TNF11_HUMAN
ID TNF11_HUMAN Reviewed; 317 AA.
AC O14788; O14723; Q96Q17; Q9P2Q3;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 11;
DE AltName: Full=Osteoclast differentiation factor;
DE Short=ODF;
DE AltName: Full=Osteoprotegerin ligand;
DE Short=OPGL;
DE AltName: Full=Receptor activator of nuclear factor kappa-B ligand;
DE Short=RANKL;
DE AltName: Full=TNF-related activation-induced cytokine;
DE Short=TRANCE;
DE AltName: CD_antigen=CD254;
DE Contains:
DE RecName: Full=Tumor necrosis factor ligand superfamily member 11, membrane form;
DE Contains:
DE RecName: Full=Tumor necrosis factor ligand superfamily member 11, soluble form;
GN Name=TNFSF11; Synonyms=OPGL, RANKL, TRANCE;
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=Bone marrow, and Peripheral blood;
RX PubMed=9367155; DOI=10.1038/36593;
RA Anderson D.M., Maraskovsky E., Billingsley W.L., Dougall W.C.,
RA Tometsko M.E., Roux E.R., Teepe M.C., DuBose R.F., Cosman D., Galibert L.;
RT "A homologue of the TNF receptor and its ligand enhance T-cell growth and
RT dendritic-cell function.";
RL Nature 390:175-179(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=9568710; DOI=10.1016/s0092-8674(00)81569-x;
RA Lacey D.L., Timms E., Tan H.-L., Kelley M.J., Dunstan C.R., Burgess T.,
RA Elliott R., Colombero A., Elliott G., Scully S., Hsu H., Sullivan J.,
RA Hawkins N., Davy E., Capparelli C., Eli A., Qian Y.-X., Kaufman S.,
RA Sarosi I., Shalhoub V., Senaldi G., Guo J., Delaney J., Boyle W.J.;
RT "Osteoprotegerin ligand is a cytokine that regulates osteoclast
RT differentiation and activation.";
RL Cell 93:165-176(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RA Ikeda T., Kuroyama H., Hirokawa K.;
RT "Determination of human RANKL isoforms.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
RX PubMed=10708588; DOI=10.1006/bbrc.2000.2314;
RA Nagai M., Kyakumoto S., Sato N.;
RT "Cancer cells responsible for humoral hypercalcemia express mRNA encoding a
RT secreted form of ODF/TRANCE that induces osteoclast formation.";
RL Biochem. Biophys. Res. Commun. 269:532-536(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-317.
RC TISSUE=Thymocyte;
RX PubMed=9312132; DOI=10.1074/jbc.272.40.25190;
RA Wong B.R., Rho J., Arron J., Robinson E., Orlinick J., Chao M.,
RA Kalachikov S., Cayani E., Bartlett F.S. III, Frankel W.N., Lee S.Y.,
RA Choi Y.;
RT "TRANCE is a novel ligand of the tumor necrosis factor receptor family that
RT activates c-Jun N-terminal kinase in T cells.";
RL J. Biol. Chem. 272:25190-25194(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 162-317 IN COMPLEX WITH TNFRSF11B,
RP FUNCTION, MUTAGENESIS OF ARG-223 AND LYS-257, AND INTERACTION WITH
RP TNFRSF11B.
RX PubMed=22664871; DOI=10.4049/jimmunol.1103387;
RA Luan X., Lu Q., Jiang Y., Zhang S., Wang Q., Yuan H., Zhao W., Wang J.,
RA Wang X.;
RT "Crystal structure of human RANKL complexed with its decoy receptor
RT osteoprotegerin.";
RL J. Immunol. 189:245-252(2012).
RN [8]
RP VARIANT OPTB2 LYS-199.
RX PubMed=17632511; DOI=10.1038/ng2076;
RA Sobacchi C., Frattini A., Guerrini M.M., Abinun M., Pangrazio A.,
RA Susani L., Bredius R., Mancini G., Cant A., Bishop N., Grabowski P.,
RA Del Fattore A., Messina C., Errigo G., Coxon F.P., Scott D.I., Teti A.,
RA Rogers M.J., Vezzoni P., Villa A., Helfrich M.H.;
RT "Osteoclast-poor human osteopetrosis due to mutations in the gene encoding
RT RANKL.";
RL Nat. Genet. 39:960-962(2007).
CC -!- FUNCTION: Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK.
CC Osteoclast differentiation and activation factor. Augments the ability
CC of dendritic cells to stimulate naive T-cell proliferation. May be an
CC important regulator of interactions between T-cells and dendritic cells
CC and may play a role in the regulation of the T-cell-dependent immune
CC response. May also play an important role in enhanced bone-resorption
CC in humoral hypercalcemia of malignancy (PubMed:22664871). Induces
CC osteoclastogenesis by activating multiple signaling pathways in
CC osteoclast precursor cells, chief among which is induction of long
CC lasting oscillations in the intracellular concentration of Ca (2+)
CC resulting in the activation of NFATC1, which translocates to the
CC nucleus and induces osteoclast-specific gene transcription to allow
CC differentiation of osteoclasts. During osteoclast differentiation, in a
CC TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and
CC mitochondrial ROS generation necessary for proper osteoclast generation
CC (By similarity). {ECO:0000250|UniProtKB:O35235,
CC ECO:0000269|PubMed:22664871}.
CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with TNFRSF11B
CC (PubMed:22664871). Interacts with TNFRSF11A. Interacts with FBN1 (via
CC N-terminal domain) in a Ca(+2)-dependent manner (By similarity).
CC Interacts with TNFAIP6 (via both Link and CUB domains).
CC {ECO:0000250|UniProtKB:O35235, ECO:0000269|PubMed:22664871}.
CC -!- INTERACTION:
CC O14788; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-7404021, EBI-2804156;
CC O14788; P98066: TNFAIP6; NbExp=4; IntAct=EBI-7404021, EBI-11700693;
CC O14788; O00300: TNFRSF11B; NbExp=3; IntAct=EBI-7404021, EBI-15481185;
CC O14788; O00526: UPK2; NbExp=3; IntAct=EBI-7404021, EBI-10179682;
CC PRO_0000034515; Q9Y6Q6: TNFRSF11A; NbExp=9; IntAct=EBI-15488409, EBI-525675;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type II
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type II
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member
CC 11, soluble form]: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O14788-1; Sequence=Displayed;
CC Name=2; Synonyms=SODF;
CC IsoId=O14788-2; Sequence=VSP_006447;
CC Name=3;
CC IsoId=O14788-3; Sequence=VSP_006446;
CC -!- TISSUE SPECIFICITY: Highest in the peripheral lymph nodes, weak in
CC spleen, peripheral blood Leukocytes, bone marrow, heart, placenta,
CC skeletal muscle, stomach and thyroid.
CC -!- INDUCTION: Up-regulated by T-cell receptor stimulation.
CC -!- PTM: The soluble form of isoform 1 derives from the membrane form by
CC proteolytic processing (By similarity). The cleavage may be catalyzed
CC by ADAM17. {ECO:0000250}.
CC -!- DISEASE: Osteopetrosis, autosomal recessive 2 (OPTB2) [MIM:259710]: A
CC rare genetic disease characterized by abnormally dense bone, due to
CC defective resorption of immature bone. Osteopetrosis occurs in two
CC forms: a severe autosomal recessive form occurring in utero, infancy,
CC or childhood, and a benign autosomal dominant form occurring in
CC adolescence or adulthood. Recessive osteopetrosis commonly manifests in
CC early infancy with macrocephaly, feeding difficulties, evolving
CC blindness and deafness, bone marrow failure, severe anemia, and
CC hepatosplenomegaly. Deafness and blindness are generally thought to
CC represent effects of pressure on nerves. OPTB2 is characterized by
CC paucity of osteoclasts, suggesting a molecular defect in osteoclast
CC development. {ECO:0000269|PubMed:17632511}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR EMBL; AF019047; AAB86811.1; -; mRNA.
DR EMBL; AF053712; AAC39731.1; -; mRNA.
DR EMBL; AB064269; BAB79694.1; -; mRNA.
DR EMBL; AB061227; BAB71768.1; -; mRNA.
DR EMBL; AB064270; BAB79695.1; -; mRNA.
DR EMBL; AB037599; BAA90488.1; -; mRNA.
DR EMBL; BC074823; AAH74823.1; -; mRNA.
DR EMBL; BC074890; AAH74890.1; -; mRNA.
DR EMBL; AF013171; AAC51762.1; -; mRNA.
DR CCDS; CCDS9384.1; -. [O14788-1]
DR CCDS; CCDS9385.1; -. [O14788-2]
DR RefSeq; NP_003692.1; NM_003701.3. [O14788-1]
DR RefSeq; NP_143026.1; NM_033012.3. [O14788-2]
DR RefSeq; XP_011533582.1; XM_011535280.2. [O14788-2]
DR RefSeq; XP_016876292.1; XM_017020803.1. [O14788-2]
DR PDB; 3URF; X-ray; 2.70 A; A=162-317.
DR PDB; 5BNQ; X-ray; 2.80 A; A=158-317.
DR PDBsum; 3URF; -.
DR PDBsum; 5BNQ; -.
DR AlphaFoldDB; O14788; -.
DR SMR; O14788; -.
DR BioGRID; 114160; 35.
DR IntAct; O14788; 25.
DR MINT; O14788; -.
DR STRING; 9606.ENSP00000381775; -.
DR BindingDB; O14788; -.
DR ChEMBL; CHEMBL2364162; -.
DR DrugBank; DB06511; AMGN-0007.
DR DrugBank; DB06643; Denosumab.
DR DrugBank; DB00480; Lenalidomide.
DR DrugBank; DB11582; Thiocolchicoside.
DR DrugCentral; O14788; -.
DR MoonDB; O14788; Predicted.
DR GlyGen; O14788; 2 sites.
DR iPTMnet; O14788; -.
DR PhosphoSitePlus; O14788; -.
DR BioMuta; TNFSF11; -.
DR MassIVE; O14788; -.
DR PaxDb; O14788; -.
DR PeptideAtlas; O14788; -.
DR PRIDE; O14788; -.
DR ProteomicsDB; 48237; -. [O14788-1]
DR ProteomicsDB; 48238; -. [O14788-2]
DR ProteomicsDB; 48239; -. [O14788-3]
DR ABCD; O14788; 79 sequenced antibodies.
DR Antibodypedia; 3366; 1186 antibodies from 49 providers.
DR DNASU; 8600; -.
DR Ensembl; ENST00000239849.8; ENSP00000239849.7; ENSG00000120659.15. [O14788-3]
DR Ensembl; ENST00000358545.6; ENSP00000351347.2; ENSG00000120659.15. [O14788-2]
DR Ensembl; ENST00000398795.7; ENSP00000381775.3; ENSG00000120659.15. [O14788-1]
DR Ensembl; ENST00000405262.6; ENSP00000384042.2; ENSG00000120659.15. [O14788-2]
DR Ensembl; ENST00000544862.5; ENSP00000444913.1; ENSG00000120659.15. [O14788-2]
DR GeneID; 8600; -.
DR KEGG; hsa:8600; -.
DR MANE-Select; ENST00000398795.7; ENSP00000381775.3; NM_003701.4; NP_003692.1.
DR UCSC; uc058wqy.1; human. [O14788-1]
DR CTD; 8600; -.
DR DisGeNET; 8600; -.
DR GeneCards; TNFSF11; -.
DR HGNC; HGNC:11926; TNFSF11.
DR HPA; ENSG00000120659; Tissue enhanced (breast, liver, lymphoid tissue).
DR MalaCards; TNFSF11; -.
DR MIM; 259710; phenotype.
DR MIM; 602642; gene.
DR neXtProt; NX_O14788; -.
DR OpenTargets; ENSG00000120659; -.
DR Orphanet; 667; Autosomal recessive malignant osteopetrosis.
DR PharmGKB; PA36619; -.
DR VEuPathDB; HostDB:ENSG00000120659; -.
DR eggNOG; ENOG502R8MX; Eukaryota.
DR GeneTree; ENSGT01050000244878; -.
DR HOGENOM; CLU_070352_0_0_1; -.
DR InParanoid; O14788; -.
DR OMA; HIVRSQH; -.
DR OrthoDB; 24858at2759; -.
DR PhylomeDB; O14788; -.
DR TreeFam; TF332169; -.
DR PathwayCommons; O14788; -.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR SignaLink; O14788; -.
DR SIGNOR; O14788; -.
DR BioGRID-ORCS; 8600; 5 hits in 1071 CRISPR screens.
DR GeneWiki; RANKL; -.
DR GenomeRNAi; 8600; -.
DR Pharos; O14788; Tclin.
DR PRO; PR:O14788; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; O14788; protein.
DR Bgee; ENSG00000120659; Expressed in tibia and 72 other tissues.
DR ExpressionAtlas; O14788; baseline and differential.
DR Genevisible; O14788; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; NAS:UniProtKB.
DR GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; IC:BHF-UCL.
DR GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0002548; P:monocyte chemotaxis; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IDA:BHF-UCL.
DR GO; GO:0002158; P:osteoclast proliferation; IEA:Ensembl.
DR GO; GO:0038001; P:paracrine signaling; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IDA:UniProtKB.
DR GO; GO:0051466; P:positive regulation of corticotropin-releasing hormone secretion; ISS:BHF-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:BHF-UCL.
DR GO; GO:0071848; P:positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling; IDA:BHF-UCL.
DR GO; GO:0071812; P:positive regulation of fever generation by positive regulation of prostaglandin secretion; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IDA:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR GO; GO:2001206; P:positive regulation of osteoclast development; IEA:Ensembl.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0050870; P:positive regulation of T cell activation; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR GO; GO:1904616; P:regulation of actin binding; IEA:Ensembl.
DR GO; GO:0071847; P:TNFSF11-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0044691; P:tooth eruption; IEA:Ensembl.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISS:BHF-UCL.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR017355; TNF_ligand_10/11.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00229; TNF; 1.
DR PIRSF; PIRSF038013; TNF10_TNF11; 1.
DR SMART; SM00207; TNF; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytokine; Cytoplasm;
KW Developmental protein; Differentiation; Disease variant; Glycoprotein;
KW Membrane; Osteopetrosis; Receptor; Reference proteome; Secreted;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="Tumor necrosis factor ligand superfamily member 11,
FT membrane form"
FT /id="PRO_0000034514"
FT CHAIN 140..317
FT /note="Tumor necrosis factor ligand superfamily member 11,
FT soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034515"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 139..140
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10708588, ECO:0000303|Ref.3"
FT /id="VSP_006447"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_006446"
FT VARIANT 199
FT /note="M -> K (in OPTB2; dbSNP:rs121909072)"
FT /evidence="ECO:0000269|PubMed:17632511"
FT /id="VAR_037424"
FT MUTAGEN 223
FT /note="R->A: Reduces affinity for TNFRSF11B."
FT /evidence="ECO:0000269|PubMed:22664871"
FT MUTAGEN 257
FT /note="K->A: Reduces affinity for TNFRSF11B."
FT /evidence="ECO:0000269|PubMed:22664871"
FT CONFLICT 194
FT /note="A -> G (in Ref. 6; AAC51762)"
FT /evidence="ECO:0000305"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3URF"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5BNQ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:5BNQ"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3URF"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3URF"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:3URF"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3URF"
FT STRAND 212..225
FT /evidence="ECO:0007829|PDB:3URF"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3URF"
FT STRAND 235..248
FT /evidence="ECO:0007829|PDB:3URF"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:3URF"
FT STRAND 269..283
FT /evidence="ECO:0007829|PDB:3URF"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:3URF"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:3URF"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:3URF"
FT STRAND 306..314
FT /evidence="ECO:0007829|PDB:3URF"
SQ SEQUENCE 317 AA; 35478 MW; 766176446348097F CRC64;
MRRASRDYTK YLRGSEEMGG GPGAPHEGPL HAPPPPAPHQ PPAASRSMFV ALLGLGLGQV
VCSVALFFYF RAQMDPNRIS EDGTHCIYRI LRLHENADFQ DTTLESQDTK LIPDSCRRIK
QAFQGAVQKE LQHIVGSQHI RAEKAMVDGS WLDLAKRSKL EAQPFAHLTI NATDIPSGSH
KVSLSSWYHD RGWAKISNMT FSNGKLIVNQ DGFYYLYANI CFRHHETSGD LATEYLQLMV
YVTKTSIKIP SSHTLMKGGS TKYWSGNSEF HFYSINVGGF FKLRSGEEIS IEVSNPSLLD
PDQDATYFGA FKVRDID
