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Tumor necrosis factor receptor superfamily member 21 (Death receptor 6) (CD antigen CD358)

 TNR21_HUMAN             Reviewed;         655 AA.
O75509; B2RDI9; Q0D2P5; Q96D86;
27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
23-MAY-2018, entry version 170.
RecName: Full=Tumor necrosis factor receptor superfamily member 21;
AltName: Full=Death receptor 6;
AltName: CD_antigen=CD358;
Flags: Precursor;
Name=TNFRSF21; Synonyms=DR6; ORFNames=UNQ437/PRO868;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INTERACTION WITH TRADD.
PubMed=9714541; DOI=10.1016/S0014-5793(98)00791-1;
Pan G., Bauer J.H., Haridas V., Wang S., Liu D., Yu G., Vincenz C.,
Aggarwal B.B., Ni J., Dixit V.M.;
"Identification and functional characterization of DR6, a novel death
domain-containing TNF receptor.";
FEBS Lett. 431:351-356(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Colon, and Eye;
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).
[7]
SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-82; ASN-141; ASN-252;
ASN-257; ASN-278 AND ASN-289, MUTAGENESIS OF ASN-82; ASN-141; ASN-252;
ASN-257; ASN-278 AND ASN-289, INDUCTION BY TNF, AND PALMITOYLATION AT
CYS-368.
PubMed=19654028; DOI=10.1016/j.bbamcr.2009.07.008;
Klima M., Zajedova J., Doubravska L., Andera L.;
"Functional analysis of the posttranslational modifications of the
death receptor 6.";
Biochim. Biophys. Acta 1793:1579-1587(2009).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=21725297; DOI=10.1038/nm.2373;
Mi S., Lee X., Hu Y., Ji B., Shao Z., Yang W., Huang G., Walus L.,
Rhodes K., Gong B.J., Miller R.H., Pepinsky R.B.;
"Death receptor 6 negatively regulates oligodendrocyte survival,
maturation and myelination.";
Nat. Med. 17:816-821(2011).
[9]
FUNCTION.
PubMed=22761420; DOI=10.1074/jbc.M112.362038;
Zeng L., Li T., Xu D.C., Liu J., Mao G., Cui M.Z., Fu X., Xu X.;
"Death receptor 6 induces apoptosis not through type I or type II
pathways, but via a unique mitochondria-dependent pathway by
interacting with Bax protein.";
J. Biol. Chem. 287:29125-29133(2012).
[10]
INDUCTION, TISSUE SPECIFICITY, AND INTERACTION WITH NGFR.
PubMed=23559013; DOI=10.1038/cddis.2013.110;
Hu Y., Lee X., Shao Z., Apicco D., Huang G., Gong B.J., Pepinsky R.B.,
Mi S.;
"A DR6/p75(NTR) complex is responsible for beta-amyloid-induced
cortical neuron death.";
Cell Death Dis. 4:E579-E579(2013).
[11]
STRUCTURE BY NMR OF 562-655.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the carboxyl-terminal CARD-like domain in human
TNFR-related death receptor-6.";
Submitted (DEC-2006) to the PDB data bank.
[12]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 42-218, AND DISULFIDE BOND.
PubMed=21463639; DOI=10.1016/j.jmb.2011.03.048;
Kuester M., Kemmerzehl S., Dahms S.O., Roeser D., Than M.E.;
"The crystal structure of death receptor 6 (DR6): a potential receptor
of the amyloid precursor protein (APP).";
J. Mol. Biol. 409:189-201(2011).
[13]
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 42-349, DISULFIDE BOND, AND
GLYCOSYLATION.
PubMed=22525750; DOI=10.1107/S0907444912004490;
Ru H., Zhao L., Ding W., Jiao L., Shaw N., Liang W., Zhang L.,
Hung L.W., Matsugaki N., Wakatsuki S., Liu Z.J.;
"S-SAD phasing study of death receptor 6 and its solution conformation
revealed by SAXS.";
Acta Crystallogr. D 68:521-530(2012).
-!- FUNCTION: Promotes apoptosis, possibly via a pathway that involves
the activation of NF-kappa-B. Can also promote apoptosis mediated
by BAX and by the release of cytochrome c from the mitochondria
into the cytoplasm. Plays a role in neuronal apoptosis, including
apoptosis in response to amyloid peptides derived from APP, and is
required for both normal cell body death and axonal pruning.
Trophic-factor deprivation triggers the cleavage of surface APP by
beta-secretase to release sAPP-beta which is further cleaved to
release an N-terminal fragment of APP (N-APP). N-APP binds
TNFRSF21; this triggers caspase activation and degeneration of
both neuronal cell bodies (via caspase-3) and axons (via caspase-
6). Negatively regulates oligodendrocyte survival, maturation and
myelination. Plays a role in signaling cascades triggered by
stimulation of T-cell receptors, in the adaptive immune response
and in the regulation of T-cell differentiation and proliferation.
Negatively regulates T-cell responses and the release of cytokines
such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively
regulates the production of IgG, IgM and IgM in response to
antigens. May inhibit the activation of JNK in response to T-cell
stimulation. {ECO:0000269|PubMed:21725297,
ECO:0000269|PubMed:22761420, ECO:0000269|PubMed:9714541}.
-!- SUBUNIT: Interacts with N-APP (By similarity). Associates with
TRADD. Interacts with NGFR. {ECO:0000250,
ECO:0000269|PubMed:23559013, ECO:0000269|PubMed:9714541}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19654028};
Single-pass type I membrane protein {ECO:0000269|PubMed:19654028}.
-!- TISSUE SPECIFICITY: Detected in fetal spinal cord and in brain
neurons, with higher levels in brain from Alzheimer disease
patients (at protein level). Highly expressed in heart, brain,
placenta, pancreas, lymph node, thymus and prostate. Detected at
lower levels in lung, skeletal muscle, kidney, testis, uterus,
small intestine, colon, spleen, bone marrow and fetal liver. Very
low levels were found in adult liver and peripheral blood
leukocytes. {ECO:0000269|PubMed:21725297,
ECO:0000269|PubMed:23559013, ECO:0000269|PubMed:9714541}.
-!- INDUCTION: Up-regulated by TNF. {ECO:0000269|PubMed:19654028,
ECO:0000269|PubMed:23559013}.
-!- CAUTION: It is uncertain whether Met-1 or Met-25 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH10241.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF068868; AAC34583.1; -; mRNA.
EMBL; AY358304; AAQ88671.1; -; mRNA.
EMBL; AK315560; BAG37936.1; -; mRNA.
EMBL; BT007420; AAP36088.1; -; mRNA.
EMBL; AL096801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010241; AAH10241.1; ALT_INIT; mRNA.
EMBL; BC017730; AAH17730.1; -; mRNA.
EMBL; BC021572; AAH21572.1; -; mRNA.
CCDS; CCDS4921.1; -.
RefSeq; NP_055267.1; NM_014452.4.
UniGene; Hs.443577; -.
PDB; 2DBH; NMR; -; A=567-655.
PDB; 3QO4; X-ray; 2.20 A; A=42-218.
PDB; 3U3P; X-ray; 2.09 A; A=42-348.
PDB; 3U3Q; X-ray; 2.70 A; A=42-348.
PDB; 3U3S; X-ray; 2.70 A; A=42-348.
PDB; 3U3T; X-ray; 3.21 A; A=42-348.
PDB; 3U3V; X-ray; 2.96 A; A=42-348.
PDBsum; 2DBH; -.
PDBsum; 3QO4; -.
PDBsum; 3U3P; -.
PDBsum; 3U3Q; -.
PDBsum; 3U3S; -.
PDBsum; 3U3T; -.
PDBsum; 3U3V; -.
ProteinModelPortal; O75509; -.
SMR; O75509; -.
BioGrid; 118090; 9.
CORUM; O75509; -.
DIP; DIP-53299N; -.
IntAct; O75509; 6.
MINT; O75509; -.
STRING; 9606.ENSP00000296861; -.
iPTMnet; O75509; -.
PhosphoSitePlus; O75509; -.
SwissPalm; O75509; -.
MaxQB; O75509; -.
PaxDb; O75509; -.
PeptideAtlas; O75509; -.
PRIDE; O75509; -.
DNASU; 27242; -.
Ensembl; ENST00000296861; ENSP00000296861; ENSG00000146072.
GeneID; 27242; -.
KEGG; hsa:27242; -.
UCSC; uc003oyv.5; human.
CTD; 27242; -.
DisGeNET; 27242; -.
EuPathDB; HostDB:ENSG00000146072.6; -.
GeneCards; TNFRSF21; -.
HGNC; HGNC:13469; TNFRSF21.
HPA; CAB009805; -.
HPA; HPA006746; -.
MIM; 605732; gene.
neXtProt; NX_O75509; -.
OpenTargets; ENSG00000146072; -.
PharmGKB; PA37775; -.
eggNOG; ENOG410IHQ6; Eukaryota.
eggNOG; ENOG410YYKW; LUCA.
GeneTree; ENSGT00760000119204; -.
HOGENOM; HOG000136852; -.
HOVERGEN; HBG054218; -.
InParanoid; O75509; -.
KO; K05157; -.
OMA; LMEDTAQ; -.
OrthoDB; EOG091G03XW; -.
PhylomeDB; O75509; -.
TreeFam; TF331157; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
SIGNOR; O75509; -.
ChiTaRS; TNFRSF21; human.
EvolutionaryTrace; O75509; -.
GeneWiki; TNFRSF21; -.
GenomeRNAi; 27242; -.
PRO; PR:O75509; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000146072; -.
CleanEx; HS_TNFRSF21; -.
ExpressionAtlas; O75509; baseline and differential.
Genevisible; O75509; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0001783; P:B cell apoptotic process; ISS:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0006959; P:humoral immune response; ISS:UniProtKB.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0042552; P:myelination; ISS:UniProtKB.
GO; GO:0030889; P:negative regulation of B cell proliferation; ISS:UniProtKB.
GO; GO:2001180; P:negative regulation of interleukin-10 secretion; ISS:UniProtKB.
GO; GO:2000666; P:negative regulation of interleukin-13 secretion; ISS:UniProtKB.
GO; GO:2000663; P:negative regulation of interleukin-5 secretion; ISS:UniProtKB.
GO; GO:0031642; P:negative regulation of myelination; IMP:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0048713; P:regulation of oligodendrocyte differentiation; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
CDD; cd08778; Death_TNFRSF21; 1.
CDD; cd10583; TNFRSF21; 1.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR022330; TNFR_21.
InterPro; IPR034037; TNFRSF21_death.
InterPro; IPR034034; TNFRSF21_N.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
Pfam; PF00531; Death; 1.
Pfam; PF00020; TNFR_c6; 3.
PRINTS; PR01971; TNFACTORR21.
SMART; SM00005; DEATH; 1.
SMART; SM01411; Ephrin_rec_like; 2.
SMART; SM00208; TNFR; 4.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS00652; TNFR_NGFR_1; 1.
PROSITE; PS50050; TNFR_NGFR_2; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Apoptosis; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 41 {ECO:0000255}.
CHAIN 42 655 Tumor necrosis factor receptor
superfamily member 21.
/FTId=PRO_0000034602.
TOPO_DOM 42 349 Extracellular. {ECO:0000255}.
TRANSMEM 350 370 Helical. {ECO:0000255}.
TOPO_DOM 371 655 Cytoplasmic. {ECO:0000255}.
REPEAT 50 88 TNFR-Cys 1.
REPEAT 90 131 TNFR-Cys 2.
REPEAT 133 167 TNFR-Cys 3.
REPEAT 170 211 TNFR-Cys 4.
DOMAIN 415 498 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
LIPID 368 368 S-palmitoyl cysteine.
{ECO:0000269|PubMed:19654028}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19654028}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19654028}.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19654028}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19654028}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19654028}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19654028}.
DISULFID 67 80
DISULFID 70 88
DISULFID 91 106
DISULFID 109 123
DISULFID 113 131
DISULFID 133 144
DISULFID 150 168
DISULFID 171 186
DISULFID 192 211
MUTAGEN 82 82 N->Q: Abolishes one glycosylation site
and reduces total N-glycosylation; when
associated with Q-252; Q-278 and Q-289.
{ECO:0000269|PubMed:19654028}.
MUTAGEN 141 141 N->Q: Abolishes one glycosylation site
and reduces total N-glycosylation; when
associated with Q-82; Q-252; Q-278 and Q-
289. {ECO:0000269|PubMed:19654028}.
MUTAGEN 252 252 N->Q: Abolishes one glycosylation site
and reduces total N-glycosylation; when
associated with Q-278 and Q-289.
{ECO:0000269|PubMed:19654028}.
MUTAGEN 257 257 N->Q: Abolishes one glycosylation site
and reduces total N-glycosylation; when
associated with Q-82; Q-141; Q-252; Q-278
and Q-289. {ECO:0000269|PubMed:19654028}.
MUTAGEN 278 278 N->Q: Abolishes one glycosylation site
and reduces total N-glycosylation.
Abolishes one glycosylation site and
reduces total N-glycosylation; when
associated with Q-82; Q-141; Q-252; Q-257
and Q-289. {ECO:0000269|PubMed:19654028}.
MUTAGEN 289 289 N->Q: Abolishes one glycosylation site
and reduces total N-glycosylation; when
associated with Q-278.
{ECO:0000269|PubMed:19654028}.
MUTAGEN 368 368 C->V: Abolishes palmitoylation.
STRAND 53 57 {ECO:0000244|PDB:3U3P}.
TURN 59 61 {ECO:0000244|PDB:3U3P}.
STRAND 64 68 {ECO:0000244|PDB:3U3P}.
STRAND 74 78 {ECO:0000244|PDB:3U3P}.
STRAND 82 84 {ECO:0000244|PDB:3U3T}.
STRAND 87 90 {ECO:0000244|PDB:3U3P}.
STRAND 99 101 {ECO:0000244|PDB:3U3V}.
STRAND 118 121 {ECO:0000244|PDB:3U3P}.
STRAND 130 132 {ECO:0000244|PDB:3U3P}.
STRAND 137 140 {ECO:0000244|PDB:3U3P}.
STRAND 143 146 {ECO:0000244|PDB:3U3P}.
STRAND 154 158 {ECO:0000244|PDB:3U3P}.
STRAND 162 164 {ECO:0000244|PDB:3U3P}.
STRAND 167 170 {ECO:0000244|PDB:3U3P}.
STRAND 181 183 {ECO:0000244|PDB:3U3P}.
HELIX 193 195 {ECO:0000244|PDB:3U3P}.
STRAND 198 201 {ECO:0000244|PDB:3U3P}.
STRAND 205 207 {ECO:0000244|PDB:3U3P}.
STRAND 210 212 {ECO:0000244|PDB:3U3P}.
STRAND 571 573 {ECO:0000244|PDB:2DBH}.
HELIX 579 591 {ECO:0000244|PDB:2DBH}.
HELIX 598 606 {ECO:0000244|PDB:2DBH}.
HELIX 609 616 {ECO:0000244|PDB:2DBH}.
HELIX 621 635 {ECO:0000244|PDB:2DBH}.
HELIX 637 650 {ECO:0000244|PDB:2DBH}.
HELIX 652 654 {ECO:0000244|PDB:2DBH}.
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


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