[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1016/0092-8674(90)90815-V; PubMed=2158862 [NCBI, ExPASy, EBI, Israel, Japan] Loetscher H., Pan Y.-C.E., Lahm H.-W., Gentz R., Brockhaus M., Tabuchi H., Lesslauer W.; "Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor."; Cell 61:351-359(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Placenta; DOI=10.1016/0092-8674(90)90816-W; PubMed=2158863 [NCBI, ExPASy, EBI, Israel, Japan] Schall T.J., Lewis M., Koller K.J., Lee A., Rice G.C., Wong G.H.W., Getanaga T., Granger G.A., Lentz R., Raab H., Kohr W.J., Goeddel D.V.; "Molecular cloning and expression of a receptor for human tumor necrosis factor."; Cell 61:361-370(1990).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1089/dna.1990.9.705; PubMed=1702293 [NCBI, ExPASy, EBI, Israel, Japan] Himmler A., Maurer-Fogy I., Kroenke M., Scheurich P., Pfizenmaier K., Lantz M., Olsson I., Hauptmann R., Stratowa C., Adolf G.R.; "Molecular cloning and expression of human and rat tumor necrosis factor receptor chain (p60) and its soluble derivative, tumor necrosis factor-binding protein."; DNA Cell Biol. 9:705-715(1990).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 41-53; 110-124 AND 199-201 (ISOFORM 1). PubMed=1698610 [NCBI, ExPASy, EBI, Israel, Japan] Nophar Y., Kemper O., Brakebusch C., Engelmann H., Zwang R., Aderka D., Holtmann H., Wallach D.; "Soluble forms of tumor necrosis factor receptors (TNF-Rs). The cDNA for the type I TNF-R, cloned using amino acid sequence data of its soluble form, encodes both the cell surface and a soluble form of the receptor."; EMBO J. 9:3269-3278(1990).
[5]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Placenta; DOI=10.1073/pnas.87.19.7380; PubMed=2170974 [NCBI, ExPASy, EBI, Israel, Japan] Gray P.W., Barrett K., Chantry D., Turner M., Feldman M.; "Cloning of human tumor necrosis factor (TNF) receptor cDNA and expression of recombinant soluble TNF-binding protein."; Proc. Natl. Acad. Sci. U.S.A. 87:7380-7384(1990).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0888-7543(92)90226-I; PubMed=1315717 [NCBI, ExPASy, EBI, Israel, Japan] Fuchs P., Strehl S., Dworzak M., Himmler A., Ambros P.F.; "Structure of the human TNF receptor 1 (p60) gene (TNFR1) and localization to chromosome 12p13."; Genomics 13:219-224(1992).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-75 AND GLN-121. SeattleSNPs variation discovery resource; Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). TISSUE=Neutrophil, Teratocarcinoma, Tongue, and Uterus; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Muscle; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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]	PROTEIN SEQUENCE OF 41-57 (ISOFORM 1). TISSUE=Urine; PubMed=8015639 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki J., Tomizawa S., Arai H., Seki Y., Maruyama K., Kuroume T.; "Purification of two types of TNF inhibitors in the urine of the patient with chronic glomerulonephritis."; Nephron 66:386-390(1994).
[11]	PROTEIN SEQUENCE OF 41-45 (ISOFORM 1). PubMed=2153136 [NCBI, ExPASy, EBI, Israel, Japan] Engelmann H., Novick D., Wallach D.; "Two tumor necrosis factor-binding proteins purified from human urine. Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors."; J. Biol. Chem. 265:1531-1536(1990).
[12]	INTERACTION WITH HCV CORE PROTEIN. PubMed=9557650 [NCBI, ExPASy, EBI, Israel, Japan] Zhu N., Khoshnan A., Schneider R., Matsumoto M., Dennert G., Ware C.F., Lai M.M.C.; "Hepatitis C virus core protein binds to the cytoplasmic domain of tumor necrosis factor (TNF) receptor 1 and enhances TNF-induced apoptosis."; J. Virol. 72:3691-3697(1998).
[13]	INTERACTION WITH RIPK1 AND SQSTM1. DOI=10.1093/emboj/18.11.3044; PubMed=10356400 [NCBI, ExPASy, EBI, Israel, Japan] Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.; "The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."; EMBO J. 18:3044-3053(1999).
[14]	INTERACTION WITH FEM1B. DOI=10.1074/jbc.274.45.32461; PubMed=10542291 [NCBI, ExPASy, EBI, Israel, Japan] Chan S.-L., Tan K.-O., Zhang L., Yee K.S.Y., Ronca F., Chan M.-Y., Yu V.C.; "F1Aalpha, a death receptor-binding protein homologous to the Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase substrate that mediates apoptosis."; J. Biol. Chem. 274:32461-32468(1999).
[15]	INTERACTION WITH GRB2. DOI=10.1084/jem.189.11.1707; PubMed=10359574 [NCBI, ExPASy, EBI, Israel, Japan] Hildt E., Oess S.; "Identification of Grb2 as a novel binding partner of tumor necrosis factor (TNF) receptor I."; J. Exp. Med. 189:1707-1714(1999).
[16]	INTERACTION WITH BAG4. DOI=10.1126/science.283.5401.543; PubMed=9915703 [NCBI, ExPASy, EBI, Israel, Japan] Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.; "Prevention of constitutive TNF receptor 1 signaling by silencer of death domains."; Science 283:543-546(1999).
[17]	INTERACTION WITH BRE. DOI=10.1074/jbc.M408678200; PubMed=15465831 [NCBI, ExPASy, EBI, Israel, Japan] Li Q., Ching A.K.-K., Chan B.C.-L., Chow S.K.-Y., Lim P.-L., Ho T.C.-Y., Ip W.-K., Wong C.-K., Lam C.W.-K., Lee K.K.-H., Chan J.Y.-H., Chui Y.-L.; "A death receptor-associated anti-apoptotic protein, BRE, inhibits mitochondrial apoptotic pathway."; J. Biol. Chem. 279:52106-52116(2004).
[18]	X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 30-211 IN COMPLEX WITH TNFB. DOI=10.1016/0092-8674(93)90132-A; PubMed=8387891 [NCBI, ExPASy, EBI, Israel, Japan] Banner D.W., D'Arcy A., Janes W., Gentz R., Schoenfeld H.-J., Broger C., Loetscher H., Lesslauer W.; "Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation."; Cell 73:431-445(1993).
[19]	X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 41-202. DOI=10.1016/S0969-2126(96)00134-7; PubMed=8939750 [NCBI, ExPASy, EBI, Israel, Japan] Naismith J.H., Devine T.Q., Khono H., Sprang S.R.; "Structures of the extracellular domain of the type I tumor necrosis factor receptor."; Structure 4:1251-1262(1996).
[20]	VARIANTS FHF ARG-59; TYR-62; MET-79; PHE-81; ARG-117 AND TYR-117. DOI=10.1016/S0092-8674(00)80721-7; PubMed=10199409 [NCBI, ExPASy, EBI, Israel, Japan] McDermott M.F., Aksentijevich I., Galon J., McDermott E.M., Ogunkolade B.W., Centola M., Mansfield E., Gadina M., Karenko L., Pettersson T., McCarthy J., Frucht D.M., Aringer M., Torosyan Y., Teppo A.-M., Wilson M., Karaarslan H.M., Wan Y., Todd I., Wood G., Schlimgen R., Kumarajeewa T.R., Cooper S.M., Vella J.P., Amos C.I., Mulley J., Quane K.A., Molloy M.G., Rnaki A., Powell R.J., Hitman G.A., O'Shea J., Kastner D.L.; "Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes."; Cell 97:133-144(1999).
[21]	VARIANT FHF SER-59. DOI=10.1002/1529-0131(200007)43:7<1535::AID-ANR18>3.3.CO;2-3; PubMed=10902757 [NCBI, ExPASy, EBI, Israel, Japan] Dode C., Papo T., Fieschi C., Pecheux C., Dion E., Picard F., Godeau P., Bienvenu J., Piette J.-C., Delpech M., Grateau G.; "A novel missense mutation (C30S) in the gene encoding tumor necrosis factor receptor 1 linked to autosomal-dominant recurrent fever with localized myositis in a French family."; Arthritis Rheum. 43:1535-1542(2000).
[22]	VARIANTS FHF GLN-51; SER-59; GLY-62; LEU-75; GLY-115 AND GLN-121. DOI=10.1086/321976; PubMed=11443543 [NCBI, ExPASy, EBI, Israel, Japan] Aksentijevich I., Galon J., Soares M., Mansfield E., Hull K., Oh H.-H., Goldbach-Mansky R., Dean J., Athreya B., Reginato A.J., Henrickson M., Pons-Estel B., O'Shea J.J., Kastner D.L.; "The tumor-necrosis-factor receptor-associated periodic syndrome: new mutations in TNFRSF1A, ancestral origins, genotype-phenotype studies, and evidence for further genetic heterogeneity of periodic fevers."; Am. J. Hum. Genet. 69:301-314(2001).
[23]	VARIANTS FHF SER-99 AND PRO-121. DOI=10.1002/art.11215; PubMed=13130484 [NCBI, ExPASy, EBI, Israel, Japan] Aganna E., Hammond L., Hawkins P.N., Aldea A., McKee S.A., Ploos van Amstel H.K., Mischung C., Kusuhara K., Saulsbury F.T., Lachmann H.J., Bybee A., McDermott E.M., La Regina M., Arostegui J.I., Campistol J.M., Worthington S., High K.P., Molloy M.G., Baker N., Bidwell J.L., Castaner J.L., Whiteford M.L., Janssens-Korpola P.L., Manna R., Powell R.J., Woo P., Solis P., Minden K., Frenkel J., Yague J., Mirakian R.M., Hitman G.A., McDermott M.F.; "Heterogeneity among patients with tumor necrosis factor receptor-associated periodic syndrome phenotypes."; Arthritis Rheum. 48:2632-2644(2003).
[24]	VARIANT FHF SER-99. DOI=10.1007/s00431-003-1338-0; PubMed=14610673 [NCBI, ExPASy, EBI, Israel, Japan] Kusuhara K., Nomura A., Nakao F., Hara T.; "Tumour necrosis factor receptor-associated periodic syndrome with a novel mutation in the TNFRSF1A gene in a Japanese family."; Eur. J. Pediatr. 163:30-32(2004).

Comments

FUNCTION: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.
SUBUNIT: Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling. Interacts with BAG4, BRE, FEM1B, GRB2, SQSTM1 and TRPC4AP. Interacts with HCV core protein.
INTERACTION:
P48729:CSNK1A1; NbExp=1; IntAct=EBI-299451, EBI-1383726;
P01375:TNF; NbExp=1; IntAct=EBI-299451, EBI-359977;
Q15628:TRADD; NbExp=5; IntAct=EBI-299451, EBI-359215;
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Secreted.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P19438-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P19438-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_037153.

Name	3
Isoform ID	P19438-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_037154.

DOMAIN: The domain that induces A-SMASE is probably identical to the death domain. The N-SMASE activation domain (NSD) is both necessary and sufficient for activation of N-SMASE.
DOMAIN: Both the cytoplasmic membrane-proximal region and the C-terminal region containing the death domain are involved in the interaction with TRPC4AP (By similarity).
PTM: The soluble form is produced from the membrane form by proteolytic processing.
DISEASE: Defects in TNFRSF1A are the cause of familial hibernian fever (FHF) [MIM:142680]; also known as tumor necrosis factor receptor-associated periodic syndrome (TRAPS). FHF is a hereditary periodic fever syndrome characterized by recurrent fever, abdominal pain, localized tender skin lesions and myalgia. Reactive amyloidosis is the main complication and occurs in 25% of cases.
SIMILARITY: Contains 1 death domain.
SIMILARITY: Contains 4 TNFR-Cys repeats.
WEB RESOURCE: Name=INFEVERS; Note=Repertory of FMF and hereditary autoinflammatory disorders mutations; URL="http://fmf.igh.cnrs.fr/ISSAID/infevers/disease_menu.php?n=2";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=TNFRSF1A";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/tnfrsf1a/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M58286; AAA36753.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33294; AAA03210.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63121; AAA36754.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X55313; CAA39021.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M60275; AAA36756.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M75866; AAA61201.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M75864; AAA61201.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M75865; AAA61201.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY131997; AAM77802.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK056611; BAG51763.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291088; BAF83777.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK298729; BAG60879.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK304517; BAG65321.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK315509; BAG37891.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010140; AAH10140.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
A21522; CAA01558.1; -; Unassigned_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00018880; -.

A38208; GQHUT1.

NP_001056.1; -.

3D structure databases

PDB

1EXT; X-ray; 1.85 A; A/B=41-201.	[ExPASy / RCSB / EBI]
1FT4; X-ray; 2.90 A; A/B=41-201.	[ExPASy / RCSB / EBI]
1ICH; NMR; -; A=345-455.	[ExPASy / RCSB / EBI]
1NCF; X-ray; 2.25 A; A/B=41-201.	[ExPASy / RCSB / EBI]
1TNR; X-ray; 2.85 A; R=44-182.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1EXT; -.
1FT4; -.
1ICH; -.
1NCF; -.
1TNR; -.

ModBase

P19438.

Protein-protein interaction databases

DIP

DIP:407N; -.

IntAct

P19438; 80.

PTM databases

PhosphoSite

P19438; -.

Enzyme and pathway databases

Pathway_Interaction_DB

nfkappabcanonicalpathway; Canonical NF-kappaB pathway.
caspase_pathway; Caspase cascade in apoptosis.
ceramidepathway; Ceramide signaling pathway.
hivnefpathway; HIV-1 Nef: Negative effector of Fas and TNF-alpha.
hdac_classi_pathway; Signaling events mediated by HDAC Class I.
tnfpathway; TNF receptor signaling pathway.

Reactome

REACT_578; Apoptosis.

Organism-specific databases

GeneCards

GC12M006308; -.

H-InvDB

HIX0010360; -.

HGNC

HGNC:11916; TNFRSF1A.

GenAtlas

TNFRSF1A.

HPA

CAB010309; -.
HPA004102; -.

MIM

142680; phenotype. [NCBI / EBI]
191190; gene. [NCBI / EBI]

Orphanet

32960; TRAPS syndrome.

PharmGKB

PA36609; -.

Gene expression databases

Bgee

P19438; -.

CleanEx

HS_TNFRSF1A; -.

GermOnline

ENSG00000067182; Homo sapiens.

Ontologies

GO:0005576;	Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0045121;	Cellular component: membrane raft (inferred from direct assay from UniProtKB).
GO:0005031;	Molecular function: tumor necrosis factor receptor activity (traceable author statement from UniProtKB).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0019221;	Biological process: cytokine-mediated signaling pathway (inferred from sequence or structural similarity from UniProtKB).
GO:0006954;	Biological process: inflammatory response (inferred from sequence or structural similarity from UniProtKB).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0043123;	Biological process: positive regulation of I-kappaB kinase/NF-kappaB cascade (inferred from expression pattern from UniProtKB).
GO:0050729;	Biological process: positive regulation of inflammatory response (inferred from sequence or structural similarity from UniProtKB).
GO:0045944;	Biological process: positive regulation of transcription from RNA polymerase II promoter (inferred from sequence or structural similarity from UniProtKB).
GO:0006693;	Biological process: prostaglandin metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000488; Death.
IPR011029; DEATH-like.
IPR001368; TNFR_Cys_rich_reg.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.533.10; DEATH_like; 1.

Pfam

PF00531; Death; 1.
PF00020; TNFR_c6; 3.
Pfam graphical view of domain structure.

SMART

SM00005; DEATH; 1.
SM00208; TNFR; 4.
SMART graphical view of domain structure.

PROSITE

PS50017; DEATH_DOMAIN; 1.
PS00652; TNFR_NGFR_1; 3.
PS50050; TNFR_NGFR_2; 3.
PROSITE graphical view of domain structure (profiles).

Other

SWISS-3DIMAGE

P19438.

Proteomic databases

PRIDE

P19438; -.

Genome annotation databases

Ensembl

ENSG00000067182; Homo sapiens. [Contig view]

GeneID

7132; -.

KEGG

hsa:7132; -.

Phylogenomic databases

HOGENOM

P19438; -.

HOVERGEN

P19438; -.

OMA

P19438; CGCRKNQ.

Other

NextBio

27905; -.

PMAP-CutDB

P19438; -.

SOURCE

TNFRSF1A; Homo sapiens.

ProtoNet

P19438.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Amyloidosis; Apoptosis; Cell membrane; Cleavage on pair of basic residues; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Host-virus interaction; Membrane; Polymorphism; Receptor; Repeat; Secreted; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`
`CHAIN`	`22 455`	`434`	`Tumor necrosis factor receptor superfamily member 1A, membrane form.`	`PRO_0000034543`
`CHAIN`	`41 291`	`251`	`Tumor necrosis factor-binding protein 1.`	`PRO_0000034544`
`TOPO_DOM`	`22 211`	`190`	`Extracellular (Potential).`
`TRANSMEM`	`212 234`	`23`	`Potential.`
`TOPO_DOM`	`235 455`	`221`	`Cytoplasmic (Potential).`
`REPEAT`	`43 82`	`40`	`TNFR-Cys 1.`
`REPEAT`	`83 125`	`43`	`TNFR-Cys 2.`
`REPEAT`	`126 166`	`41`	`TNFR-Cys 3.`
`REPEAT`	`167 196`	`30`	`TNFR-Cys 4.`
`DOMAIN`	`356 441`	`86`	`Death.`
`REGION`	`338 348`	`11`	`N-SMase activation domain (NSD).`
`CARBOHYD`	`54 54`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`145 145`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`151 151`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`44 58`
`DISULFID`	`59 72`
`DISULFID`	`62 81`
`DISULFID`	`84 99`
`DISULFID`	`102 117`
`DISULFID`	`105 125`
`DISULFID`	`127 143`
`DISULFID`	`146 158`
`DISULFID`	`149 166`
`DISULFID`	`168 179`
`DISULFID`	`182 195`
`DISULFID`	`185 191`
`VAR_SEQ`	`1 232`		`Missing (in isoform 3).`	`VSP_037154`
`VAR_SEQ`	`1 108`		`Missing (in isoform 2).`	`VSP_037153`
`VARIANT`	`51 51`	`1`	`H -> Q (in FHF).`	`VAR_019329 [3D]`
`VARIANT`	`59 59`	`1`	`C -> R (in FHF).`	`VAR_013410 [3D]`
`VARIANT`	`59 59`	`1`	`C -> S (in FHF).`	`VAR_019302 [3D]`
`VARIANT`	`62 62`	`1`	`C -> G (in FHF).`	`VAR_019303 [3D]`
`VARIANT`	`62 62`	`1`	`C -> Y (in FHF).`	`VAR_013411 [3D]`
`VARIANT`	`75 75`	`1`	`P -> L (in FHF; may be a polymorphism; dbSNP:rs4149637 [NCBI]).`	`VAR_019330 [3D]`
`VARIANT`	`79 79`	`1`	`T -> M (in FHF).`	`VAR_013412 [3D]`
`VARIANT`	`81 81`	`1`	`C -> F (in FHF).`	`VAR_013413 [3D]`
`VARIANT`	`99 99`	`1`	`C -> S (in FHF).`	`VAR_019304 [3D]`
`VARIANT`	`115 115`	`1`	`S -> G (in FHF).`	`VAR_019331 [3D]`
`VARIANT`	`117 117`	`1`	`C -> R (in FHF).`	`VAR_013414 [3D]`
`VARIANT`	`117 117`	`1`	`C -> Y (in FHF).`	`VAR_013415 [3D]`
`VARIANT`	`121 121`	`1`	`R -> P (in FHF).`	`VAR_019305 [3D]`
`VARIANT`	`121 121`	`1`	`R -> Q (in FHF; may be a polymorphism; dbSNP:rs4149584 [NCBI]).`	`VAR_019332 [3D]`
`VARIANT`	`305 305`	`1`	`P -> T (in dbSNP:rs1804532 [NCBI]).`	`VAR_011813`
`CONFLICT`	`13 13`		`L -> LILPQ (in Ref. 8; BAG51763).`
`CONFLICT`	`255 255`		`K -> E (in Ref. 8; BAG37891).`
`CONFLICT`	`286 286`		`S -> G (in Ref. 8; BAG51763).`
`CONFLICT`	`394 394`		`R -> L (in Ref. 8; BAF83777).`
`CONFLICT`	`412 412`		`Missing (in Ref. 5; AAA36756).`
`CONFLICT`	`443 446`		`GPAA -> APP (in Ref. 5; AAA36756).`
`STRAND`	`48 50`	`3`
`STRAND`	`58 60`	`3`
`STRAND`	`66 70`	`5`
`STRAND`	`80 83`	`4`
`STRAND`	`92 94`	`3`
`HELIX`	`107 109`	`3`
`STRAND`	`112 115`	`4`
`STRAND`	`124 126`	`3`
`STRAND`	`131 137`	`7`
`STRAND`	`140 145`	`6`
`STRAND`	`152 156`	`5`
`STRAND`	`165 168`	`4`
`STRAND`	`172 175`	`4`
`STRAND`	`178 181`	`4`
`HELIX`	`182 184`	`3`
`HELIX`	`192 195`	`4`
`HELIX`	`357 365`	`9`
`HELIX`	`371 378`	`8`
`HELIX`	`382 391`	`10`
`HELIX`	`396 410`	`15`
`HELIX`	`417 427`	`11`
`HELIX`	`431 441`	`11`

Sequence information

Length: 455 AA [This is the length of the unprocessed precursor]

Molecular weight: 50495 Da [This is the MW of the unprocessed precursor]

CRC64: 4CEFBA96D03B8225 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLSTVPDLL LPLVLLELLV GIYPSGVIGL VPHLGDREKR DSVCPQGKYI HPQNNSICCT 

        70         80         90        100        110        120 
KCHKGTYLYN DCPGPGQDTD CRECESGSFT ASENHLRHCL SCSKCRKEMG QVEISSCTVD 

       130        140        150        160        170        180 
RDTVCGCRKN QYRHYWSENL FQCFNCSLCL NGTVHLSCQE KQNTVCTCHA GFFLRENECV 

       190        200        210        220        230        240 
SCSNCKKSLE CTKLCLPQIE NVKGTEDSGT TVLLPLVIFF GLCLLSLLFI GLMYRYQRWK 

       250        260        270        280        290        300 
SKLYSIVCGK STPEKEGELE GTTTKPLAPN PSFSPTPGFT PTLGFSPVPS STFTSSSTYT 

       310        320        330        340        350        360 
PGDCPNFAAP RREVAPPYQG ADPILATALA SDPIPNPLQK WEDSAHKPQS LDTDDPATLY 

       370        380        390        400        410        420 
AVVENVPPLR WKEFVRRLGL SDHEIDRLEL QNGRCLREAQ YSMLATWRRR TPRREATLEL 

       430        440        450 
LGRVLRDMDL LGCLEDIEEA LCGPAALPPA PSLLR

P19438 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools