TNR27_MOUSE
ID TNR27_MOUSE Reviewed; 297 AA.
AC Q8BX35; Q8BM50;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 27;
DE AltName: Full=X-linked ectodysplasin-A2 receptor;
DE Short=EDA-A2 receptor;
GN Name=Eda2r; Synonyms=Tnfrsf27, Xedar;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Receptor for EDA isoform A2, but not for EDA isoform A1.
CC Mediates the activation of the NF-kappa-B and JNK pathways. Activation
CC seems to be mediated by binding to TRAF3 and TRAF6 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Associates with TRAF1, TRAF3 and TRAF6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type III
CC membrane protein {ECO:0000250}.
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DR EMBL; AK034909; BAC28879.1; -; mRNA.
DR EMBL; AK049134; BAC33562.1; -; mRNA.
DR CCDS; CCDS30293.1; -.
DR RefSeq; NP_001154904.1; NM_001161432.1.
DR RefSeq; NP_001154905.1; NM_001161433.1.
DR RefSeq; NP_780749.3; NM_175540.5.
DR RefSeq; XP_006528088.1; XM_006528025.2.
DR RefSeq; XP_006528089.1; XM_006528026.2.
DR AlphaFoldDB; Q8BX35; -.
DR BioGRID; 232789; 2.
DR IntAct; Q8BX35; 1.
DR STRING; 10090.ENSMUSP00000109463; -.
DR GlyGen; Q8BX35; 2 sites.
DR iPTMnet; Q8BX35; -.
DR PhosphoSitePlus; Q8BX35; -.
DR MaxQB; Q8BX35; -.
DR PaxDb; Q8BX35; -.
DR PRIDE; Q8BX35; -.
DR ProteomicsDB; 258810; -.
DR Antibodypedia; 3374; 342 antibodies from 32 providers.
DR DNASU; 245527; -.
DR Ensembl; ENSMUST00000037353; ENSMUSP00000041210; ENSMUSG00000034457.
DR Ensembl; ENSMUST00000113832; ENSMUSP00000109463; ENSMUSG00000034457.
DR GeneID; 245527; -.
DR KEGG; mmu:245527; -.
DR UCSC; uc009tus.2; mouse.
DR CTD; 60401; -.
DR MGI; MGI:2442860; Eda2r.
DR VEuPathDB; HostDB:ENSMUSG00000034457; -.
DR eggNOG; ENOG502S069; Eukaryota.
DR GeneTree; ENSGT00940000153259; -.
DR HOGENOM; CLU_041149_0_0_1; -.
DR InParanoid; Q8BX35; -.
DR OMA; EVQCAFR; -.
DR OrthoDB; 672843at2759; -.
DR PhylomeDB; Q8BX35; -.
DR TreeFam; TF331385; -.
DR Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
DR BioGRID-ORCS; 245527; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Eda2r; mouse.
DR PRO; PR:Q8BX35; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BX35; protein.
DR Bgee; ENSMUSG00000034457; Expressed in temporalis muscle and 116 other tissues.
DR ExpressionAtlas; Q8BX35; baseline and differential.
DR Genevisible; Q8BX35; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IGI:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR CDD; cd15838; TNFRSF27; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR022319; TNFR_27.
DR InterPro; IPR034060; TNFRSF27_N.
DR PANTHER; PTHR12120:SF8; PTHR12120:SF8; 2.
DR Pfam; PF00020; TNFR_c6; 2.
DR PRINTS; PR01973; TNFACTORR27.
DR SMART; SM00208; TNFR; 2.
DR PROSITE; PS00652; TNFR_NGFR_1; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..297
FT /note="Tumor necrosis factor receptor superfamily member
FT 27"
FT /id="PRO_0000058939"
FT TOPO_DOM 1..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 2..41
FT /note="TNFR-Cys 1"
FT REPEAT 43..83
FT /note="TNFR-Cys 2"
FT REPEAT 85..118
FT /note="TNFR-Cys 3"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 18..31
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 21..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 44..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 61..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 64..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 86..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 107..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT CONFLICT 70
FT /note="V -> A (in Ref. 1; BAC28879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33066 MW; 46FEFDDC51D739BE CRC64;
MDCQENEYRD QWGRCVTCQQ CGPGQELSKD CGYGEGGDAH CIVCPPRKYK STWGHHRCQT
CITCAVINRV QKANCTNTSN AICGDCLPRF YRKTRIGGLQ DQECIPCTKQ TPSSEVQCTF
QLSLVKVDAH TVPPREATLV ALVGSLLVVF ALAFLGLFFL YCKQIFNRHC QCRDSLQYEA
EKTVEEDSLF PVPPGQETSP EFPANEGILE IKPLNSILDD DCSSTRGFPT QESFTMASCA
SESHSQWVHT PIECTELDLQ KFSSSIPSTG PETLRENTAE HSGDRLELYV PFEVPSL
