TNR16_CHICK
ID TNR16_CHICK Reviewed; 416 AA.
AC P18519;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 16;
DE AltName: Full=Gp80-LNGFR;
DE AltName: Full=Low affinity neurotrophin receptor p75NTR;
DE AltName: Full=Low-affinity nerve growth factor receptor;
DE Short=NGF receptor;
DE AltName: Full=p75 ICD;
DE Flags: Precursor;
GN Name=NGFR; Synonyms=TNFRSF16;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=2560385; DOI=10.1016/0896-6273(89)90179-7;
RA Large T.H., Weskamp G., Helder J.C., Radeke M.J., Misko T.P., Shooter E.M.,
RA Reichardt L.F.;
RT "Structure and developmental expression of the nerve growth factor receptor
RT in the chicken central nervous system.";
RL Neuron 2:1123-1134(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-416.
RX PubMed=2154393; DOI=10.1016/0012-1606(90)90255-h;
RA Heuer J.G., Fatemie-Nainie S., Wheeler E.F., Bothwell M.;
RT "Structure and developmental expression of the chicken NGF receptor.";
RL Dev. Biol. 137:287-304(1990).
CC -!- FUNCTION: Low affinity receptor which can bind to NGF, BDNF, NTF3, and
CC NTF4. Forms a heterodimeric receptor with SORCS2 that binds the
CC precursor forms of NGF, BDNF and NTF3 with high affinity, and has much
CC lower affinity for mature NGF and BDNF (By similarity). Plays an
CC important role in differentiation and survival of specific neuronal
CC populations during development (By similarity). Can mediate cell
CC survival as well as cell death of neural cells. Plays a role in the
CC inactivation of RHOA (By similarity). Necessary for the circadian
CC oscillation of clock genes in the suprachiasmatic nucleus (SCmgetaN) of
CC the brain and in liver and of the genes involved in glucose and lipid
CC metabolism in the liver (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P08138, ECO:0000250|UniProtKB:Q9Z0W1}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Heterodimer with
CC SORCS2. The extracellular domains of the heterodimer bind NGF (By
CC similarity). {ECO:0000250|UniProtKB:P07174,
CC ECO:0000250|UniProtKB:P08138}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Z0W1};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9Z0W1}.
CC Perikaryon {ECO:0000250|UniProtKB:Q9Z0W1}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9Z0W1}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q9Z0W1}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic dorsal root ganglion and
CC retina. {ECO:0000269|PubMed:2560385}.
CC -!- PTM: N- and O-glycosylated.
CC -!- PTM: Phosphorylated on serine residues.
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 PIR; JN0006; JN0006.
DR AlphaFoldDB; P18519; -.
DR SMR; P18519; -.
DR STRING; 9031.ENSGALP00000041297; -.
DR iPTMnet; P18519; -.
DR PaxDb; P18519; -.
DR Ensembl; ENSGALT00000046359; ENSGALP00000046489; ENSGALG00000035950.
DR VEuPathDB; HostDB:geneid_425805; -.
DR eggNOG; ENOG502QWPN; Eukaryota.
DR GeneTree; ENSGT00730000110974; -.
DR InParanoid; P18519; -.
DR OMA; GECCMEC; -.
DR PhylomeDB; P18519; -.
DR PRO; PR:P18519; -.
DR Proteomes; UP000000539; Chromosome 27.
DR Bgee; ENSGALG00000035950; Expressed in spleen and 6 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0043121; F:neurotrophin binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd13416; TNFRSF16; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR041448; TNFR16_TM.
DR InterPro; IPR022325; TNFR_16.
DR InterPro; IPR034046; TNFRSF16_N.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF18422; TNFR_16_TM; 1.
DR Pfam; PF00020; TNFR_c6; 2.
DR PRINTS; PR01966; TNFACTORR16.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00208; TNFR; 4.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00652; TNFR_NGFR_1; 3.
DR PROSITE; PS50050; TNFR_NGFR_2; 3.
PE 2: Evidence at transcript level;
KW Apoptosis; Biological rhythms; Cell membrane; Cell projection;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Membrane; Neurogenesis; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..416
FT /note="Tumor necrosis factor receptor superfamily member
FT 16"
FT /id="PRO_0000034594"
FT TOPO_DOM 29..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 23..57
FT /note="TNFR-Cys 1"
FT REPEAT 58..99
FT /note="TNFR-Cys 2"
FT REPEAT 100..138
FT /note="TNFR-Cys 3"
FT REPEAT 140..180
FT /note="TNFR-Cys 4"
FT DOMAIN 333..410
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 270..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 36..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 39..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 59..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 78..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 81..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 101..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 117..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 120..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 141..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 159..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 162..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT CONFLICT 36
FT /note="C -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="T -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="N -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="K -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 44654 MW; 6BCEAAB54F4D2D56 CRC64;
MAGFVPLLLL LLPAGPTWGS KEKCLTKMYT TSGECCKACN LGEGVVQPCG VNQTVCEPCL
DSVTYSDTVS ATEPCKPCTQ CVGLHSMSAP CVESDDAVCR CAYGYFQDEL SGSCKECSIC
EVGFGLMFPC RDSQDTVCEE CPEGTFSDEA NFVDPCLPCT ICEENEVMVK ECTATSDAEC
RDLHPRWTTH TPSLAGSDSP EPITRDPFNT EGMATTLADI VTTVMGSSQP VVSRGTADNL
IPVYCSILAA VVVGLVAYIA FKRWNSCKQN KQGANNRPVN QTPSPEGEKL HSDSGISVDS
QSLHDQQPPN QSTQGPAPKG DGSLYASLPP SKQEEVEKLL SSSAEETWRQ LAGELGYKED
LIDCFTREES PARALLADWS AKETATLDAL LVALRKIQRG DIAESLYSES TATSPV
