ID FADD_MOUSE Reviewed; 205 AA. AC Q61160; Q3TC37; Q61082; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 194. DE RecName: Full=FAS-associated death domain protein {ECO:0000303|PubMed:8649383}; DE AltName: Full=FAS-associating death domain-containing protein {ECO:0000303|PubMed:8649383}; DE AltName: Full=Mediator of receptor induced toxicity {ECO:0000303|PubMed:8649383}; GN Name=Fadd {ECO:0000303|PubMed:8649383, ECO:0000312|MGI:MGI:109324}; GN Synonyms=Mort1 {ECO:0000303|PubMed:8649383}; 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]. RX PubMed=8649383; DOI=10.1128/mcb.16.6.2756; RA Zhang J., Winoto A.; RT "A mouse Fas-associated protein with homology to the human Mort1/FADD RT protein is essential for Fas-induced apoptosis."; RL Mol. Cell. Biol. 16:2756-2763(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8565075; DOI=10.1016/s0092-8674(00)80984-8; RA Hsu H., Shu H.-B., Pan M.G., Goeddel D.V.; RT "TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 RT signal transduction pathways."; RL Cell 84:299-308(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Thymus; 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 STRAIN=Czech II; TISSUE=Mammary gland, and Salivary gland; 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 INTERACTION WITH NOL3. RX PubMed=15383280; DOI=10.1016/j.molcel.2004.08.020; RA Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B., Hayakawa Y., RA Lee P., Korsmeyer S.J., Kitsis R.N.; RT "Inhibition of both the extrinsic and intrinsic death pathways through RT nonhomotypic death-fold interactions."; RL Mol. Cell 15:901-912(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; 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 [7] RP INTERACTION WITH RIPK1. RX PubMed=28842570; DOI=10.1038/s41467-017-00406-w; RA Geng J., Ito Y., Shi L., Amin P., Chu J., Ouchida A.T., Mookhtiar A.K., RA Zhao H., Xu D., Shan B., Najafov A., Gao G., Akira S., Yuan J.; RT "Regulation of RIPK1 activation by TAK1-mediated phosphorylation dictates RT apoptosis and necroptosis."; RL Nat. Commun. 8:359-359(2017). RN [8] RP INTERACTION WITH CASP8 AND RIPK1. RX PubMed=29440439; DOI=10.1073/pnas.1722013115; RA Meng H., Liu Z., Li X., Wang H., Jin T., Wu G., Shan B., RA Christofferson D.E., Qi C., Yu Q., Li Y., Yuan J.; RT "Death-domain dimerization-mediated activation of RIPK1 controls RT necroptosis and RIPK1-dependent apoptosis."; RL Proc. Natl. Acad. Sci. U.S.A. 115:E2001-E2009(2018). RN [9] RP INTERACTION WITH TRADD. RX PubMed=30185824; DOI=10.1038/s41418-018-0166-8; RA Anderton H., Bandala-Sanchez E., Simpson D.S., Rickard J.A., Ng A.P., RA Di Rago L., Hall C., Vince J.E., Silke J., Liccardi G., Feltham R.; RT "RIPK1 prevents TRADD-driven, but TNFR1 independent, apoptosis during RT development."; RL Cell Death Differ. 26:877-889(2019). RN [10] RP INTERACTION WITH RIPK1. RX PubMed=31519887; DOI=10.1038/s41467-019-12033-8; RA Tang Y., Tu H., Zhang J., Zhao X., Wang Y., Qin J., Lin X.; RT "K63-linked ubiquitination regulates RIPK1 kinase activity to prevent cell RT death during embryogenesis and inflammation."; RL Nat. Commun. 10:4157-4157(2019). RN [11] RP IDENTIFICATION IN THE AIM2 PANOPTOSOME COMPLEX. RX PubMed=34471287; DOI=10.1038/s41586-021-03875-8; RA Lee S., Karki R., Wang Y., Nguyen L.N., Kalathur R.C., Kanneganti T.D.; RT "AIM2 forms a complex with pyrin and ZBP1 to drive PANoptosis and host RT defence."; RL Nature 597:415-419(2021). RN [12] RP STRUCTURE BY NMR OF 89-183. RX PubMed=10347191; DOI=10.1074/jbc.274.23.16337; RA Jeong E.-J., Bang S., Lee T.H., Park Y.-I., Sim W.-S., Kim K.-S.; RT "The solution structure of FADD death domain. Structural basis of death RT domain interactions of Fas and FADD."; RL J. Biol. Chem. 274:16337-16342(1999). CC -!- FUNCTION: Apoptotic adapter molecule that recruits caspases CASP8 or CC CASP10 to the activated FAS/CD95 or TNFRSF1A/TNFR-1 receptors. The CC resulting aggregate called the death-inducing signaling complex (DISC) CC performs CASP8 proteolytic activation. Active CASP8 initiates the CC subsequent cascade of caspases mediating apoptosis. Involved in CC interferon-mediated antiviral immune response, playing a role in the CC positive regulation of interferon signaling. CC {ECO:0000250|UniProtKB:Q13158}. CC -!- SUBUNIT: Can self-associate (By similarity). Component of the AIM2 CC PANoptosome complex, a multiprotein complex that drives inflammatory CC cell death (PANoptosis) (PubMed:34471287). Component of the death- CC induced signaling complex (DISC) composed of cell surface receptor CC FAS/CD95 or TNFRSF1A, adapter protein FADD and the CASP8 protease; CC recruitment of CASP8 to the complex is required for processing of CASP8 CC into the p18 and p10 subunits (By similarity). Interacts (via death CC domain) with FAS (via death domain) (By similarity). Interacts directly CC (via DED domain) with NOL3 (via CARD domain); inhibits death-inducing CC signaling complex (DISC) assembly by inhibiting the increase in FAS- CC FADD binding induced by FAS activation (PubMed:15383280). Interacts CC with CFLAR, PEA15 and MBD4 (By similarity). When phosphorylated, part CC of a complex containing HIPK3 and FAS (By similarity). May interact CC with MAVS/IPS1 (By similarity). Interacts with MOCV v-CFLAR protein and CC PIDD1 (By similarity). Interacts with RIPK1 and TRADD (PubMed:28842570, CC PubMed:29440439, PubMed:30185824, PubMed:31519887). Interacts with CC stimulated TNFRSF10B (By similarity). {ECO:0000250|UniProtKB:Q13158, CC ECO:0000269|PubMed:15383280, ECO:0000269|PubMed:28842570, CC ECO:0000269|PubMed:29440439, ECO:0000269|PubMed:30185824, CC ECO:0000269|PubMed:31519887, ECO:0000269|PubMed:34471287}. CC -!- INTERACTION: CC Q61160; O89110: Casp8; NbExp=6; IntAct=EBI-524415, EBI-851690; CC Q61160; P25446: Fas; NbExp=3; IntAct=EBI-524415, EBI-296206; CC Q61160; Q60855: Ripk1; NbExp=9; IntAct=EBI-524415, EBI-529119; CC Q61160; Q9QZL0: Ripk3; NbExp=6; IntAct=EBI-524415, EBI-2367423; CC -!- DOMAIN: Contains a death domain involved in the binding of the CC corresponding domain within Fas receptor. CC {ECO:0000250|UniProtKB:Q13158}. CC -!- DOMAIN: The interaction between the FAS and FADD death domains is CC crucial for the formation of the death-inducing signaling complex CC (DISC). {ECO:0000250|UniProtKB:Q13158}. 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; U50406; AAB07789.1; -; mRNA. DR EMBL; U43184; AAA97876.1; -; mRNA. DR EMBL; AK084808; BAC39283.1; -; mRNA. DR EMBL; AK169798; BAE41374.1; -; mRNA. DR EMBL; AK170927; BAE42120.1; -; mRNA. DR EMBL; BC004584; AAH04584.1; -; mRNA. DR EMBL; BC021400; AAH21400.1; -; mRNA. DR CCDS; CCDS22050.1; -. DR RefSeq; NP_034305.1; NM_010175.5. DR PDB; 1FAD; NMR; -; A=89-183. DR PDBsum; 1FAD; -. DR AlphaFoldDB; Q61160; -. DR SMR; Q61160; -. DR BioGRID; 199586; 17. DR ComplexPortal; CPX-1914; Ripoptosome. DR DIP; DIP-34771N; -. DR IntAct; Q61160; 15. DR MINT; Q61160; -. DR STRING; 10090.ENSMUSP00000033394; -. DR iPTMnet; Q61160; -. DR PhosphoSitePlus; Q61160; -. DR EPD; Q61160; -. DR jPOST; Q61160; -. DR MaxQB; Q61160; -. DR PaxDb; 10090-ENSMUSP00000033394; -. DR PeptideAtlas; Q61160; -. DR ProteomicsDB; 271550; -. DR Pumba; Q61160; -. DR Antibodypedia; 698; 1164 antibodies from 42 providers. DR DNASU; 14082; -. DR Ensembl; ENSMUST00000033394.8; ENSMUSP00000033394.8; ENSMUSG00000031077.8. DR GeneID; 14082; -. DR KEGG; mmu:14082; -. DR UCSC; uc009kql.1; mouse. DR AGR; MGI:109324; -. DR CTD; 8772; -. DR MGI; MGI:109324; Fadd. DR VEuPathDB; HostDB:ENSMUSG00000031077; -. DR eggNOG; ENOG502S2RV; Eukaryota. DR GeneTree; ENSGT00390000002105; -. DR HOGENOM; CLU_087961_0_0_1; -. DR InParanoid; Q61160; -. DR OMA; CKMNLVA; -. DR OrthoDB; 2960517at2759; -. DR PhylomeDB; Q61160; -. DR TreeFam; TF102046; -. DR Reactome; R-MMU-140534; Caspase activation via Death Receptors in the presence of ligand. DR Reactome; R-MMU-2562578; TRIF-mediated programmed cell death. DR Reactome; R-MMU-3371378; Regulation by c-FLIP. DR Reactome; R-MMU-5218900; CASP8 activity is inhibited. DR Reactome; R-MMU-5357786; TNFR1-induced proapoptotic signaling. DR Reactome; R-MMU-5357905; Regulation of TNFR1 signaling. DR Reactome; R-MMU-5675482; Regulation of necroptotic cell death. DR Reactome; R-MMU-69416; Dimerization of procaspase-8. DR Reactome; R-MMU-75157; FasL/ CD95L signaling. DR Reactome; R-MMU-75158; TRAIL signaling. DR BioGRID-ORCS; 14082; 26 hits in 81 CRISPR screens. DR ChiTaRS; Fadd; mouse. DR EvolutionaryTrace; Q61160; -. DR PRO; PR:Q61160; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q61160; Protein. DR Bgee; ENSMUSG00000031077; Expressed in substantia propria of cornea and 204 other cell types or tissues. DR GO; GO:0031265; C:CD95 death-inducing signaling complex; ISO:MGI. DR GO; GO:0044297; C:cell body; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0031264; C:death-inducing signaling complex; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0097342; C:ripoptosome; ISS:UniProtKB. DR GO; GO:0089720; F:caspase binding; ISS:UniProtKB. DR GO; GO:0035877; F:death effector domain binding; ISO:MGI. DR GO; GO:0005123; F:death receptor binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI. DR GO; GO:0002020; F:protease binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0033612; F:receptor serine/threonine kinase binding; ISO:MGI. DR GO; GO:0035591; F:signaling adaptor activity; IDA:MGI. DR GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:MGI. DR GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; ISO:MGI. DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB. DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI. DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl. DR GO; GO:0048738; P:cardiac muscle tissue development; TAS:UniProtKB. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0071550; P:death-inducing signaling complex assembly; ISO:MGI. DR GO; GO:0051607; P:defense response to virus; ISO:MGI. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI. DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB. DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0048535; P:lymph node development; IGI:UniProtKB. DR GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI. DR GO; GO:0097527; P:necroptotic signaling pathway; ISO:MGI. DR GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IMP:UniProtKB. DR GO; GO:0060546; P:negative regulation of necroptotic process; IGI:MGI. DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:UniProtKB. DR GO; GO:0002821; P:positive regulation of adaptive immune response; IMP:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl. DR GO; GO:2000454; P:positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation; IMP:UniProtKB. DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IDA:MGI. DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IGI:MGI. DR GO; GO:0045089; P:positive regulation of innate immune response; IBA:GO_Central. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI. DR GO; GO:0045651; P:positive regulation of macrophage differentiation; ISO:MGI. DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI. DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISO:MGI. DR GO; GO:0032729; P:positive regulation of type II interferon production; IMP:UniProtKB. DR GO; GO:0060544; P:regulation of necroptotic process; ISO:MGI. DR GO; GO:0048536; P:spleen development; IGI:UniProtKB. DR GO; GO:0030217; P:T cell differentiation; TAS:UniProtKB. DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:UniProtKB. DR GO; GO:0043029; P:T cell homeostasis; IMP:UniProtKB. DR GO; GO:0048538; P:thymus development; IGI:UniProtKB. DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; ISO:MGI. DR CDD; cd08306; Death_FADD; 1. DR CDD; cd08336; DED_FADD; 1. DR Gene3D; 1.10.533.10; Death Domain, Fas; 2. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR000488; Death_domain. DR InterPro; IPR001875; DED_dom. DR InterPro; IPR016729; FADD_DD. DR InterPro; IPR049634; FADD_vert. DR PANTHER; PTHR15077:SF9; FAS-ASSOCIATED DEATH DOMAIN PROTEIN; 1. DR PANTHER; PTHR15077; FAS-ASSOCIATING DEATH DOMAIN-CONTAINING PROTEIN FADD; 1. DR Pfam; PF00531; Death; 1. DR Pfam; PF01335; DED; 1. DR PIRSF; PIRSF018586; FADD; 1. DR SMART; SM00005; DEATH; 1. DR SMART; SM00031; DED; 1. DR SUPFAM; SSF47986; DEATH domain; 1. DR PROSITE; PS50017; DEATH_DOMAIN; 1. DR PROSITE; PS50168; DED; 1. DR Genevisible; Q61160; MM. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; Immunity; Innate immunity; Phosphoprotein; KW Reference proteome. FT CHAIN 1..205 FT /note="FAS-associated death domain protein" FT /id="PRO_0000191280" FT DOMAIN 3..81 FT /note="DED" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065" FT DOMAIN 97..181 FT /note="Death" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064" FT REGION 181..205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 183..205 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 191 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CONFLICT 168 FT /note="C -> F (in Ref. 2; AAA97876)" FT /evidence="ECO:0000305" FT HELIX 94..118 FT /evidence="ECO:0007829|PDB:1FAD" FT HELIX 123..132 FT /evidence="ECO:0007829|PDB:1FAD" FT HELIX 137..152 FT /evidence="ECO:0007829|PDB:1FAD" FT HELIX 153..156 FT /evidence="ECO:0007829|PDB:1FAD" FT HELIX 158..168 FT /evidence="ECO:0007829|PDB:1FAD" FT HELIX 171..181 FT /evidence="ECO:0007829|PDB:1FAD" SQ SEQUENCE 205 AA; 22960 MW; 4BC8D86B33A58783 CRC64; MDPFLVLLHS LSGSLSGNDL MELKFLCRER VSKRKLERVQ SGLDLFTVLL EQNDLERGHT GLLRELLASL RRHDLLQRLD DFEAGTATAA PPGEADLQVA FDIVCDNVGR DWKRLARELK VSEAKMDGIE EKYPRSLSER VRESLKVWKN AEKKNASVAG LVKALRTCRL NLVADLVEEA QESVSKSENM SPVLRDSTVS SSETP //