ID TR10A_HUMAN Reviewed; 468 AA. AC O00220; A8K5I4; Q53Y72; Q96E62; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 3. DT 13-FEB-2019, entry version 185. DE RecName: Full=Tumor necrosis factor receptor superfamily member 10A; DE AltName: Full=Death receptor 4; DE AltName: Full=TNF-related apoptosis-inducing ligand receptor 1; DE Short=TRAIL receptor 1; DE Short=TRAIL-R1; DE AltName: CD_antigen=CD261; DE Flags: Precursor; GN Name=TNFRSF10A; Synonyms=APO2, DR4, TRAILR1; 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], AND VARIANTS ARG-141; THR-209 AND LYS-441. RX PubMed=9082980; DOI=10.1126/science.276.5309.111; RA Pan G., O'Rourke K., Chinnaiyan A.M., Gentz R., Ebner R., Ni J., RA Dixit V.M.; RT "The receptor for the cytotoxic ligand TRAIL."; RL Science 276:111-113(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-441. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-141; THR-209 RP AND LYS-441. RC TISSUE=Tongue; 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 [GENOMIC DNA], AND VARIANT LYS-441. RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., RA Nickerson D.A.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-441. RC TISSUE=Ovary; 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 FUNCTION. RX PubMed=9430227; DOI=10.1016/S1074-7613(00)80400-8; RA Chaudhary P.M., Eby M., Jasmin A., Bookwalter A., Murray J., Hood L.; RT "Death receptor 5, a new member of the TNFR family, and DR4 induce RT FADD-dependent apoptosis and activate the NF-kappaB pathway."; RL Immunity 7:821-830(1997). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [9] RP INTERACTION WITH ARAP1. RX PubMed=18165900; DOI=10.1007/s10495-007-0171-8; RA Simova S., Klima M., Cermak L., Sourkova V., Andera L.; RT "Arf and Rho GAP adapter protein ARAP1 participates in the RT mobilization of TRAIL-R1/DR4 to the plasma membrane."; RL Apoptosis 13:423-436(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 AND SER-466, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL141. RX PubMed=23498957; DOI=10.1016/j.chom.2013.02.003; RA Smith W., Tomasec P., Aicheler R., Loewendorf A., Nemcovicova I., RA Wang E.C., Stanton R.J., Macauley M., Norris P., Willen L., RA Ruckova E., Nomoto A., Schneider P., Hahn G., Zajonc D.M., Ware C.F., RA Wilkinson G.W., Benedict C.A.; RT "Human cytomegalovirus glycoprotein UL141 targets the TRAIL death RT receptors to thwart host innate antiviral defenses."; RL Cell Host Microbe 13:324-335(2013). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-52, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.O113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., RA Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., RA Vemulapalli V., Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [14] {ECO:0000244|PDB:5CIR} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 125-232 IN COMPLEX WITH RP TNFSF10, SUBUNIT, FUNCTION, AND DISULFIDE BONDS. RX PubMed=26457518; DOI=10.1107/S2053230X15016416; RA Ramamurthy V., Yamniuk A.P., Lawrence E.J., Yong W., Schneeweis L.A., RA Cheng L., Murdock M., Corbett M.J., Doyle M.L., Sheriff S.; RT "The structure of the death receptor 4-TNF-related apoptosis-inducing RT ligand (DR4-TRAIL) complex."; RL Acta Crystallogr. F 71:1273-1281(2015). CC -!- FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL CC (PubMed:26457518). The adapter molecule FADD recruits caspase-8 to CC the activated receptor. The resulting death-inducing signaling CC complex (DISC) performs caspase-8 proteolytic activation which CC initiates the subsequent cascade of caspases (aspartate-specific CC cysteine proteases) mediating apoptosis. Promotes the activation CC of NF-kappa-B. {ECO:0000269|PubMed:26457518, CC ECO:0000269|PubMed:9430227}. CC -!- SUBUNIT: Monomer (PubMed:26457518). Three TNFRSF10A molecules CC interact with the TNFSF10 homotrimer (PubMed:26457518). Can CC interact with TRADD and RIPK1. Interacts with ARAP1. Interacts CC with HCMV protein UL141; this interaction prevents TNFRSF10A cell CC surface expression. {ECO:0000269|PubMed:18165900, CC ECO:0000269|PubMed:23498957, ECO:0000269|PubMed:26457518}. CC -!- INTERACTION: CC Q96P48:ARAP1; NbExp=4; IntAct=EBI-518861, EBI-710003; CC Q14790:CASP8; NbExp=9; IntAct=EBI-518861, EBI-78060; CC P50591:TNFSF10; NbExp=4; IntAct=EBI-518861, EBI-495373; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Widely expressed. High levels are found in CC spleen, peripheral blood leukocytes, small intestine and thymus, CC but also in K-562 erythroleukemia cells, MCF-7 breast carcinoma CC cells and activated T-cells. 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; U90875; AAC51226.1; -; mRNA. DR EMBL; BT006906; AAP35552.1; -; mRNA. DR EMBL; AK291299; BAF83988.1; -; mRNA. DR EMBL; EF064713; ABK41896.1; -; Genomic_DNA. DR EMBL; AC100861; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC012866; AAH12866.1; -; mRNA. DR CCDS; CCDS6039.1; -. DR RefSeq; NP_003835.3; NM_003844.3. DR UniGene; Hs.213467; -. DR UniGene; Hs.591834; -. DR PDB; 5CIR; X-ray; 3.00 A; E/F/G=125-232. DR PDBsum; 5CIR; -. DR ProteinModelPortal; O00220; -. DR SMR; O00220; -. DR BioGrid; 114325; 50. DR IntAct; O00220; 11. DR MINT; O00220; -. DR STRING; 9606.ENSP00000221132; -. DR BindingDB; O00220; -. DR ChEMBL; CHEMBL3551; -. DR GuidetoPHARMACOLOGY; 1879; -. DR iPTMnet; O00220; -. DR PhosphoSitePlus; O00220; -. DR SwissPalm; O00220; -. DR BioMuta; TNFRSF10A; -. DR EPD; O00220; -. DR jPOST; O00220; -. DR MaxQB; O00220; -. DR PaxDb; O00220; -. DR PeptideAtlas; O00220; -. DR PRIDE; O00220; -. DR ProteomicsDB; 47790; -. DR DNASU; 8797; -. DR Ensembl; ENST00000221132; ENSP00000221132; ENSG00000104689. DR GeneID; 8797; -. DR KEGG; hsa:8797; -. DR UCSC; uc003xda.4; human. DR CTD; 8797; -. DR DisGeNET; 8797; -. DR EuPathDB; HostDB:ENSG00000104689.9; -. DR GeneCards; TNFRSF10A; -. DR H-InvDB; HIX0022944; -. DR HGNC; HGNC:11904; TNFRSF10A. DR HPA; HPA050958; -. DR HPA; HPA054475; -. DR MIM; 603611; gene. DR neXtProt; NX_O00220; -. DR OpenTargets; ENSG00000104689; -. DR PharmGKB; PA36597; -. DR eggNOG; ENOG410IZX0; Eukaryota. DR eggNOG; ENOG4111ZZM; LUCA. DR GeneTree; ENSGT00940000162957; -. DR HOGENOM; HOG000142423; -. DR HOVERGEN; HBG061626; -. DR InParanoid; O00220; -. DR KO; K04722; -. DR OMA; CTPWSDL; -. DR OrthoDB; 817293at2759; -. DR PhylomeDB; O00220; -. DR TreeFam; TF333916; -. DR Reactome; R-HSA-140534; Caspase activation via Death Receptors in the presence of ligand. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-3371378; Regulation by c-FLIP. DR Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis. DR Reactome; R-HSA-5218900; CASP8 activity is inhibited. DR Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands. DR Reactome; R-HSA-69416; Dimerization of procaspase-8. DR Reactome; R-HSA-75158; TRAIL signaling. DR SignaLink; O00220; -. DR SIGNOR; O00220; -. DR GeneWiki; TNFRSF10A; -. DR GenomeRNAi; 8797; -. DR PRO; PR:O00220; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000104689; Expressed in 187 organ(s), highest expression level in buccal mucosa cell. DR ExpressionAtlas; O00220; baseline and differential. DR Genevisible; O00220; HS. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005035; F:death receptor activity; TAS:ProtInc. DR GO; GO:0002020; F:protease binding; IPI:UniProtKB. DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB. DR GO; GO:0045569; F:TRAIL binding; NAS:UniProtKB. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome. DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; NAS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:Reactome. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; TAS:ProtInc. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome. DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome. DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IDA:ParkinsonsUK-UCL. DR CDD; cd08315; Death_TRAILR_DR4_DR5; 1. DR CDD; cd10580; TNFRSF10; 1. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR000488; Death_domain. DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg. DR InterPro; IPR020465; TNFR_10. DR InterPro; IPR034024; TNFRSF10_N. DR InterPro; IPR034029; TNFRSF10A/B_death. DR Pfam; PF00531; Death; 1. DR Pfam; PF00020; TNFR_c6; 2. DR PIRSF; PIRSF037867; CD261_antigen; 1. DR PRINTS; PR01956; TNFACTORR10. DR SMART; SM00005; DEATH; 1. DR SMART; SM00208; TNFR; 2. DR SUPFAM; SSF47986; SSF47986; 1. DR PROSITE; PS50017; DEATH_DOMAIN; 1. DR PROSITE; PS00652; TNFR_NGFR_1; 2. DR PROSITE; PS50050; TNFR_NGFR_2; 2. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; Complete proteome; Disulfide bond; KW Glycoprotein; Membrane; Methylation; Phosphoprotein; Polymorphism; KW Receptor; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 468 Tumor necrosis factor receptor FT superfamily member 10A. FT /FTId=PRO_0000034579. FT TOPO_DOM 24 239 Extracellular. {ECO:0000255}. FT TRANSMEM 240 262 Helical. {ECO:0000255}. FT TOPO_DOM 263 468 Cytoplasmic. {ECO:0000255}. FT REPEAT 107 145 TNFR-Cys 1. FT REPEAT 147 188 TNFR-Cys 2. FT REPEAT 189 229 TNFR-Cys 3. FT DOMAIN 365 448 Death. {ECO:0000255|PROSITE- FT ProRule:PRU00064}. FT COMPBIAS 29 32 Poly-Ala. FT MOD_RES 52 52 Omega-N-methylarginine. FT {ECO:0000244|PubMed:24129315}. FT MOD_RES 424 424 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 463 463 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 466 466 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:20068231}. FT CARBOHYD 156 156 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 132 145 {ECO:0000244|PDB:5CIR, FT ECO:0000255|PROSITE-ProRule:PRU00206, FT ECO:0000269|PubMed:26457518}. FT DISULFID 148 164 {ECO:0000244|PDB:5CIR, FT ECO:0000255|PROSITE-ProRule:PRU00206, FT ECO:0000269|PubMed:26457518}. FT DISULFID 167 180 {ECO:0000244|PDB:5CIR, FT ECO:0000255|PROSITE-ProRule:PRU00206, FT ECO:0000269|PubMed:26457518}. FT DISULFID 170 188 {ECO:0000244|PDB:5CIR, FT ECO:0000255|PROSITE-ProRule:PRU00206, FT ECO:0000269|PubMed:26457518}. FT DISULFID 190 204 {ECO:0000244|PDB:5CIR, FT ECO:0000255|PROSITE-ProRule:PRU00206, FT ECO:0000269|PubMed:26457518}. FT DISULFID 207 221 {ECO:0000244|PDB:5CIR, FT ECO:0000255|PROSITE-ProRule:PRU00206, FT ECO:0000269|PubMed:26457518}. FT DISULFID 211 229 {ECO:0000244|PDB:5CIR, FT ECO:0000255|PROSITE-ProRule:PRU00206, FT ECO:0000269|PubMed:26457518}. FT VARIANT 11 11 G -> V (in dbSNP:rs34737614). FT /FTId=VAR_052349. FT VARIANT 33 33 T -> I (in dbSNP:rs20577). FT /FTId=VAR_016149. FT VARIANT 105 105 P -> R (in dbSNP:rs11986840). FT /FTId=VAR_052350. FT VARIANT 141 141 H -> R (in dbSNP:rs17620). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9082980}. FT /FTId=VAR_016150. FT VARIANT 209 209 R -> T (in dbSNP:rs20575). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9082980}. FT /FTId=VAR_016151. FT VARIANT 228 228 E -> A (in dbSNP:rs20576). FT /FTId=VAR_016152. FT VARIANT 297 297 N -> H (in dbSNP:rs17088980). FT /FTId=VAR_052351. FT VARIANT 441 441 R -> K (in dbSNP:rs2230229). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9082980, FT ECO:0000269|Ref.2, ECO:0000269|Ref.4}. FT /FTId=VAR_052352. FT CONFLICT 281 281 W -> C (in Ref. 3; BAF83988). FT {ECO:0000305}. FT STRAND 136 138 {ECO:0000244|PDB:5CIR}. FT STRAND 145 147 {ECO:0000244|PDB:5CIR}. FT TURN 150 152 {ECO:0000244|PDB:5CIR}. FT STRAND 157 159 {ECO:0000244|PDB:5CIR}. FT STRAND 174 178 {ECO:0000244|PDB:5CIR}. FT STRAND 187 190 {ECO:0000244|PDB:5CIR}. FT STRAND 216 219 {ECO:0000244|PDB:5CIR}. FT STRAND 228 230 {ECO:0000244|PDB:5CIR}. SQ SEQUENCE 468 AA; 50089 MW; 7E96619D0BDC0CD4 CRC64; MAPPPARVHL GAFLAVTPNP GSAASGTEAA AATPSKVWGS SAGRIEPRGG GRGALPTSMG QHGPSARARA GRAPGPRPAR EASPRLRVHK TFKFVVVGVL LQVVPSSAAT IKLHDQSIGT QQWEHSPLGE LCPPGSHRSE HPGACNRCTE GVGYTNASNN LFACLPCTAC KSDEEERSPC TTTRNTACQC KPGTFRNDNS AEMCRKCSRG CPRGMVKVKD CTPWSDIECV HKESGNGHNI WVILVVTLVV PLLLVAVLIV CCCIGSGCGG DPKCMDRVCF WRLGLLRGPG AEDNAHNEIL SNADSLSTFV SEQQMESQEP ADLTGVTVQS PGEAQCLLGP AEAEGSQRRR LLVPANGADP TETLMLFFDK FANIVPFDSW DQLMRQLDLT KNEIDVVRAG TAGPGDALYA MLMKWVNKTG RNASIHTLLD ALERMEERHA REKIQDLLVD SGKFIYLEDG TGSAVSLE //