TNR11_HUMAN
ID TNR11_HUMAN Reviewed; 616 AA.
AC Q9Y6Q6; I4EC36; I4EC38; I4EC39; I7JE63; N0GVH0; Q59EP9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 11A;
DE AltName: Full=Osteoclast differentiation factor receptor;
DE Short=ODFR;
DE AltName: Full=Receptor activator of NF-KB;
DE AltName: CD_antigen=CD265;
DE Flags: Precursor;
GN Name=TNFRSF11A; Synonyms=RANK;
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=Dendritic cell;
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 RANK-E5A), SUBCELLULAR LOCATION
RP (ISOFORMS 1 AND RANK-E5A), AND ALTERNATIVE SPLICING.
RC TISSUE=Blood;
RX PubMed=23664977; DOI=10.1016/j.gene.2013.04.075;
RA Sirinian C., Papanastasiou A.D., Zarkadis I.K., Kalofonos H.P.;
RT "Alternative splicing generates a truncated isoform of human TNFRSF11A
RT (RANK) with an altered capacity to activate NF-kappaB.";
RL Gene 525:124-129(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 159-523 (ISOFORM 5), AND ALTERNATIVE SPLICING.
RC TISSUE=Blood;
RA Papanastasiou A.D., Sirinian C., Kalofonos H.P.;
RT "Alternative splicing generates multiple human TNFRSF11A (RANK) isoforms.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=9878548; DOI=10.1006/bbrc.1998.9788;
RA Nakagawa N., Kinosaki M., Yamaguchi K., Shima N., Yasuda H., Yano K.,
RA Morinaga T., Higashio K.;
RT "RANK is the essential signaling receptor for osteoclast differentiation
RT factor in osteoclastogenesis.";
RL Biochem. Biophys. Res. Commun. 253:395-400(1998).
RN [6]
RP INTERACTION WITH TRAF1; TRAF2; TRAF3; TRAF5 AND TRAF6.
RX PubMed=9774460; DOI=10.1074/jbc.273.43.28355;
RA Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.;
RT "The TRAF family of signal transducers mediates NF-kappaB activation by the
RT TRANCE receptor.";
RL J. Biol. Chem. 273:28355-28359(1998).
RN [7]
RP INTERACTION WITH GAB2.
RX PubMed=15750601; DOI=10.1038/nm1203;
RA Wada T., Nakashima T., Oliveira-dos-Santos A.J., Gasser J., Hara H.,
RA Schett G., Penninger J.M.;
RT "The molecular scaffold Gab2 is a crucial component of RANK signaling and
RT osteoclastogenesis.";
RL Nat. Med. 11:394-399(2005).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP VARIANT FEO LEU-LEU-CYS-ALA-LEU-LEU-21 INS, VARIANT PDB2
RP ALA-LEU-LEU-LEU-LEU-CYS-ALA-LEU-LEU-21 INS, AND VARIANT VAL-192.
RX PubMed=10615125; DOI=10.1038/71667;
RA Hughes A.E., Ralston S.H., Marken J., Bell C., MacPherson H.,
RA Wallace R.G.H., van Hul W., Whyte M.P., Nakatsuka K., Hovy L.,
RA Anderson D.M.;
RT "Mutations in TNFRSF11A, affecting the signal peptide of RANK, cause
RT familial expansile osteolysis.";
RL Nat. Genet. 24:45-48(2000).
RN [11]
RP VARIANTS OPTB7 ARG-53; CYS-129; GLY-170; ARG-175 AND SER-244.
RX PubMed=18606301; DOI=10.1016/j.ajhg.2008.06.015;
RA Guerrini M.M., Sobacchi C., Cassani B., Abinun M., Kilic S.S.,
RA Pangrazio A., Moratto D., Mazzolari E., Clayton-Smith J., Orchard P.,
RA Coxon F.P., Helfrich M.H., Crockett J.C., Mellis D., Vellodi A., Tezcan I.,
RA Notarangelo L.D., Rogers M.J., Vezzoni P., Villa A., Frattini A.;
RT "Human osteoclast-poor osteopetrosis with hypogammaglobulinemia due to
RT TNFRSF11A (RANK) mutations.";
RL Am. J. Hum. Genet. 83:64-76(2008).
CC -!- FUNCTION: Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-
CC mediated osteoclastogenesis. Involved in the regulation of interactions
CC between T-cells and dendritic cells. {ECO:0000269|PubMed:9878548}.
CC -!- SUBUNIT: Binds to the clefts between the subunits of the TNFSF11 ligand
CC trimer to form a heterohexamer (By similarity). Interacts with TRAF1,
CC TRAF2, TRAF3, TRAF5 and TRAF6. Interacts (via cytoplasmic domain) with
CC GAB2. {ECO:0000250, ECO:0000269|PubMed:15750601,
CC ECO:0000269|PubMed:9774460}.
CC -!- INTERACTION:
CC Q9Y6Q6; PRO_0000034515 [O14788]: TNFSF11; NbExp=9; IntAct=EBI-525675, EBI-15488409;
CC Q9Y6Q6; Q12933: TRAF2; NbExp=2; IntAct=EBI-525675, EBI-355744;
CC Q9Y6Q6-2; P00533: EGFR; NbExp=3; IntAct=EBI-20899422, EBI-297353;
CC Q9Y6Q6-2; Q12933: TRAF2; NbExp=5; IntAct=EBI-20899422, EBI-355744;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:23664977}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:23664977}.
CC -!- SUBCELLULAR LOCATION: [Isoform RANK-e5a]: Cell membrane
CC {ECO:0000269|PubMed:23664977}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:23664977}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9Y6Q6-1; Sequence=Displayed;
CC Name=2; Synonyms=delta7,8,9;
CC IsoId=Q9Y6Q6-2; Sequence=VSP_046901;
CC Name=3; Synonyms=delta8,9;
CC IsoId=Q9Y6Q6-3; Sequence=VSP_054180;
CC Name=4; Synonyms=delta9;
CC IsoId=Q9Y6Q6-4; Sequence=VSP_054181, VSP_054182;
CC Name=5; Synonyms=exon9a;
CC IsoId=Q9Y6Q6-5; Sequence=VSP_054183;
CC Name=RANK-e5a;
CC IsoId=Q9Y6Q6-6; Sequence=VSP_054179;
CC -!- TISSUE SPECIFICITY: Ubiquitous expression with high levels in skeletal
CC muscle, thymus, liver, colon, small intestine and adrenal gland.
CC -!- DISEASE: Familial expansile osteolysis (FEO) [MIM:174810]: Rare
CC autosomal dominant bone disorder characterized by focal areas of
CC increased bone remodeling. The osteolytic lesions develop usually in
CC the long bones during early adulthood. FEO is often associated with
CC early-onset deafness and loss of dentition.
CC {ECO:0000269|PubMed:10615125}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Paget disease of bone 2, early-onset (PDB2) [MIM:602080]: A
CC form of Paget disease, a disorder of bone remodeling characterized by
CC increased bone turnover affecting one or more sites throughout the
CC skeleton, primarily the axial skeleton. Osteoclastic overactivity
CC followed by compensatory osteoblastic activity leads to a structurally
CC disorganized mosaic of bone (woven bone), which is mechanically weaker,
CC larger, less compact, more vascular, and more susceptible to fracture
CC than normal adult lamellar bone. {ECO:0000269|PubMed:10615125}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Osteopetrosis, autosomal recessive 7 (OPTB7) [MIM:612301]: 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. OPTB7 is characterized by
CC paucity of osteoclasts, suggesting a molecular defect in osteoclast
CC development. OPTB7 is associated with hypogammaglobulinemia.
CC {ECO:0000269|PubMed:18606301}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform RANK-e5a]: Reduced ability to bind RANKL and to
CC activate NF-kappaB as compared to isoform 1. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92999.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF018253; AAB86809.1; -; mRNA.
DR EMBL; HF584702; CCQ44072.1; -; mRNA.
DR EMBL; HE647782; CCF23032.1; -; mRNA.
DR EMBL; HE649916; CCF55033.1; -; mRNA.
DR EMBL; HE649917; CCF55034.1; -; mRNA.
DR EMBL; HE659518; CCF77738.1; -; mRNA.
DR EMBL; AB209762; BAD92999.1; ALT_INIT; mRNA.
DR CCDS; CCDS11980.1; -. [Q9Y6Q6-1]
DR CCDS; CCDS59324.1; -. [Q9Y6Q6-2]
DR CCDS; CCDS74227.1; -. [Q9Y6Q6-4]
DR CCDS; CCDS74228.1; -. [Q9Y6Q6-3]
DR RefSeq; NP_001257878.1; NM_001270949.1. [Q9Y6Q6-4]
DR RefSeq; NP_001257879.1; NM_001270950.1. [Q9Y6Q6-3]
DR RefSeq; NP_001257880.1; NM_001270951.1. [Q9Y6Q6-2]
DR RefSeq; NP_001265197.1; NM_001278268.1. [Q9Y6Q6-6]
DR RefSeq; NP_003830.1; NM_003839.3. [Q9Y6Q6-1]
DR PDB; 1LB5; X-ray; 2.40 A; B=342-349.
DR PDBsum; 1LB5; -.
DR AlphaFoldDB; Q9Y6Q6; -.
DR SMR; Q9Y6Q6; -.
DR BioGRID; 114320; 15.
DR CORUM; Q9Y6Q6; -.
DR ELM; Q9Y6Q6; -.
DR IntAct; Q9Y6Q6; 7.
DR MINT; Q9Y6Q6; -.
DR STRING; 9606.ENSP00000465500; -.
DR DrugBank; DB05959; ENMD-1198.
DR GlyGen; Q9Y6Q6; 2 sites.
DR iPTMnet; Q9Y6Q6; -.
DR PhosphoSitePlus; Q9Y6Q6; -.
DR BioMuta; TNFRSF11A; -.
DR DMDM; 19924309; -.
DR jPOST; Q9Y6Q6; -.
DR MassIVE; Q9Y6Q6; -.
DR MaxQB; Q9Y6Q6; -.
DR PaxDb; Q9Y6Q6; -.
DR PeptideAtlas; Q9Y6Q6; -.
DR PRIDE; Q9Y6Q6; -.
DR ProteomicsDB; 86765; -. [Q9Y6Q6-1]
DR Antibodypedia; 4165; 812 antibodies from 43 providers.
DR DNASU; 8792; -.
DR Ensembl; ENST00000269485.11; ENSP00000269485.7; ENSG00000141655.17. [Q9Y6Q6-2]
DR Ensembl; ENST00000586569.3; ENSP00000465500.1; ENSG00000141655.17. [Q9Y6Q6-1]
DR Ensembl; ENST00000616710.4; ENSP00000479567.1; ENSG00000141655.17. [Q9Y6Q6-4]
DR Ensembl; ENST00000617039.4; ENSP00000482466.1; ENSG00000141655.17. [Q9Y6Q6-3]
DR GeneID; 8792; -.
DR KEGG; hsa:8792; -.
DR MANE-Select; ENST00000586569.3; ENSP00000465500.1; NM_003839.4; NP_003830.1.
DR UCSC; uc002lin.5; human. [Q9Y6Q6-1]
DR CTD; 8792; -.
DR DisGeNET; 8792; -.
DR GeneCards; TNFRSF11A; -.
DR HGNC; HGNC:11908; TNFRSF11A.
DR HPA; ENSG00000141655; Tissue enhanced (intestine, salivary gland).
DR MalaCards; TNFRSF11A; -.
DR MIM; 174810; phenotype.
DR MIM; 602080; phenotype.
DR MIM; 603499; gene.
DR MIM; 612301; phenotype.
DR neXtProt; NX_Q9Y6Q6; -.
DR OpenTargets; ENSG00000141655; -.
DR Orphanet; 391490; Adult-onset myasthenia gravis.
DR Orphanet; 1782; Dysosteosclerosis.
DR Orphanet; 85195; Familial expansile osteolysis.
DR Orphanet; 2801; Juvenile Paget disease.
DR Orphanet; 280110; NON RARE IN EUROPE: Paget disease of bone.
DR Orphanet; 178389; Osteopetrosis-hypogammaglobulinemia syndrome.
DR PharmGKB; PA36601; -.
DR VEuPathDB; HostDB:ENSG00000141655; -.
DR eggNOG; ENOG502RWJI; Eukaryota.
DR GeneTree; ENSGT00940000161211; -.
DR HOGENOM; CLU_052667_2_0_1; -.
DR InParanoid; Q9Y6Q6; -.
DR OMA; CTCGLNF; -.
DR OrthoDB; 1038336at2759; -.
DR PhylomeDB; Q9Y6Q6; -.
DR PathwayCommons; Q9Y6Q6; -.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR SignaLink; Q9Y6Q6; -.
DR SIGNOR; Q9Y6Q6; -.
DR BioGRID-ORCS; 8792; 5 hits in 1070 CRISPR screens.
DR ChiTaRS; TNFRSF11A; human.
DR GeneWiki; RANK; -.
DR GenomeRNAi; 8792; -.
DR Pharos; Q9Y6Q6; Tbio.
DR PRO; PR:Q9Y6Q6; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9Y6Q6; protein.
DR Bgee; ENSG00000141655; Expressed in parotid gland and 145 other tissues.
DR ExpressionAtlas; Q9Y6Q6; baseline and differential.
DR Genevisible; Q9Y6Q6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0019955; F:cytokine binding; IPI:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; ISS:BHF-UCL.
DR GO; GO:0002250; P:adaptive immune response; IMP:BHF-UCL.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0060086; P:circadian temperature homeostasis; ISS:BHF-UCL.
DR GO; GO:0048535; P:lymph node development; IBA:GO_Central.
DR GO; GO:0060749; P:mammary gland alveolus development; IBA:GO_Central.
DR GO; GO:0002548; P:monocyte chemotaxis; NAS:BHF-UCL.
DR GO; GO:0072674; P:multinuclear osteoclast differentiation; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IBA:GO_Central.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:BHF-UCL.
DR GO; GO:0045780; P:positive regulation of bone resorption; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0071848; P:positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling; IMP:BHF-UCL.
DR GO; GO:0071812; P:positive regulation of fever generation by positive regulation of prostaglandin secretion; ISS:BHF-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0034097; P:response to cytokine; IMP:BHF-UCL.
DR GO; GO:0070555; P:response to interleukin-1; ISS:BHF-UCL.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:BHF-UCL.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0071847; P:TNFSF11-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISS:BHF-UCL.
DR CDD; cd13411; TNFRSF11A; 1.
DR InterPro; IPR041648; RANK_CRD_2.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR022323; TNFR_11.
DR InterPro; IPR022361; TNFR_11A.
DR InterPro; IPR034040; TNFRSF11A_N.
DR Pfam; PF18278; RANK_CRD_2; 1.
DR Pfam; PF00020; TNFR_c6; 2.
DR PRINTS; PR01961; TNFACTORR11.
DR PRINTS; PR01974; TNFACTORR11A.
DR SMART; SM00208; TNFR; 4.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Deafness;
KW Disease variant; Disulfide bond; Glycoprotein; Membrane; Metal-binding;
KW Osteopetrosis; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Sodium; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..616
FT /note="Tumor necrosis factor receptor superfamily member
FT 11A"
FT /id="PRO_0000034585"
FT TOPO_DOM 30..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 34..68
FT /note="TNFR-Cys 1"
FT REPEAT 71..112
FT /note="TNFR-Cys 2"
FT REPEAT 114..151
FT /note="TNFR-Cys 3"
FT REPEAT 154..194
FT /note="TNFR-Cys 4"
FT REGION 468..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 47..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 50..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 71..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 92..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 114..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 124..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 133..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 154..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 175..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VAR_SEQ 143..157
FT /note="LQLNKDTVCKPCLAG -> C (in isoform RANK-e5a)"
FT /evidence="ECO:0000303|PubMed:23664977"
FT /id="VSP_054179"
FT VAR_SEQ 206..522
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_046901"
FT VAR_SEQ 244..522
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_054180"
FT VAR_SEQ 263
FT /note="S -> M (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_054181"
FT VAR_SEQ 264..616
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_054182"
FT VAR_SEQ 523..616
FT /note="GNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGAAAAAEPMGRPVQEET
FT LARRDSFAGNGPRFPDPCGGPEGLREPEKASRPVQEQGGAKA -> D (in isoform
FT 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_054183"
FT VARIANT 21
FT /note="L -> LALLLLCALL (in PDB2)"
FT /evidence="ECO:0000269|PubMed:10615125"
FT /id="VAR_011516"
FT VARIANT 21
FT /note="L -> LLLCALL (in FEO)"
FT /evidence="ECO:0000269|PubMed:10615125"
FT /id="VAR_011517"
FT VARIANT 53
FT /note="G -> R (in OPTB7; two patients with osteoclast-poor
FT osteopetrosis; dbSNP:rs121908659)"
FT /evidence="ECO:0000269|PubMed:18606301"
FT /id="VAR_046788"
FT VARIANT 129
FT /note="R -> C (in OPTB7; a patient with osteoclast-poor
FT osteopetrosis; dbSNP:rs121908657)"
FT /evidence="ECO:0000269|PubMed:18606301"
FT /id="VAR_046789"
FT VARIANT 141
FT /note="H -> Y (in dbSNP:rs35211496)"
FT /id="VAR_046790"
FT VARIANT 170
FT /note="R -> G (in OPTB7; two siblings with osteoclast-poor
FT osteopetrosis; dbSNP:rs121908655)"
FT /evidence="ECO:0000269|PubMed:18606301"
FT /id="VAR_046791"
FT VARIANT 175
FT /note="C -> R (in OPTB7; two patients with osteoclast-poor
FT osteopetrosis; dbSNP:rs121908656)"
FT /evidence="ECO:0000269|PubMed:18606301"
FT /id="VAR_046792"
FT VARIANT 192
FT /note="A -> V (in dbSNP:rs1805034)"
FT /evidence="ECO:0000269|PubMed:10615125"
FT /id="VAR_011518"
FT VARIANT 244
FT /note="A -> S (in OPTB7; one patient with osteoclast-poor
FT osteopetrosis; dbSNP:rs121908658)"
FT /evidence="ECO:0000269|PubMed:18606301"
FT /id="VAR_046793"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1LB5"
SQ SEQUENCE 616 AA; 66034 MW; E3DE9A7A08196F81 CRC64;
MAPRARRRRP LFALLLLCAL LARLQVALQI APPCTSEKHY EHLGRCCNKC EPGKYMSSKC
TTTSDSVCLP CGPDEYLDSW NEEDKCLLHK VCDTGKALVA VVAGNSTTPR RCACTAGYHW
SQDCECCRRN TECAPGLGAQ HPLQLNKDTV CKPCLAGYFS DAFSSTDKCR PWTNCTFLGK
RVEHHGTEKS DAVCSSSLPA RKPPNEPHVY LPGLIILLLF ASVALVAAII FGVCYRKKGK
ALTANLWHWI NEACGRLSGD KESSGDSCVS THTANFGQQG ACEGVLLLTL EEKTFPEDMC
YPDQGGVCQG TCVGGGPYAQ GEDARMLSLV SKTEIEEDSF RQMPTEDEYM DRPSQPTDQL
LFLTEPGSKS TPPFSEPLEV GENDSLSQCF TGTQSTVGSE SCNCTEPLCR TDWTPMSSEN
YLQKEVDSGH CPHWAASPSP NWADVCTGCR NPPGEDCEPL VGSPKRGPLP QCAYGMGLPP
EEEASRTEAR DQPEDGADGR LPSSARAGAG SGSSPGGQSP ASGNVTGNSN STFISSGQVM
NFKGDIIVVY VSQTSQEGAA AAAEPMGRPV QEETLARRDS FAGNGPRFPD PCGGPEGLRE
PEKASRPVQE QGGAKA
