ID E2DGP8_DANRE Unreviewed; 431 AA. AC E2DGP8; A0A8M1NXA9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 02-SEP-2026, entry version 102. DE SubName: Full=Nerve growth factor recptor {ECO:0000313|EMBL:ADN85513.1}; GN Name=ngfrb {ECO:0000313|ZFIN:ZDB-GENE-070606-2}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:ADN85513.1}; RN [1] {ECO:0000313|EMBL:ADN85513.1} RP NUCLEOTIDE SEQUENCE. RA Han H.W., Chu C.Y., Cheng C.H., Chen G.D., Huang C.J.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00206}. 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; GQ983383; ADN85513.1; -; mRNA. DR RefSeq; NP_001185589.1; NM_001198660.1. DR AlphaFoldDB; E2DGP8; -. DR STRING; 7955.ENSDARP00000126756; -. DR GlyGen; E2DGP8; 1 site. DR PaxDb; 7955-ENSDARP00000126756; -. DR PeptideAtlas; E2DGP8; -. DR GeneID; 564338; -. DR KEGG; dre:564338; -. DR AGR; ZFIN:ZDB-GENE-070606-2; -. DR CTD; 564338; -. DR ZFIN; ZDB-GENE-070606-2; ngfrb. DR eggNOG; ENOG502QWPN; Eukaryota. DR GeneTree; ENSGT00730000110974; -. DR OMA; TMDEEPC; -. DR OrthoDB; 10048028at2759; -. DR Reactome; R-DRE-193634; Axonal growth inhibition (RHOA activation). DR Reactome; R-DRE-193692; Regulated proteolysis of p75NTR. DR Reactome; R-DRE-205017; NFG and proNGF binds to p75NTR. DR Reactome; R-DRE-209543; p75NTR recruits signalling complexes. DR Reactome; R-DRE-209560; NF-kB is activated and signals survival. DR Reactome; R-DRE-209563; Axonal growth stimulation. DR Bgee; ENSDARG00000089223; Expressed in spleen and 14 other cell types or tissues. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015026; F:coreceptor activity; IBA:GO_Central. DR GO; GO:0005035; F:death receptor activity; IBA:GO_Central. DR GO; GO:0048406; F:nerve growth factor binding; IBA:GO_Central. DR GO; GO:0001822; P:kidney development; IMP:ZFIN. DR GO; GO:0048916; P:posterior lateral line development; IMP:ZFIN. DR GO; GO:0048922; P:posterior lateral line neuromast deposition; IMP:ZFIN. DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central. DR CDD; cd08311; Death_p75NR; 1. DR CDD; cd13416; TNFRSF16; 1. DR FunFam; 1.10.533.10:FF:000123; Nerve growth factor receptor b; 1. DR FunFam; 2.10.50.10:FF:000012; tumor necrosis factor receptor superfamily member 16; 1. DR FunFam; 2.10.50.10:FF:000013; Tumor necrosis factor receptor superfamily member 16; 1. DR Gene3D; 6.10.250.1780; -; 1. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR000488; Death_dom. DR InterPro; IPR052302; Neurotrophin_rcpt-DD. DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg. DR InterPro; IPR041448; TNFR16_TM. DR InterPro; IPR022325; TNFR_16. DR InterPro; IPR034046; TNFRSF16_N. DR PANTHER; PTHR46605; TUMOR NECROSIS FACTOR RECEPTOR; 1. DR PANTHER; PTHR46605:SF3; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 16; 1. DR Pfam; PF00531; Death; 1. DR Pfam; PF18422; TNFR_16_TM; 1. DR Pfam; PF00020; TNFR_c6; 3. DR PRINTS; PR01966; TNFACTORR16. DR SMART; SM00005; DEATH; 1. DR SMART; SM00208; TNFR; 4. DR SUPFAM; SSF47986; DEATH domain; 1. DR SUPFAM; SSF57586; TNF receptor-like; 3. DR PROSITE; PS50017; DEATH_DOMAIN; 1. DR PROSITE; PS00652; TNFR_NGFR_1; 2. DR PROSITE; PS50050; TNFR_NGFR_2; 4. PE 2: Evidence at transcript level; KW Apoptosis {ECO:0000256|ARBA:ARBA00022703}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00206}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1..16 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 17..431 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5015088710" FT TRANSMEM 248..268 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 20..53 FT /note="TNFR-Cys" FT /evidence="ECO:0000259|PROSITE:PS50050" FT REPEAT 20..53 FT /note="TNFR-Cys" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DOMAIN 55..96 FT /note="TNFR-Cys" FT /evidence="ECO:0000259|PROSITE:PS50050" FT REPEAT 55..96 FT /note="TNFR-Cys" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DOMAIN 97..135 FT /note="TNFR-Cys" FT /evidence="ECO:0000259|PROSITE:PS50050" FT REPEAT 97..135 FT /note="TNFR-Cys" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DOMAIN 137..177 FT /note="TNFR-Cys" FT /evidence="ECO:0000259|PROSITE:PS50050" FT REPEAT 137..177 FT /note="TNFR-Cys" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DOMAIN 362..421 FT /note="Death" FT /evidence="ECO:0000259|PROSITE:PS50017" FT REGION 183..203 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 280..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 189..199 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 280..294 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 304..315 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 33..46 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DISULFID 75..88 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DISULFID 78..96 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DISULFID 114..127 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DISULFID 117..135 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DISULFID 138..153 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DISULFID 156..169 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" FT DISULFID 159..177 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206" SQ SEQUENCE 431 AA; 46601 MW; 3C9CB77DD894EA0F CRC64; MFTVTVVFLL VGEALSSRDT CPSGAFTTRG ECCKQCQPGE GMVKPCGATQ TVCEPCLDSE TFSENFSHKD KCLPCTQCSE LMRMLTPCTD ANDALCVCDY GFFLNQLSGR CEACTVCPVG QGVQVPCNFE RDTVCEKCED DTYSDQDTSF DPCLPCTVCD QPEMEVKSCT PVSDAVCQDF DAPNSSPSPS APPPTPYFTP SPSIHKFSSP GPSVVSYTEK LLPDNPTESV TTTDPGQKRL HGLSDNLIPI YTSILAAVLL GLVAFIIFKR WNSCKQNKQA NNRACSANPS QTPSPEGEKL HSDSGISVDS QSLQDGQGPP HTVVKIDGGS ALSLPLHTRE EVEKLLNRTN EGEESAANEE TDWCSLAGLL GYKEEHIANF KQEERPIQAL LSHWASQDSA NIDTLCTALK KINREDIAQS IIVKPTATSA V //