TNR21_MOUSE
ID TNR21_MOUSE Reviewed; 655 AA.
AC Q9EPU5; Q3UYG3; Q543Y9; Q91W77; Q91XH9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RA Isogai D., Ichino M., Yoshinari M., Yamaura A., Kurokawa F., Minami M.;
RT "Mouse DR6: mouse homolog of human TNFR-related death receptor-6 (DR6).";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RA Kim V., Machleidt T., Shi W.-X., Wang X., Cai Z.;
RT "Murine DR6: murine TNFR-related death receptor-6.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=11485735; DOI=10.1016/s1074-7613(01)00162-5;
RA Liu J., Na S., Glasebrook A., Fox N., Solenberg P.J., Zhang Q., Song H.Y.,
RA Yang D.D.;
RT "Enhanced CD4+ T cell proliferation and Th2 cytokine production in DR6-
RT deficient mice.";
RL Immunity 15:23-34(2001).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=11714751; DOI=10.1084/jem.194.10.1441;
RA Zhao H., Yan M., Wang H., Erickson S., Grewal I.S., Dixit V.M.;
RT "Impaired c-Jun amino terminal kinase activity and T cell differentiation
RT in death receptor 6-deficient mice.";
RL J. Exp. Med. 194:1441-1448(2001).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12515813; DOI=10.1084/jem.20020617;
RA Schmidt C.S., Liu J., Zhang T., Song H.Y., Sandusky G., Mintze K.,
RA Benschop R.J., Glasebrook A., Yang D.D., Na S.;
RT "Enhanced B cell expansion, survival, and humoral responses by targeting
RT death receptor 6.";
RL J. Exp. Med. 197:51-62(2003).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH APP.
RX PubMed=19225519; DOI=10.1038/nature07767;
RA Nikolaev A., McLaughlin T., O'Leary D.D.M., Tessier-Lavigne M.;
RT "APP binds DR6 to trigger axon pruning and neuron death via distinct
RT caspases.";
RL Nature 457:981-989(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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, maturation
RT and myelination.";
RL Nat. Med. 17:816-821(2011).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 cortical
RT neuron death.";
RL Cell Death Dis. 4:E579-E579(2013).
CC -!- FUNCTION: Promotes apoptosis, possibly via a pathway that involves the
CC activation of NF-kappa-B. Can also promote apoptosis mediated by BAX
CC and by the release of cytochrome c from the mitochondria into the
CC cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in
CC response to amyloid peptides derived from APP, and is required for both
CC normal cell body death and axonal pruning. Trophic-factor deprivation
CC triggers the cleavage of surface APP by beta-secretase to release sAPP-
CC beta which is further cleaved to release an N-terminal fragment of APP
CC (N-APP). N-APP binds TNFRSF21; this triggers caspase activation and
CC degeneration of both neuronal cell bodies (via caspase-3) and axons
CC (via caspase-6). Negatively regulates oligodendrocyte survival,
CC maturation and myelination. Plays a role in signaling cascades
CC triggered by stimulation of T-cell receptors, in the adaptive immune
CC response and in the regulation of T-cell differentiation and
CC proliferation. Negatively regulates T-cell responses and the release of
CC cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells.
CC Negatively 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:11485735, ECO:0000269|PubMed:11714751,
CC ECO:0000269|PubMed:12515813, ECO:0000269|PubMed:19225519,
CC ECO:0000269|PubMed:21725297, ECO:0000269|PubMed:23559013}.
CC -!- SUBUNIT: Associates with TRADD. Interacts with NGFR (By similarity).
CC Interacts with N-APP. {ECO:0000250, ECO:0000269|PubMed:19225519}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12515813};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:12515813}.
CC -!- TISSUE SPECIFICITY: Detected in spleen B-cells (at protein level).
CC Ubiquitous. Highly expressed in adult spleen, thymus, testis, prostate,
CC ovary, small intestine, colon, brain, lung and kidney, and in fetal
CC brain, liver and lung. Detected at lower levels in adult peripheral
CC blood leukocytes, lung, and in fetal muscle, heart, kidney, small
CC intestine and skin. Detected in T-cells, B-cells and monocytes. In T-
CC cells expression is highest in Th0 cells, intermediate in Th2 cells and
CC lower in Th1 cells. Expressed at low levels in proliferating
CC progenitors in the spinal cord, but is highly expressed by
CC differentiating neurons within the spinal cord and adjacent dorsal root
CC ganglia. Expressed by developing neurons as they differentiate and
CC enter a pro-apoptotic state. Expressed by both cell bodies and axons.
CC {ECO:0000269|PubMed:11485735, ECO:0000269|PubMed:11714751,
CC ECO:0000269|PubMed:12515813, ECO:0000269|PubMed:19225519}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are born at the
CC expected Mendelian rate, are viable and fertile. Mutant mice display an
CC increased number of T-cells in the peripheral blood, but only a minor
CC increase of the number of T-cells in spleen and thymus. T-cells from
CC mutant mice show increased proliferative responses to antigens and
CC produce higher levels of IL4, IL5, IL10, IL13 and IFNG. Mutant mice
CC have normal serum levels of IgG and IgM in the absence of antigen, but
CC produce higher levels of IgG, IgM and IgM in response to antigens.
CC Likewise, B-cells from mutant mice display increased proliferation and
CC decreased apoptosis in response to antigens. Mutant mice show increased
CC levels of mature oligodendrocytes, decreased levels of apoptotic
CC oligodendrocytes and increased myelination. Mutant mice are not
CC susceptible to neuronal apoptosis triggered by exposure to amyloid
CC peptides derived from APP. {ECO:0000269|PubMed:11485735,
CC ECO:0000269|PubMed:11714751, ECO:0000269|PubMed:12515813,
CC ECO:0000269|PubMed:21725297, ECO:0000269|PubMed:23559013}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-25 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AF322069; AAG38115.1; -; mRNA.
DR EMBL; AY043489; AAK74193.1; -; mRNA.
DR EMBL; AK043823; BAC31664.1; -; mRNA.
DR EMBL; AK134704; BAE22249.1; -; mRNA.
DR EMBL; BC016420; AAH16420.1; -; mRNA.
DR CCDS; CCDS28794.1; -.
DR RefSeq; NP_848704.1; NM_178589.3.
DR PDB; 4YN0; X-ray; 2.20 A; A=42-220.
DR PDBsum; 4YN0; -.
DR AlphaFoldDB; Q9EPU5; -.
DR SMR; Q9EPU5; -.
DR DIP; DIP-59733N; -.
DR IntAct; Q9EPU5; 2.
DR STRING; 10090.ENSMUSP00000024708; -.
DR GlyGen; Q9EPU5; 6 sites.
DR iPTMnet; Q9EPU5; -.
DR PhosphoSitePlus; Q9EPU5; -.
DR MaxQB; Q9EPU5; -.
DR PaxDb; Q9EPU5; -.
DR PRIDE; Q9EPU5; -.
DR ProteomicsDB; 260642; -.
DR Antibodypedia; 1463; 647 antibodies from 41 providers.
DR DNASU; 94185; -.
DR Ensembl; ENSMUST00000024708; ENSMUSP00000024708; ENSMUSG00000023915.
DR GeneID; 94185; -.
DR KEGG; mmu:94185; -.
DR UCSC; uc008cov.1; mouse.
DR CTD; 27242; -.
DR MGI; MGI:2151075; Tnfrsf21.
DR VEuPathDB; HostDB:ENSMUSG00000023915; -.
DR eggNOG; ENOG502QVMX; Eukaryota.
DR GeneTree; ENSGT00940000156212; -.
DR HOGENOM; CLU_027496_0_0_1; -.
DR InParanoid; Q9EPU5; -.
DR OMA; THQQGPH; -.
DR OrthoDB; 869160at2759; -.
DR PhylomeDB; Q9EPU5; -.
DR TreeFam; TF331157; -.
DR BioGRID-ORCS; 94185; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Tnfrsf21; mouse.
DR PRO; PR:Q9EPU5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9EPU5; protein.
DR Bgee; ENSMUSG00000023915; Expressed in right kidney and 254 other tissues.
DR Genevisible; Q9EPU5; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0007413; P:axonal fasciculation; ISO:MGI.
DR GO; GO:0001783; P:B cell apoptotic process; IMP:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0006959; P:humoral immune response; IMP:UniProtKB.
DR GO; GO:0042552; P:myelination; IMP:UniProtKB.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:UniProtKB.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:UniProtKB.
DR GO; GO:0032696; P:negative regulation of interleukin-13 production; IMP:UniProtKB.
DR GO; GO:0032714; P:negative regulation of interleukin-5 production; IMP:UniProtKB.
DR GO; GO:0031642; P:negative regulation of myelination; ISO:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0097252; P:oligodendrocyte apoptotic process; IMP:UniProtKB.
DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
DR CDD; cd08778; Death_TNFRSF21; 1.
DR CDD; cd10583; TNFRSF21; 1.
DR Gene3D; 1.10.533.10; -; 2.
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 PANTHER; PTHR46921; PTHR46921; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00020; TNFR_c6; 2.
DR PRINTS; PR01971; TNFACTORR21.
DR SMART; SM00005; DEATH; 1.
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; Disulfide bond;
KW Glycoprotein; Immunity; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..655
FT /note="Tumor necrosis factor receptor superfamily member
FT 21"
FT /id="PRO_0000034603"
FT TOPO_DOM 42..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 50..88
FT /note="TNFR-Cys 1"
FT REPEAT 90..131
FT /note="TNFR-Cys 2"
FT REPEAT 133..167
FT /note="TNFR-Cys 3"
FT REPEAT 170..211
FT /note="TNFR-Cys 4"
FT DOMAIN 415..498
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 222..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 368
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 70..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 91..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 109..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 113..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 133..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 150..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 171..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 192..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT CONFLICT 93
FT /note="A -> T (in Ref. 3; BAE22249)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="W -> L (in Ref. 1; AAG38115)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="M -> I (in Ref. 4; AAH16420)"
FT /evidence="ECO:0000305"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4YN0"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4YN0"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4YN0"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4YN0"
SQ SEQUENCE 655 AA; 71983 MW; 5EC7C51C7C99EFF7 CRC64;
MGTRASSITA LASCSRTAGQ VGATMVAGSL LLLGFLSTIT AQPEQKTLSL PGTYRHVDRT
TGQVLTCDKC PAGTYVSEHC TNMSLRVCSS CPAGTFTRHE NGIERCHDCS QPCPWPMIER
LPCAALTDRE CICPPGMYQS NGTCAPHTVC PVGWGVRKKG TENEDVRCKQ CARGTFSDVP
SSVMKCKAHT DCLGQNLEVV KPGTKETDNV CGMRLFFSST NPPSSGTVTF SHPEHMESHD
VPSSTYEPQG MNSTDSNSTA SVRTKVPSGI EEGTVPDNTS STSGKEGTNR TLPNPPQVTH
QQAPHHRHIL KLLPSSMEAT GEKSSTAIKA PKRGHPRQNA HKHFDINEHL PWMIVLFLLL
VLVLIVVCSI RKSSRTLKKG PRQDPSAIVE KAGLKKSLTP TQNREKWIYY RNGHGIDILK
LVAAQVGSQW KDIYQFLCNA SEREVAAFSN GYTADHERAY AALQHWTIRG PEASLAQLIS
ALRQHRRNDV VEKIRGLMED TTQLETDKLA LPMSPSPLSP SPMPSPNVKL ENSTLLTVEP
SPLDKNKCFF VDESEPLLRC DSTSSGSSAL SRNGSFITKE KKDTVLRQVR LDPCDLQPIF
DDMLHILNPE ELRVIEEIPQ AEDKLDRLFE IIGVKSQEAS QTLLDSVYSH LPDLL
