.60.40.10:FF:001265; Leukemia inhibitory factor receptor; 1. DR FunFam; 2.60.40.10:FF:001011; leukemia inhibitory factor receptor; 1. DR FunFam; 2.60.40.10:FF:001124; leukemia inhibitory factor receptor; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR048497; LIF-R-like_Ig-like. DR InterPro; IPR040817; LIFR_D2. DR InterPro; IPR040901; LIFR_N. DR InterPro; IPR050379; Type-I_Cytokine_Rcpt. DR PANTHER; PTHR23036; CYTOKINE RECEPTOR; 1. DR PANTHER; PTHR23036:SF105; LEUKEMIA INHIBITORY FACTOR RECEPTOR; 1. DR Pfam; PF00041; fn3; 1. DR Pfam; PF21177; LIF-R_Ig-like; 1. DR Pfam; PF17971; LIFR_D2; 1. DR Pfam; PF25552; LIFR_D4; 1. DR Pfam; PF18207; LIFR_N; 1. DR SMART; SM00060; FN3; 5. DR SUPFAM; SSF49265; Fibronectin type III; 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; Proteomics identification; Receptor; KW Reference proteome; Repeat; Secreted; Signal; Transmembrane; KW 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 1086..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 STWS1)" 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 141..147 FT /evidence="ECO:0007829|PDB:8D74" FT TURN 148..151 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:8D74" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 169..178 FT /evidence="ECO:0007829|PDB:8D74" FT TURN 179..181 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 186..192 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 201..206 FT /evidence="ECO:0007829|PDB:8D74" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 216..225 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:3E0G" FT STRAND 257..262 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 267..271 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 277..284 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 297..301 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 312..320 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 322..330 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 337..345 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 348..354 FT /evidence="ECO:0007829|PDB:8D74" FT HELIX 363..365 FT /evidence="ECO:0007829|PDB:3E0G" FT STRAND 368..376 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 393..398 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 405..413 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 418..426 FT /evidence="ECO:0007829|PDB:8D74" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 437..440 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 445..448 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 452..454 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 464..471 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 477..484 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 489..491 FT /evidence="ECO:0007829|PDB:8D74" FT STRAND 501..504 FT /evidence="ECO:0007829|PDB:3E0G" FT STRAND 506..510 FT /evidence="ECO:0007829|PDB:3E0G" FT STRAND 513..516 FT /evidence="ECO:0007829|PDB:8D74" 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 //