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Death domain-containing membrane protein NRADD (Neurotrophin receptor homolog-2) (NRH2) (Neurotrophin receptor-alike death domain protein) (P75-like apoptosis-inducing death domain protein) (PLAIDD)

 NRADD_RAT               Reviewed;         228 AA.
Q8K5A9; G3V8U7; Q8K5A8;
25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
25-JAN-2012, sequence version 2.
22-NOV-2017, entry version 88.
RecName: Full=Death domain-containing membrane protein NRADD;
AltName: Full=Neurotrophin receptor homolog-2;
Short=NRH2;
AltName: Full=Neurotrophin receptor-alike death domain protein;
AltName: Full=P75-like apoptosis-inducing death domain protein;
Short=PLAIDD;
Name=Nradd; Synonyms=Nrh2, Plaidd;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION
WITH NGFR, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Embryonic brain;
PubMed=12095158; DOI=10.1385/NMM:1:3:153;
Frankowski H., Castro-Obregon S., del Rio G., Rao R.V., Bredesen D.E.;
"PLAIDD, a type II death domain protein that interacts with p75
neurotrophin receptor.";
NeuroMolecular Med. 1:153-170(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
PubMed=12728256; DOI=10.1038/sj.cdd.4401208;
Wang X., Shao Z., Zetoune F.S., Zeidler M.G., Gowrishankar K.,
Vincenz C.;
"NRADD, a novel membrane protein with a death domain involved in
mediating apoptosis in response to ER stress.";
Cell Death Differ. 10:580-591(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, AND INTERACTION WITH NGFR AND SORT1.
PubMed=19407813; DOI=10.1038/emboj.2009.118;
Kim T., Hempstead B.L.;
"NRH2 is a trafficking switch to regulate sortilin localization and
permit proneurotrophin-induced cell death.";
EMBO J. 28:1612-1623(2009).
-!- FUNCTION: Modulates NTRK1 signaling. Can activate several
intracellular signaling pathways, leading to activation of JUN.
Promotes translocation of SORT1 to the cell membrane, and thereby
hinders lysosomal degradation of SOTR1 and promotes its
interaction with NGFR (By similarity). Both isoform 1 and isoform
2 promote apoptosis. {ECO:0000250, ECO:0000269|PubMed:12095158,
ECO:0000269|PubMed:19407813}.
-!- SUBUNIT: Interacts with NTRK1 (By similarity). Isoform 1 and
isoform 2 interact with NGFR. Interacts with SORT1. {ECO:0000250,
ECO:0000269|PubMed:12095158, ECO:0000269|PubMed:19407813}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12095158};
Single-pass type III membrane protein
{ECO:0000269|PubMed:12095158}. Nucleus {ECO:0000250}.
Note=Proteolytic processing gives rise to an intracellular domain
that translocates to the nucleus. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=Q8K5A9-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=Q8K5A9-2; Sequence=VSP_042237;
-!- TISSUE SPECIFICITY: Detected in embryo, including embryonic brain.
Detected at very low levels in adult testis, spleen, thymus and
lung. {ECO:0000269|PubMed:12095158}.
-!- DEVELOPMENTAL STAGE: Highly expressed in embryo. Expressed at very
low levels in adult. {ECO:0000269|PubMed:12095158}.
-!- PTM: Isoform 1 is N-glycosylated. Isoform 2 is not N-glycosylated.
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EMBL; AF497263; AAM28824.1; -; mRNA.
EMBL; AF497264; AAM28825.1; -; mRNA.
EMBL; AF534395; AAN05632.1; -; mRNA.
EMBL; CH473954; EDL77074.1; -; Genomic_DNA.
RefSeq; NP_640352.1; NM_139259.2.
RefSeq; XP_006243983.1; XM_006243921.2. [Q8K5A9-2]
UniGene; Rn.40242; -.
SMR; Q8K5A9; -.
IntAct; Q8K5A9; 2.
MINT; MINT-7290480; -.
STRING; 10116.ENSRNOP00000028416; -.
iPTMnet; Q8K5A9; -.
PhosphoSitePlus; Q8K5A9; -.
PaxDb; Q8K5A9; -.
PRIDE; Q8K5A9; -.
Ensembl; ENSRNOT00000028416; ENSRNOP00000028416; ENSRNOG00000020936. [Q8K5A9-1]
GeneID; 246143; -.
KEGG; rno:246143; -.
UCSC; RGD:708524; rat. [Q8K5A9-1]
CTD; 67169; -.
RGD; 708524; Nradd.
eggNOG; ENOG410J99A; Eukaryota.
eggNOG; ENOG4111D5W; LUCA.
GeneTree; ENSGT00730000110974; -.
HOGENOM; HOG000147886; -.
HOVERGEN; HBG071107; -.
InParanoid; Q8K5A9; -.
OMA; AFKCWRS; -.
OrthoDB; EOG091G0QZB; -.
PhylomeDB; Q8K5A9; -.
TreeFam; TF106466; -.
PRO; PR:Q8K5A9; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000020936; -.
Genevisible; Q8K5A9; RN.
GO; GO:0044298; C:cell body membrane; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0030027; C:lamellipodium; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0032589; C:neuron projection membrane; IDA:RGD.
GO; GO:0005641; C:nuclear envelope lumen; ISO:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0005166; F:neurotrophin p75 receptor binding; IPI:RGD.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; IBA:GO_Central.
GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0001701; P:in utero embryonic development; IEP:RGD.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0010942; P:positive regulation of cell death; IDA:RGD.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
Pfam; PF00531; Death; 1.
SMART; SM00005; DEATH; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Cell membrane; Complete proteome;
Glycoprotein; Membrane; Nucleus; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 228 Death domain-containing membrane protein
NRADD.
/FTId=PRO_0000415384.
TOPO_DOM 1 52 Extracellular. {ECO:0000255}.
TRANSMEM 53 73 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 74 228 Cytoplasmic. {ECO:0000255}.
DOMAIN 143 222 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
COMPBIAS 139 142 Poly-Gln.
CARBOHYD 4 4 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 13 61 Missing (in isoform 2).
{ECO:0000303|PubMed:12095158}.
/FTId=VSP_042237.
CONFLICT 159 159 Q -> R (in Ref. 1; AAM28824/AAM28825 and
2; AAN05632). {ECO:0000305}.
SEQUENCE 228 AA; 24400 MW; 8B9B243656DCC525 CRC64;
MLHNVSKGVV YSDTALKGQD GDREGMWVGA GGALAPNTSS LFPPEPPGAS SNIIPVYCAL
LATVVLGLLA YVAFKCWRSR KQRQQLAKAR TVELGDPDRD QRHGDSSVFV DSPHGLEPCI
PSQGPHADLG CRLYLHIPQQ QQEEVQRLLI LGEPAKGWQG LAGQLGYQAE AVETMACDQD
PAYALLRDWA AQEGSGATLR VLEDALTAIG REDVVQVLSS PAEGCSVV


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