ID TNR21_HUMAN Reviewed; 655 AA. AC O75509; B2RDI9; Q0D2P5; Q96D86; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 13-FEB-2019, entry version 177. DE RecName: Full=Tumor necrosis factor receptor superfamily member 21; DE AltName: Full=Death receptor 6; DE AltName: CD_antigen=CD358; DE Flags: Precursor; GN Name=TNFRSF21; Synonyms=DR6; ORFNames=UNQ437/PRO868; 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], FUNCTION, TISSUE SPECIFICITY, AND RP INTERACTION WITH TRADD. RX PubMed=9714541; DOI=10.1016/S0014-5793(98)00791-1; RA Pan G., Bauer J.H., Haridas V., Wang S., Liu D., Yu G., Vincenz C., RA Aggarwal B.B., Ni J., Dixit V.M.; RT "Identification and functional characterization of DR6, a novel death RT domain-containing TNF receptor."; RL FEBS Lett. 431:351-356(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Colon, and Eye; 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 [7] RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-82; ASN-141; ASN-252; RP ASN-257; ASN-278 AND ASN-289, MUTAGENESIS OF ASN-82; ASN-141; ASN-252; RP ASN-257; ASN-278 AND ASN-289, INDUCTION BY TNF, AND PALMITOYLATION AT RP CYS-368. RX PubMed=19654028; DOI=10.1016/j.bbamcr.2009.07.008; RA Klima M., Zajedova J., Doubravska L., Andera L.; RT "Functional analysis of the posttranslational modifications of the RT death receptor 6."; RL Biochim. Biophys. Acta 1793:1579-1587(2009). RN [8] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=21725297; DOI=10.1038/nm.2373; RA Mi S., Lee X., Hu Y., Ji B., Shao Z., Yang W., Huang G., Walus L., RA Rhodes K., Gong B.J., Miller R.H., Pepinsky R.B.; RT "Death receptor 6 negatively regulates oligodendrocyte survival, RT maturation and myelination."; RL Nat. Med. 17:816-821(2011). RN [9] RP FUNCTION. RX PubMed=22761420; DOI=10.1074/jbc.M112.362038; RA Zeng L., Li T., Xu D.C., Liu J., Mao G., Cui M.Z., Fu X., Xu X.; RT "Death receptor 6 induces apoptosis not through type I or type II RT pathways, but via a unique mitochondria-dependent pathway by RT interacting with Bax protein."; RL J. Biol. Chem. 287:29125-29133(2012). RN [10] RP INDUCTION, TISSUE SPECIFICITY, AND INTERACTION WITH NGFR. RX PubMed=23559013; DOI=10.1038/cddis.2013.110; RA Hu Y., Lee X., Shao Z., Apicco D., Huang G., Gong B.J., Pepinsky R.B., RA Mi S.; RT "A DR6/p75(NTR) complex is responsible for beta-amyloid-induced RT cortical neuron death."; RL Cell Death Dis. 4:E579-E579(2013). RN [11] RP STRUCTURE BY NMR OF 562-655. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the carboxyl-terminal CARD-like domain in human RT TNFR-related death receptor-6."; RL Submitted (DEC-2006) to the PDB data bank. RN [12] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 42-218, AND DISULFIDE BOND. RX PubMed=21463639; DOI=10.1016/j.jmb.2011.03.048; RA Kuester M., Kemmerzehl S., Dahms S.O., Roeser D., Than M.E.; RT "The crystal structure of death receptor 6 (DR6): a potential receptor RT of the amyloid precursor protein (APP)."; RL J. Mol. Biol. 409:189-201(2011). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 42-349, DISULFIDE BOND, AND RP GLYCOSYLATION. RX PubMed=22525750; DOI=10.1107/S0907444912004490; RA Ru H., Zhao L., Ding W., Jiao L., Shaw N., Liang W., Zhang L., RA Hung L.W., Matsugaki N., Wakatsuki S., Liu Z.J.; RT "S-SAD phasing study of death receptor 6 and its solution conformation RT revealed by SAXS."; RL Acta Crystallogr. D 68:521-530(2012). CC -!- FUNCTION: Promotes apoptosis, possibly via a pathway that involves CC the activation of NF-kappa-B. Can also promote apoptosis mediated CC by BAX and by the release of cytochrome c from the mitochondria CC into the cytoplasm. Plays a role in neuronal apoptosis, including CC apoptosis in response to amyloid peptides derived from APP, and is CC required for both normal cell body death and axonal pruning. CC Trophic-factor deprivation triggers the cleavage of surface APP by CC beta-secretase to release sAPP-beta which is further cleaved to CC release an N-terminal fragment of APP (N-APP). N-APP binds CC TNFRSF21; this triggers caspase activation and degeneration of CC both neuronal cell bodies (via caspase-3) and axons (via caspase- CC 6). Negatively regulates oligodendrocyte survival, maturation and CC myelination. Plays a role in signaling cascades triggered by CC stimulation of T-cell receptors, in the adaptive immune response CC and in the regulation of T-cell differentiation and proliferation. CC Negatively regulates T-cell responses and the release of cytokines CC such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively CC regulates the production of IgG, IgM and IgM in response to CC antigens. May inhibit the activation of JNK in response to T-cell CC stimulation. {ECO:0000269|PubMed:21725297, CC ECO:0000269|PubMed:22761420, ECO:0000269|PubMed:9714541}. CC -!- SUBUNIT: Interacts with N-APP (By similarity). Associates with CC TRADD. Interacts with NGFR. {ECO:0000250, CC ECO:0000269|PubMed:23559013, ECO:0000269|PubMed:9714541}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19654028}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:19654028}. CC -!- TISSUE SPECIFICITY: Detected in fetal spinal cord and in brain CC neurons, with higher levels in brain from Alzheimer disease CC patients (at protein level). Highly expressed in heart, brain, CC placenta, pancreas, lymph node, thymus and prostate. Detected at CC lower levels in lung, skeletal muscle, kidney, testis, uterus, CC small intestine, colon, spleen, bone marrow and fetal liver. Very CC low levels were found in adult liver and peripheral blood CC leukocytes. {ECO:0000269|PubMed:21725297, CC ECO:0000269|PubMed:23559013, ECO:0000269|PubMed:9714541}. CC -!- INDUCTION: Up-regulated by TNF. {ECO:0000269|PubMed:19654028, CC ECO:0000269|PubMed:23559013}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-25 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH10241.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF068868; AAC34583.1; -; mRNA. DR EMBL; AY358304; AAQ88671.1; -; mRNA. DR EMBL; AK315560; BAG37936.1; -; mRNA. DR EMBL; BT007420; AAP36088.1; -; mRNA. DR EMBL; AL096801; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC010241; AAH10241.1; ALT_INIT; mRNA. DR EMBL; BC017730; AAH17730.1; -; mRNA. DR EMBL; BC021572; AAH21572.1; -; mRNA. DR CCDS; CCDS4921.1; -. DR RefSeq; NP_055267.1; NM_014452.4. DR UniGene; Hs.443577; -. DR PDB; 2DBH; NMR; -; A=567-655. DR PDB; 3QO4; X-ray; 2.20 A; A=42-218. DR PDB; 3U3P; X-ray; 2.09 A; A=42-348. DR PDB; 3U3Q; X-ray; 2.70 A; A=42-348. DR PDB; 3U3S; X-ray; 2.70 A; A=42-348. DR PDB; 3U3T; X-ray; 3.21 A; A=42-348. DR PDB; 3U3V; X-ray; 2.96 A; A=42-348. DR PDBsum; 2DBH; -. DR PDBsum; 3QO4; -. DR PDBsum; 3U3P; -. DR PDBsum; 3U3Q; -. DR PDBsum; 3U3S; -. DR PDBsum; 3U3T; -. DR PDBsum; 3U3V; -. DR ProteinModelPortal; O75509; -. DR SMR; O75509; -. DR BioGrid; 118090; 9. DR CORUM; O75509; -. DR DIP; DIP-53299N; -. DR IntAct; O75509; 8. DR MINT; O75509; -. DR STRING; 9606.ENSP00000296861; -. DR GlyConnect; 1981; -. DR iPTMnet; O75509; -. DR PhosphoSitePlus; O75509; -. DR SwissPalm; O75509; -. DR BioMuta; TNFRSF21; -. DR EPD; O75509; -. DR jPOST; O75509; -. DR MaxQB; O75509; -. DR PaxDb; O75509; -. DR PeptideAtlas; O75509; -. DR PRIDE; O75509; -. DR ProteomicsDB; 50058; -. DR DNASU; 27242; -. DR Ensembl; ENST00000296861; ENSP00000296861; ENSG00000146072. DR GeneID; 27242; -. DR KEGG; hsa:27242; -. DR UCSC; uc003oyv.5; human. DR CTD; 27242; -. DR DisGeNET; 27242; -. DR EuPathDB; HostDB:ENSG00000146072.6; -. DR GeneCards; TNFRSF21; -. DR HGNC; HGNC:13469; TNFRSF21. DR HPA; CAB009805; -. DR HPA; HPA006746; -. DR MIM; 605732; gene. DR neXtProt; NX_O75509; -. DR OpenTargets; ENSG00000146072; -. DR PharmGKB; PA37775; -. DR eggNOG; ENOG410IHQ6; Eukaryota. DR eggNOG; ENOG410YYKW; LUCA. DR GeneTree; ENSGT00940000156212; -. DR HOGENOM; HOG000136852; -. DR HOVERGEN; HBG054218; -. DR InParanoid; O75509; -. DR KO; K05157; -. DR OMA; LMEDTAQ; -. DR OrthoDB; 869160at2759; -. DR PhylomeDB; O75509; -. DR TreeFam; TF331157; -. DR Reactome; R-HSA-1989781; PPARA activates gene expression. DR SIGNOR; O75509; -. DR ChiTaRS; TNFRSF21; human. DR EvolutionaryTrace; O75509; -. DR GeneWiki; TNFRSF21; -. DR GenomeRNAi; 27242; -. DR PRO; PR:O75509; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000146072; Expressed in 223 organ(s), highest expression level in C1 segment of cervical spinal cord. DR ExpressionAtlas; O75509; baseline and differential. DR Genevisible; O75509; HS. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB. DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB. DR GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl. DR GO; GO:0001783; P:B cell apoptotic process; ISS:UniProtKB. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB. DR GO; GO:0006959; P:humoral immune response; ISS:UniProtKB. DR GO; GO:0042552; P:myelination; ISS:UniProtKB. DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISS:UniProtKB. DR GO; GO:2001180; P:negative regulation of interleukin-10 secretion; ISS:UniProtKB. DR GO; GO:2000666; P:negative regulation of interleukin-13 secretion; ISS:UniProtKB. DR GO; GO:2000663; P:negative regulation of interleukin-5 secretion; ISS:UniProtKB. DR GO; GO:0031642; P:negative regulation of myelination; IMP:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB. DR GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome. DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; ISS:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB. DR CDD; cd08778; Death_TNFRSF21; 1. DR CDD; cd10583; TNFRSF21; 1. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR000488; Death_domain. DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg. DR InterPro; IPR022330; TNFR_21. DR InterPro; IPR034037; TNFRSF21_death. DR InterPro; IPR034034; TNFRSF21_N. DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like. DR Pfam; PF00531; Death; 1. DR Pfam; PF00020; TNFR_c6; 3. DR PRINTS; PR01971; TNFACTORR21. DR SMART; SM00005; DEATH; 1. DR SMART; SM01411; Ephrin_rec_like; 2. DR SMART; SM00208; TNFR; 4. DR SUPFAM; SSF47986; SSF47986; 1. DR PROSITE; PS50017; DEATH_DOMAIN; 1. DR PROSITE; PS00652; TNFR_NGFR_1; 1. DR PROSITE; PS50050; TNFR_NGFR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Apoptosis; Cell membrane; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 41 {ECO:0000255}. FT CHAIN 42 655 Tumor necrosis factor receptor FT superfamily member 21. FT /FTId=PRO_0000034602. FT TOPO_DOM 42 349 Extracellular. {ECO:0000255}. FT TRANSMEM 350 370 Helical. {ECO:0000255}. FT TOPO_DOM 371 655 Cytoplasmic. {ECO:0000255}. FT REPEAT 50 88 TNFR-Cys 1. FT REPEAT 90 131 TNFR-Cys 2. FT REPEAT 133 167 TNFR-Cys 3. FT REPEAT 170 211 TNFR-Cys 4. FT DOMAIN 415 498 Death. {ECO:0000255|PROSITE- FT ProRule:PRU00064}. FT LIPID 368 368 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:19654028}. FT CARBOHYD 82 82 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19654028}. FT CARBOHYD 141 141 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19654028}. FT CARBOHYD 252 252 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19654028}. FT CARBOHYD 257 257 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19654028}. FT CARBOHYD 278 278 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19654028}. FT CARBOHYD 289 289 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19654028}. FT DISULFID 67 80 FT DISULFID 70 88 FT DISULFID 91 106 FT DISULFID 109 123 FT DISULFID 113 131 FT DISULFID 133 144 FT DISULFID 150 168 FT DISULFID 171 186 FT DISULFID 192 211 FT MUTAGEN 82 82 N->Q: Abolishes one glycosylation site FT and reduces total N-glycosylation; when FT associated with Q-252; Q-278 and Q-289. FT {ECO:0000269|PubMed:19654028}. FT MUTAGEN 141 141 N->Q: Abolishes one glycosylation site FT and reduces total N-glycosylation; when FT associated with Q-82; Q-252; Q-278 and Q- FT 289. {ECO:0000269|PubMed:19654028}. FT MUTAGEN 252 252 N->Q: Abolishes one glycosylation site FT and reduces total N-glycosylation; when FT associated with Q-278 and Q-289. FT {ECO:0000269|PubMed:19654028}. FT MUTAGEN 257 257 N->Q: Abolishes one glycosylation site FT and reduces total N-glycosylation; when FT associated with Q-82; Q-141; Q-252; Q-278 FT and Q-289. {ECO:0000269|PubMed:19654028}. FT MUTAGEN 278 278 N->Q: Abolishes one glycosylation site FT and reduces total N-glycosylation. FT Abolishes one glycosylation site and FT reduces total N-glycosylation; when FT associated with Q-82; Q-141; Q-252; Q-257 FT and Q-289. {ECO:0000269|PubMed:19654028}. FT MUTAGEN 289 289 N->Q: Abolishes one glycosylation site FT and reduces total N-glycosylation; when FT associated with Q-278. FT {ECO:0000269|PubMed:19654028}. FT MUTAGEN 368 368 C->V: Abolishes palmitoylation. FT STRAND 53 57 {ECO:0000244|PDB:3U3P}. FT TURN 59 61 {ECO:0000244|PDB:3U3P}. FT STRAND 64 68 {ECO:0000244|PDB:3U3P}. FT STRAND 74 78 {ECO:0000244|PDB:3U3P}. FT STRAND 82 84 {ECO:0000244|PDB:3U3T}. FT STRAND 87 90 {ECO:0000244|PDB:3U3P}. FT STRAND 99 101 {ECO:0000244|PDB:3U3V}. FT STRAND 118 121 {ECO:0000244|PDB:3U3P}. FT STRAND 130 132 {ECO:0000244|PDB:3U3P}. FT STRAND 137 140 {ECO:0000244|PDB:3U3P}. FT STRAND 143 146 {ECO:0000244|PDB:3U3P}. FT STRAND 154 158 {ECO:0000244|PDB:3U3P}. FT STRAND 162 164 {ECO:0000244|PDB:3U3P}. FT STRAND 167 170 {ECO:0000244|PDB:3U3P}. FT STRAND 181 183 {ECO:0000244|PDB:3U3P}. FT HELIX 193 195 {ECO:0000244|PDB:3U3P}. FT STRAND 198 201 {ECO:0000244|PDB:3U3P}. FT STRAND 205 207 {ECO:0000244|PDB:3U3P}. FT STRAND 210 212 {ECO:0000244|PDB:3U3P}. FT STRAND 571 573 {ECO:0000244|PDB:2DBH}. FT HELIX 579 591 {ECO:0000244|PDB:2DBH}. FT HELIX 598 606 {ECO:0000244|PDB:2DBH}. FT HELIX 609 616 {ECO:0000244|PDB:2DBH}. FT HELIX 621 635 {ECO:0000244|PDB:2DBH}. FT HELIX 637 650 {ECO:0000244|PDB:2DBH}. FT HELIX 652 654 {ECO:0000244|PDB:2DBH}. SQ SEQUENCE 655 AA; 71845 MW; 48939391C4852A33 CRC64; MGTSPSSSTA LASCSRIARR ATATMIAGSL LLLGFLSTTT AQPEQKASNL IGTYRHVDRA TGQVLTCDKC PAGTYVSEHC TNTSLRVCSS CPVGTFTRHE NGIEKCHDCS QPCPWPMIEK LPCAALTDRE CTCPPGMFQS NATCAPHTVC PVGWGVRKKG TETEDVRCKQ CARGTFSDVP SSVMKCKAYT DCLSQNLVVI KPGTKETDNV CGTLPSFSSS TSPSPGTAIF PRPEHMETHE VPSSTYVPKG MNSTESNSSA SVRPKVLSSI QEGTVPDNTS SARGKEDVNK TLPNLQVVNH QQGPHHRHIL KLLPSMEATG GEKSSTPIKG PKRGHPRQNL HKHFDINEHL PWMIVLFLLL VLVVIVVCSI RKSSRTLKKG PRQDPSAIVE KAGLKKSMTP TQNREKWIYY CNGHGIDILK LVAAQVGSQW KDIYQFLCNA SEREVAAFSN GYTADHERAY AALQHWTIRG PEASLAQLIS ALRQHRRNDV VEKIRGLMED TTQLETDKLA LPMSPSPLSP SPIPSPNAKL ENSALLTVEP SPQDKNKGFF VDESEPLLRC DSTSSGSSAL SRNGSFITKE KKDTVLRQVR LDPCDLQPIF DDMLHFLNPE ELRVIEEIPQ AEDKLDRLFE IIGVKSQEAS QTLLDSVYSH LPDLL //