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Tumor necrosis factor receptor superfamily member 5 (B-cell surface antigen CD40) (Bp50) (CD40L receptor) (CDw40) (CD antigen CD40)

 TNR5_HUMAN              Reviewed;         277 AA.
P25942; E1P5S9; Q53GN5; Q5JY15; Q5U007; Q7M4Q8; Q86YK5; Q9BYU0;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
30-AUG-2017, entry version 204.
RecName: Full=Tumor necrosis factor receptor superfamily member 5;
AltName: Full=B-cell surface antigen CD40;
AltName: Full=Bp50;
AltName: Full=CD40L receptor;
AltName: Full=CDw40;
AltName: CD_antigen=CD40;
Flags: Precursor;
Name=CD40; Synonyms=TNFRSF5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
PubMed=2475341;
Stamenkovic I., Clark E.A., Seed B.;
"A B-lymphocyte activation molecule related to the nerve growth factor
receptor and induced by cytokines in carcinomas.";
EMBO J. 8:1403-1410(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
PubMed=11172023; DOI=10.1073/pnas.98.4.1751;
Tone M., Tone Y., Fairchild P.J., Wykes M., Waldmann H.;
"Regulation of CD40 function by its isoforms generated through
alternative splicing.";
Proc. Natl. Acad. Sci. U.S.A. 98:1751-1756(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
TISSUE=Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-124 AND ALA-227.
NIEHS SNPs program;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-223 (ISOFORM I).
TISSUE=Leukocyte;
He X., Xu L., Zeng Y.;
"Transcripts of CD40 isoform in peripheral mononuclear cells.";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 21-50, SUBUNIT, AND VARIANTS GLN-26; GLY-35 AND
THR-39.
TISSUE=Lymphoma, and Urinary bladder carcinoma;
PubMed=2463309;
Braesch-Andersen S., Paulie S., Koho H., Nika H., Aspenstroem P.,
Perlmann P.;
"Biochemical characteristics and partial amino acid sequence of the
receptor-like human B cell and carcinoma antigen CDw40.";
J. Immunol. 142:562-567(1989).
[12]
PROTEIN SEQUENCE OF 21-35.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[13]
PROTEIN SEQUENCE OF 21-30.
PubMed=11676606; DOI=10.1006/prep.2001.1501;
Khandekar S.S., Silverman C., Wells-Marani J., Bacon A.M., Birrell H.,
Brigham-Burke M., DeMarini D.J., Jonak Z.L., Camilleri P.,
Fishman-Lobell J.;
"Determination of carbohydrate structures N-linked to soluble CD154
and characterization of the interactions of CD40 with CD154 expressed
in Pichia pastoris and Chinese hamster ovary cells.";
Protein Expr. Purif. 23:301-310(2001).
[14]
INTERACTION WITH TRAF3.
PubMed=7530216; DOI=10.1016/0014-5793(94)01406-Q;
Sato T., Irie S., Reed J.C.;
"A novel member of the TRAF family of putative signal transducing
proteins binds to the cytosolic domain of CD40.";
FEBS Lett. 358:113-118(1995).
[15]
INTERACTION WITH TRAF3.
PubMed=7533327; DOI=10.1126/science.7533327;
Cheng G., Cleary A.M., Ye Z.S., Hong D.I., Lederman S., Baltimore D.;
"Involvement of CRAF1, a relative of TRAF, in CD40 signaling.";
Science 267:1494-1498(1995).
[16]
INTERACTION WITH TRAF1; TRAF2; TRAF3 AND TRAF5.
PubMed=9718306; DOI=10.1021/bi981067q;
Pullen S.S., Miller H.G., Everdeen D.S., Dang T.T., Crute J.J.,
Kehry M.R.;
"CD40-tumor necrosis factor receptor-associated factor (TRAF)
interactions: regulation of CD40 signaling through multiple TRAF
binding sites and TRAF hetero-oligomerization.";
Biochemistry 37:11836-11845(1998).
[17]
INTERACTION WITH TRAF5.
PubMed=9511754; DOI=10.1016/S0378-1119(97)00616-1;
Mizushima S., Fujita M., Ishida T., Azuma S., Kato K., Hirai M.,
Otsuka M., Yamamoto T., Inoue J.;
"Cloning and characterization of a cDNA encoding the human homolog of
tumor necrosis factor receptor-associated factor 5 (TRAF5).";
Gene 207:135-140(1998).
[18]
INTERACTION WITH TRAF6.
PubMed=9432981; DOI=10.1084/jem.187.2.237;
Kashiwada M., Shirakata Y., Inoue J., Nakano H., Okazaki K.,
Okumura K., Yamamoto T., Nagaoka H., Takemori T.;
"Tumor necrosis factor receptor-associated factor 6 (TRAF6) stimulates
extracellular signal-regulated kinase (ERK) activity in CD40 signaling
along a ras-independent pathway.";
J. Exp. Med. 187:237-244(1998).
[19]
3D-STRUCTURE MODELING OF 24-144.
PubMed=9037712;
DOI=10.1002/(SICI)1097-0134(199701)27:1<59::AID-PROT7>3.3.CO;2-Z;
Bajorath J., Aruffo A.;
"Construction and analysis of a detailed three-dimensional model of
the ligand binding domain of the human B cell receptor CD40.";
Proteins 27:59-70(1997).
[20]
3D-STRUCTURE MODELING OF 26-186 IN COMPLEX WITH CD40LG.
PubMed=9605317; DOI=10.1002/pro.5560070506;
Singh J., Garber E., van Vlijmen H., Karpsusas M., Hsu Y.-M.,
Zheng Z., Naismith J.H., Thomas D.;
"The role of polar interactions in the molecular recognition of CD40L
with its receptor CD40.";
Protein Sci. 7:1124-1135(1998).
[21]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 247-266 IN COMPLEX WITH
TRAF3.
PubMed=10984535; DOI=10.1073/pnas.97.19.10395;
Ni C.Z., Welsh K., Leo E., Chiou C.K., Wu H., Reed J.C., Ely K.R.;
"Molecular basis for CD40 signaling mediated by TRAF3.";
Proc. Natl. Acad. Sci. U.S.A. 97:10395-10399(2000).
[22]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 178-195 IN COMPLEX WITH
TRAF3.
PubMed=12005438; DOI=10.1016/S0969-2126(02)00733-5;
Li C., Ni C.Z., Havert M.L., Cabezas E., He J., Kaiser D., Reed J.C.,
Satterthwait A.C., Cheng G., Ely K.R.;
"Downstream regulator TANK binds to the CD40 recognition site on
TRAF3.";
Structure 10:403-411(2002).
[23]
VARIANT HIGM3 ARG-83.
PubMed=11675497; DOI=10.1073/pnas.221456898;
Ferrari S., Giliani S., Insalaco A., Al-Ghonaium A., Soresina A.R.,
Loubser M., Avanzini M.A., Marconi M., Badolato R., Ugazio A.G.,
Levy Y., Catalan N., Durandy A., Tbakhi A., Notarangelo L.D.,
Plebani A.;
"Mutations of CD40 gene cause an autosomal recessive form of
immunodeficiency with hyper IgM.";
Proc. Natl. Acad. Sci. U.S.A. 98:12614-12619(2001).
[24]
VARIANT HIGM3 GLY-37.
PubMed=26545377; DOI=10.1007/s00251-015-0878-6;
Ouadani H., Ben-Mustapha I., Ben-ali M., Ben-khemis L., Largueche B.,
Boussoffara R., Maalej S., Fetni I., Hassayoun S., Mahfoudh A.,
Mellouli F., Yalaoui S., Masmoudi H., Bejaoui M., Barbouche M.R.;
"Novel and recurrent AID mutations underlie prevalent autosomal
recessive form of HIGM in consanguineous patients.";
Immunogenetics 68:19-28(2016).
-!- FUNCTION: Receptor for TNFSF5/CD40LG. Transduces TRAF6- and
MAP3K8-mediated signals that activate ERK in macrophages and B
cells, leading to induction of immunoglobulin secretion.
-!- SUBUNIT: Monomer and homodimer. The variant form found in the
bladder carcinoma cell line Hu549 does not form homodimers.
Interacts with TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6. Interacts
with TRAF6 and MAP3K8; the interaction is required for ERK
activation. {ECO:0000269|PubMed:10984535,
ECO:0000269|PubMed:12005438, ECO:0000269|PubMed:2463309,
ECO:0000269|PubMed:7530216, ECO:0000269|PubMed:7533327,
ECO:0000269|PubMed:9432981, ECO:0000269|PubMed:9511754,
ECO:0000269|PubMed:9718306}.
-!- INTERACTION:
Q12933:TRAF2; NbExp=9; IntAct=EBI-525714, EBI-355744;
Q13114:TRAF3; NbExp=3; IntAct=EBI-525714, EBI-357631;
Q9Y4K3:TRAF6; NbExp=2; IntAct=EBI-525714, EBI-359276;
-!- SUBCELLULAR LOCATION: Isoform I: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform II: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=I;
IsoId=P25942-1; Sequence=Displayed;
Name=II;
IsoId=P25942-2; Sequence=VSP_006472, VSP_006473;
-!- TISSUE SPECIFICITY: B-cells and in primary carcinomas.
-!- DISEASE: Immunodeficiency with hyper-IgM 3 (HIGM3) [MIM:606843]: A
rare immunodeficiency syndrome characterized by normal or elevated
serum IgM levels with absence of IgG, IgA, and IgE. It results in
a profound susceptibility to bacterial infections.
{ECO:0000269|PubMed:11675497, ECO:0000269|PubMed:26545377}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=CD40base; Note=CD40 mutation db;
URL="http://structure.bmc.lu.se/idbase/CD40base/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tnfrsf5/";
-!- WEB RESOURCE: Name=Wikipedia; Note=CD40 entry;
URL="https://en.wikipedia.org/wiki/CD40";
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EMBL; X60592; CAA43045.1; -; mRNA.
EMBL; AJ300189; CAC29424.1; -; mRNA.
EMBL; BT019901; AAV38704.1; -; mRNA.
EMBL; AK222896; BAD96616.1; -; mRNA.
EMBL; AY504960; AAR84238.1; -; Genomic_DNA.
EMBL; EF064754; ABK41937.1; -; Genomic_DNA.
EMBL; AL035662; CAC17670.1; -; Genomic_DNA.
EMBL; AL035662; CAI42973.1; -; Genomic_DNA.
EMBL; CH471077; EAW75758.1; -; Genomic_DNA.
EMBL; CH471077; EAW75760.1; -; Genomic_DNA.
EMBL; CH471077; EAW75762.1; -; Genomic_DNA.
EMBL; BC012419; AAH12419.1; -; mRNA.
EMBL; AY225405; AAO43990.1; -; mRNA.
CCDS; CCDS13393.1; -. [P25942-1]
CCDS; CCDS13394.1; -. [P25942-2]
PIR; B60771; B60771.
PIR; S04460; A60771.
RefSeq; NP_001241.1; NM_001250.5. [P25942-1]
RefSeq; NP_001289682.1; NM_001302753.1.
RefSeq; NP_001309351.1; NM_001322422.1.
RefSeq; NP_690593.1; NM_152854.3. [P25942-2]
UniGene; Hs.472860; -.
PDB; 1CDF; Model; -; A=24-144.
PDB; 1CZZ; X-ray; 2.70 A; D/E=250-258.
PDB; 1D00; X-ray; 2.00 A; I/J/K/L/M/N/O/P=250-254.
PDB; 1FLL; X-ray; 3.50 A; X/Y=246-266.
PDB; 1LB6; X-ray; 1.80 A; B=230-236.
PDB; 3QD6; X-ray; 3.50 A; R/S/T/U=21-190.
PDB; 5DMI; X-ray; 3.69 A; A=23-193.
PDB; 5DMJ; X-ray; 2.79 A; A/D/F=23-193.
PDB; 5IHL; X-ray; 3.30 A; A/D/F/H=23-193.
PDBsum; 1CDF; -.
PDBsum; 1CZZ; -.
PDBsum; 1D00; -.
PDBsum; 1FLL; -.
PDBsum; 1LB6; -.
PDBsum; 3QD6; -.
PDBsum; 5DMI; -.
PDBsum; 5DMJ; -.
PDBsum; 5IHL; -.
ProteinModelPortal; P25942; -.
SMR; P25942; -.
BioGrid; 107396; 48.
DIP; DIP-3014N; -.
ELM; P25942; -.
IntAct; P25942; 5.
MINT; MINT-1505936; -.
STRING; 9606.ENSP00000361359; -.
BindingDB; P25942; -.
ChEMBL; CHEMBL1250358; -.
iPTMnet; P25942; -.
PhosphoSitePlus; P25942; -.
BioMuta; CD40; -.
DMDM; 116000; -.
MaxQB; P25942; -.
PaxDb; P25942; -.
PeptideAtlas; P25942; -.
PRIDE; P25942; -.
DNASU; 958; -.
Ensembl; ENST00000372276; ENSP00000361350; ENSG00000101017. [P25942-2]
Ensembl; ENST00000372285; ENSP00000361359; ENSG00000101017. [P25942-1]
GeneID; 958; -.
KEGG; hsa:958; -.
UCSC; uc002xrg.2; human. [P25942-1]
CTD; 958; -.
DisGeNET; 958; -.
GeneCards; CD40; -.
HGNC; HGNC:11919; CD40.
HPA; CAB002495; -.
HPA; CAB072868; -.
HPA; HPA031567; -.
HPA; HPA031568; -.
MalaCards; CD40; -.
MIM; 109535; gene.
MIM; 606843; phenotype.
neXtProt; NX_P25942; -.
OpenTargets; ENSG00000101017; -.
Orphanet; 101090; Hyper-IgM syndrome type 3.
PharmGKB; PA36612; -.
eggNOG; ENOG410IY0H; Eukaryota.
eggNOG; ENOG4112DB5; LUCA.
GeneTree; ENSGT00760000119204; -.
HOVERGEN; HBG005117; -.
InParanoid; P25942; -.
KO; K03160; -.
OMA; CHPWTSC; -.
OrthoDB; EOG091G03XW; -.
PhylomeDB; P25942; -.
TreeFam; TF331157; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
SIGNOR; P25942; -.
EvolutionaryTrace; P25942; -.
GeneWiki; CD40_(protein); -.
GenomeRNAi; 958; -.
PMAP-CutDB; P25942; -.
PRO; PR:P25942; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101017; -.
CleanEx; HS_CD40; -.
ExpressionAtlas; P25942; baseline and differential.
Genevisible; P25942; HS.
GO; GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
GO; GO:0043196; C:varicosity; IEA:Ensembl.
GO; GO:0003823; F:antigen binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0042100; P:B cell proliferation; NAS:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:BHF-UCL.
GO; GO:0036018; P:cellular response to erythropoietin; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0030168; P:platelet activation; NAS:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
GO; GO:0090037; P:positive regulation of protein kinase C signaling; IMP:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:BHF-UCL.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0051023; P:regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0033590; P:response to cobalamin; IEA:Ensembl.
GO; GO:0034341; P:response to interferon-gamma; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:1901652; P:response to peptide; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
CDD; cd13407; TNFRSF5; 1.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR020435; TNFR_5.
InterPro; IPR034021; TNFRSF5_N.
Pfam; PF00020; TNFR_c6; 1.
PRINTS; PR01922; TNFACTORR5.
SMART; SM00208; TNFR; 4.
PROSITE; PS00652; TNFR_NGFR_1; 1.
PROSITE; PS50050; TNFR_NGFR_2; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Immunity; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 20 {ECO:0000269|PubMed:11676606,
ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:2463309}.
CHAIN 21 277 Tumor necrosis factor receptor
superfamily member 5.
/FTId=PRO_0000034559.
TOPO_DOM 21 193 Extracellular. {ECO:0000255}.
TRANSMEM 194 215 Helical. {ECO:0000255}.
TOPO_DOM 216 277 Cytoplasmic. {ECO:0000255}.
REPEAT 25 60 TNFR-Cys 1.
REPEAT 61 103 TNFR-Cys 2.
REPEAT 104 144 TNFR-Cys 3.
REPEAT 145 187 TNFR-Cys 4.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 180 180 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 26 37
DISULFID 38 51
DISULFID 41 59
DISULFID 62 77
DISULFID 83 103
DISULFID 105 119
DISULFID 111 116
DISULFID 125 143
VAR_SEQ 166 203 SCETKDLVVQQAGTNKTDVVCGPQDRLRALVVIPIIFG ->
RSPGSAESPGGDPHHLRDPVCHPLGAGLYQKGGQEANQ
(in isoform II).
{ECO:0000303|PubMed:11172023}.
/FTId=VSP_006472.
VAR_SEQ 204 277 Missing (in isoform II).
{ECO:0000303|PubMed:11172023}.
/FTId=VSP_006473.
VARIANT 26 26 C -> Q (in bladder carcinoma cell line
Hu549; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:2463309}.
/FTId=VAR_039301.
VARIANT 35 35 S -> G (in bladder carcinoma cell line
Hu549; dbSNP:rs750234130).
{ECO:0000269|PubMed:2463309}.
/FTId=VAR_039302.
VARIANT 37 37 C -> G (in HIGM3).
{ECO:0000269|PubMed:26545377}.
/FTId=VAR_077569.
VARIANT 39 39 S -> T (in bladder carcinoma cell line
Hu549). {ECO:0000269|PubMed:2463309}.
/FTId=VAR_039303.
VARIANT 83 83 C -> R (in HIGM3; dbSNP:rs28931586).
{ECO:0000269|PubMed:11675497}.
/FTId=VAR_013628.
VARIANT 124 124 S -> L (in dbSNP:rs11569321).
{ECO:0000269|Ref.5}.
/FTId=VAR_018751.
VARIANT 227 227 P -> A (in dbSNP:rs11086998).
{ECO:0000269|Ref.5}.
/FTId=VAR_018752.
CONFLICT 112 112 T -> A (in Ref. 4; BAD96616).
{ECO:0000305}.
TURN 28 30 {ECO:0000244|PDB:5DMJ}.
STRAND 33 37 {ECO:0000244|PDB:5DMJ}.
STRAND 45 49 {ECO:0000244|PDB:5DMJ}.
STRAND 53 55 {ECO:0000244|PDB:5DMJ}.
STRAND 58 61 {ECO:0000244|PDB:5DMJ}.
STRAND 64 67 {ECO:0000244|PDB:3QD6}.
STRAND 70 72 {ECO:0000244|PDB:5DMJ}.
HELIX 85 87 {ECO:0000244|PDB:5DMJ}.
STRAND 89 93 {ECO:0000244|PDB:5DMJ}.
STRAND 97 99 {ECO:0000244|PDB:5DMJ}.
STRAND 102 108 {ECO:0000244|PDB:5DMJ}.
STRAND 110 113 {ECO:0000244|PDB:5DMJ}.
STRAND 118 121 {ECO:0000244|PDB:5DMJ}.
STRAND 129 131 {ECO:0000244|PDB:5IHL}.
STRAND 136 138 {ECO:0000244|PDB:5IHL}.
STRAND 143 145 {ECO:0000244|PDB:5IHL}.
STRAND 156 158 {ECO:0000244|PDB:5DMJ}.
STRAND 167 170 {ECO:0000244|PDB:5DMJ}.
STRAND 180 182 {ECO:0000244|PDB:5DMJ}.
STRAND 234 236 {ECO:0000244|PDB:1LB6}.
STRAND 258 260 {ECO:0000244|PDB:1FLL}.
SEQUENCE 277 AA; 30619 MW; BC8776EC2C4A5680 CRC64;
MVRLPLQCVL WGCLLTAVHP EPPTACREKQ YLINSQCCSL CQPGQKLVSD CTEFTETECL
PCGESEFLDT WNRETHCHQH KYCDPNLGLR VQQKGTSETD TICTCEEGWH CTSEACESCV
LHRSCSPGFG VKQIATGVSD TICEPCPVGF FSNVSSAFEK CHPWTSCETK DLVVQQAGTN
KTDVVCGPQD RLRALVVIPI IFGILFAILL VLVFIKKVAK KPTNKAPHPK QEPQEINFPD
DLPGSNTAAP VQETLHGCQP VTQEDGKESR ISVQERQ


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