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Database: UniProt
Entry: Q92956
LinkDB: Q92956
Original site: Q92956 
ID   TNR14_HUMAN             Reviewed;         283 AA.
AC   Q92956; B3KW30; B9DI89; Q6IB95; Q8N634; Q8WXR1; Q96J31; Q9UM65;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 3.
DT   01-OCT-2014, entry version 161.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 14;
DE   AltName: Full=Herpes virus entry mediator A;
DE            Short=Herpesvirus entry mediator A;
DE            Short=HveA;
DE   AltName: Full=Tumor necrosis factor receptor-like 2;
DE            Short=TR2;
DE   AltName: CD_antigen=CD270;
DE   Flags: Precursor;
GN   Name=TNFRSF14; Synonyms=HVEA, HVEM; ORFNames=UNQ329/PRO509;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A RECEPTOR FOR
RP   HHV-1.
RC   TISSUE=Cervix adenocarcinoma;
RX   PubMed=8898196; DOI=10.1016/S0092-8674(00)81363-X;
RA   Montgomery R.I., Warner M.S., Lum B.J., Spear P.G.;
RT   "Herpes simplex virus-1 entry into cells mediated by a novel member of
RT   the TNF/NGF receptor family.";
RL   Cell 87:427-436(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9162061; DOI=10.1074/jbc.272.22.14272;
RA   Kwon B.S., Tan K.B., Ni J., Oh K.-O., Lee Z.H., Kim K.K., Kim Y.-J.,
RA   Wang S., Gentz R., Yu G.-L., Harrop J., Lyn S.D., Silverman C.,
RA   Porter T.G., Truneh A., Young P.R.;
RT   "A newly identified member of the tumor necrosis factor receptor
RT   superfamily with a wide tissue distribution and involvement in
RT   lymphocyte activation.";
RL   J. Biol. Chem. 272:14272-14276(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Zhang W., Wan T., Cao X.;
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-17 AND
RP   ILE-241.
RX   PubMed=11756979; DOI=10.1086/338116;
RA   Struyf F., Posavad C.M., Keyaerts E., Van Ranst M., Corey L.,
RA   Spear P.G.;
RT   "Search for polymorphisms in the genes for herpesvirus entry mediator,
RT   Nectin-1, and Nectin-2 in immune seronegative individuals.";
RL   J. Infect. Dis. 185:36-44(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Spleen;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   ARG-17.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-17; THR-117;
RP   GLU-174 AND ILE-241.
RG   NIEHS SNPs program;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   PROTEIN SEQUENCE OF 39-53.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [13]
RP   INTERACTION WITH TRAF2 AND TRAF5.
RX   PubMed=9153189; DOI=10.1074/jbc.272.21.13471;
RA   Hsu H., Solovyev I., Colombero A., Elliott R., Kelley M., Boyle W.J.;
RT   "ATAR, a novel tumor necrosis factor receptor family member, signals
RT   through TRAF2 and TRAF5.";
RL   J. Biol. Chem. 272:13471-13474(1997).
RN   [14]
RP   INTERACTION WITH TRAF3 AND TRAF5.
RX   PubMed=9162022; DOI=10.1074/jbc.272.22.14029;
RA   Marsters S.A., Ayres T.M., Skubatch M., Gray C.L., Rothe M.,
RA   Ashkenazi A.;
RT   "Herpesvirus entry mediator, a member of the tumor necrosis factor
RT   receptor (TNFR) family, interacts with members of the TNFR-associated
RT   factor family and activates the transcription factors NF-kappaB and
RT   AP-1.";
RL   J. Biol. Chem. 272:14029-14032(1997).
RN   [15]
RP   INTERACTION WITH HHV-1 AND HHV-2 GLYCOPROTEIN D.
RX   PubMed=9696799;
RA   Krummenacher C., Nicola A.V., Whitbeck J.C., Lou H., Hou W.,
RA   Lambris J.D., Geraghty R.J., Spear P.G., Cohen G.H., Eisenberg R.J.;
RT   "Herpes simplex virus glycoprotein D can bind to poliovirus receptor-
RT   related protein 1 or herpesvirus entry mediator, two structurally
RT   unrelated mediators of virus entry.";
RL   J. Virol. 72:7064-7074(1998).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 39-200 IN COMPLEX WITH HUMAN
RP   HERPESVIRUS 1 GLYCOPROTEIN.
RX   PubMed=11511370; DOI=10.1016/S1097-2765(01)00298-2;
RA   Carfi A., Willis S.H., Whitbeck J.C., Krummenacher C., Cohen G.H.,
RA   Eisenberg R.J., Wiley D.C.;
RT   "Herpes simplex virus glycoprotein D bound to the human receptor
RT   HveA.";
RL   Mol. Cell 8:169-179(2001).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-137 IN COMPLEX WITH BTLA,
RP   AND GLYCOSYLATION AT ASN-110.
RX   PubMed=16169851; DOI=10.1074/jbc.M507629200;
RA   Compaan D.M., Gonzalez L.C., Tom I., Loyet K.M., Eaton D.,
RA   Hymowitz S.G.;
RT   "Attenuating lymphocyte activity: the crystal structure of the BTLA-
RT   HVEM complex.";
RL   J. Biol. Chem. 280:39553-39561(2005).
CC   -!- FUNCTION: Receptor for BTLA. Receptor for TNFSF14/LIGHT and
CC       homotrimeric TNFSF1/lymphotoxin-alpha. Involved in lymphocyte
CC       activation. Plays an important role in HSV pathogenesis because it
CC       enhanced the entry of several wild-type HSV strains of both
CC       serotypes into CHO cells, and mediated HSV entry into activated
CC       human T-cells. {ECO:0000269|PubMed:8898196}.
CC   -!- SUBUNIT: Interacts with TRAF2, TRAF3 and TRAF5. Interacts with
CC       herpes simplex virus 1 (HHV-1) and herpes simplex virus 1 (HHV-2)
CC       envelope glycoprotein D; functions as an entry receptor for these
CC       viruses. {ECO:0000269|PubMed:11511370,
CC       ECO:0000269|PubMed:16169851, ECO:0000269|PubMed:9153189,
CC       ECO:0000269|PubMed:9162022, ECO:0000269|PubMed:9696799}.
CC   -!- INTERACTION:
CC       O43557:TNFSF14; NbExp=2; IntAct=EBI-1056653, EBI-524131;
CC       Q12933-2:TRAF2; NbExp=4; IntAct=EBI-1056653, EBI-355760;
CC       O00463:TRAF5; NbExp=5; IntAct=EBI-1056653, EBI-523498;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q92956-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92956-2; Sequence=VSP_054186;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with the highest expression
CC       in lung, spleen and thymus.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16169851}.
CC   -!- SIMILARITY: Contains 3 TNFR-Cys repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00206}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/tnfrsf14/";
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DR   EMBL; U70321; AAB58354.1; -; mRNA.
DR   EMBL; U81232; AAD00505.1; -; mRNA.
DR   EMBL; AF153978; AAF75588.1; -; mRNA.
DR   EMBL; AF373877; AAL47717.1; -; mRNA.
DR   EMBL; AF373878; AAL47718.1; -; mRNA.
DR   EMBL; AY358879; AAQ89238.1; -; mRNA.
DR   EMBL; AK124010; BAG53992.1; -; mRNA.
DR   EMBL; CR456909; CAG33190.1; -; mRNA.
DR   EMBL; AY466111; AAR23264.1; -; Genomic_DNA.
DR   EMBL; AL139246; CAX30824.1; -; Genomic_DNA.
DR   EMBL; CH471183; EAW56089.1; -; Genomic_DNA.
DR   EMBL; CH471183; EAW56090.1; -; Genomic_DNA.
DR   EMBL; BC002794; AAH02794.1; -; mRNA.
DR   EMBL; BC029848; AAH29848.1; -; mRNA.
DR   CCDS; CCDS44046.1; -. [Q92956-1]
DR   RefSeq; NP_003811.2; NM_003820.2. [Q92956-1]
DR   UniGene; Hs.512898; -.
DR   PDB; 1JMA; X-ray; 2.65 A; B=39-199.
DR   PDB; 2AW2; X-ray; 2.80 A; B/Y=39-142.
DR   PDB; 4FHQ; X-ray; 2.25 A; A=39-162.
DR   PDBsum; 1JMA; -.
DR   PDBsum; 2AW2; -.
DR   PDBsum; 4FHQ; -.
DR   ProteinModelPortal; Q92956; -.
DR   SMR; Q92956; 39-200.
DR   BioGrid; 114298; 30.
DR   DIP; DIP-34779N; -.
DR   DIP; DIP-6233N; -.
DR   IntAct; Q92956; 29.
DR   MINT; MINT-208002; -.
DR   STRING; 9606.ENSP00000347948; -.
DR   GuidetoPHARMACOLOGY; 1887; -.
DR   DMDM; 13878821; -.
DR   PaxDb; Q92956; -.
DR   PRIDE; Q92956; -.
DR   DNASU; 8764; -.
DR   Ensembl; ENST00000355716; ENSP00000347948; ENSG00000157873. [Q92956-1]
DR   GeneID; 8764; -.
DR   KEGG; hsa:8764; -.
DR   UCSC; uc001ajr.3; human. [Q92956-1]
DR   CTD; 8764; -.
DR   GeneCards; GC01P002487; -.
DR   HGNC; HGNC:11912; TNFRSF14.
DR   HPA; CAB026150; -.
DR   HPA; CAB030007; -.
DR   HPA; HPA006404; -.
DR   MIM; 602746; gene.
DR   neXtProt; NX_Q92956; -.
DR   PharmGKB; PA36605; -.
DR   eggNOG; NOG40150; -.
DR   HOGENOM; HOG000065766; -.
DR   HOVERGEN; HBG072084; -.
DR   InParanoid; Q92956; -.
DR   KO; K05152; -.
DR   OMA; SPGHFCI; -.
DR   PhylomeDB; Q92956; -.
DR   TreeFam; TF331157; -.
DR   Reactome; REACT_19344; Costimulation by the CD28 family.
DR   SignaLink; Q92956; -.
DR   ChiTaRS; TNFRSF14; human.
DR   EvolutionaryTrace; Q92956; -.
DR   GeneWiki; TNFRSF14; -.
DR   GenomeRNAi; 8764; -.
DR   NextBio; 32872; -.
DR   PRO; PR:Q92956; -.
DR   ArrayExpress; Q92956; -.
DR   Bgee; Q92956; -.
DR   CleanEx; HS_TNFRSF14; -.
DR   Genevestigator; Q92956; -.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IC:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; TAS:ProtInc.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0046642; P:negative regulation of alpha-beta T cell proliferation; IEA:Ensembl.
DR   GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
DR   GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:GOC.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR022332; TNFR_14.
DR   Pfam; PF00020; TNFR_c6; 1.
DR   PRINTS; PR01965; TNFACTORR14.
DR   SMART; SM00208; TNFR; 3.
DR   PROSITE; PS00652; TNFR_NGFR_1; 1.
DR   PROSITE; PS50050; TNFR_NGFR_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Host cell receptor for virus entry; Host-virus interaction; Membrane;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     38       {ECO:0000269|PubMed:15340161}.
FT   CHAIN        39    283       Tumor necrosis factor receptor
FT                                superfamily member 14.
FT                                /FTId=PRO_0000034590.
FT   TOPO_DOM     39    202       Extracellular. {ECO:0000255}.
FT   TRANSMEM    203    223       Helical. {ECO:0000255}.
FT   TOPO_DOM    224    283       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       42     75       TNFR-Cys 1.
FT   REPEAT       78    119       TNFR-Cys 2.
FT   REPEAT      121    162       TNFR-Cys 3.
FT   CARBOHYD    110    110       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16169851}.
FT   CARBOHYD    173    173       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     42     53
FT   DISULFID     54     67
FT   DISULFID     57     75
FT   DISULFID     78     93
FT   DISULFID     96    111
FT   DISULFID     99    119
FT   DISULFID    121    138
FT   DISULFID    127    135
FT   VAR_SEQ       1    100       MEPPGDWGPPPWRSTPKTDVLRLVLYLTFLGAPCYAPALPS
FT                                CKEDEYPVGSECCPKCSPGYRVKEACGELTGTVCEPCPPGT
FT                                YIAHLNGLSKCLQCQMCD -> MVSRPPRTPLSPSSWT
FT                                (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054186.
FT   VARIANT      17     17       K -> R (in dbSNP:rs4870).
FT                                {ECO:0000269|PubMed:11756979,
FT                                ECO:0000269|PubMed:12975309,
FT                                ECO:0000269|Ref.8}.
FT                                /FTId=VAR_013007.
FT   VARIANT     117    117       A -> T (in dbSNP:rs2234163).
FT                                {ECO:0000269|Ref.8}.
FT                                /FTId=VAR_018955.
FT   VARIANT     174    174       G -> E (in dbSNP:rs11573986).
FT                                {ECO:0000269|Ref.8}.
FT                                /FTId=VAR_018956.
FT   VARIANT     241    241       V -> I (in dbSNP:rs2234167).
FT                                {ECO:0000269|PubMed:11756979,
FT                                ECO:0000269|Ref.8}.
FT                                /FTId=VAR_013440.
FT   CONFLICT    135    135       C -> R (in Ref. 10; AAH29848).
FT                                {ECO:0000305}.
FT   STRAND       46     49
FT   STRAND       52     55
FT   STRAND       61     65
FT   STRAND       69     71
FT   STRAND       74     77
FT   STRAND       86     88
FT   HELIX       101    103
FT   STRAND      105    109
FT   STRAND      113    115
FT   STRAND      118    121
FT   STRAND      125    131
FT   STRAND      134    140
SQ   SEQUENCE   283 AA;  30392 MW;  46CE13C2C70242C1 CRC64;
     MEPPGDWGPP PWRSTPKTDV LRLVLYLTFL GAPCYAPALP SCKEDEYPVG SECCPKCSPG
     YRVKEACGEL TGTVCEPCPP GTYIAHLNGL SKCLQCQMCD PAMGLRASRN CSRTENAVCG
     CSPGHFCIVQ DGDHCAACRA YATSSPGQRV QKGGTESQDT LCQNCPPGTF SPNGTLEECQ
     HQTKCSWLVT KAGAGTSSSH WVWWFLSGSL VIVIVCSTVG LIICVKRRKP RGDVVKVIVS
     VQRKRQEAEG EATVIEALQA PPDVTTVAVE ETIPSFTGRS PNH
//
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