FADD_MOUSE
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 03-AUG-2022, entry version 185.
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, Spleen,
RC 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 adaptor molecule that recruits caspase-8 or
CC caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The
CC resulting aggregate called the death-inducing signaling complex (DISC)
CC performs caspase-8 proteolytic activation. Active caspase-8 initiates
CC the 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). Interacts with CFLAR,
CC PEA15 and MBD4 (By similarity). When phosphorylated, part of a complex
CC containing HIPK3 and FAS (By similarity). May interact with MAVS/IPS1
CC (By similarity). Interacts with MOCV v-CFLAR protein and PIDD1 (By
CC similarity). Interacts (via death domain) with FAS (via death domain)
CC (By similarity). Interacts with CASP8 (PubMed:29440439). Interacts
CC directly (via DED domain) with NOL3 (via CARD domain); inhibits death-
CC inducing signaling complex (DISC) assembly by inhibiting the increase
CC in FAS-FADD binding induced by FAS activation (PubMed:15383280).
CC Interacts with RIPK1, TRADD and CASP8 (PubMed:28842570,
CC PubMed:29440439, PubMed:30185824, PubMed:31519887). Component of the
CC AIM2 PANoptosome complex, a multiprotein complex that drives
CC inflammatory cell death (PANoptosis) (PubMed:34471287). 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=8; 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; Q61160; -.
DR PeptideAtlas; Q61160; -.
DR PRIDE; Q61160; -.
DR ProteomicsDB; 271550; -.
DR Antibodypedia; 698; 1037 antibodies from 42 providers.
DR DNASU; 14082; -.
DR Ensembl; ENSMUST00000033394; ENSMUSP00000033394; ENSMUSG00000031077.
DR GeneID; 14082; -.
DR KEGG; mmu:14082; -.
DR UCSC; uc009kql.1; mouse.
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; 1619689at2759; -.
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 76 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 201 other tissues.
DR Genevisible; Q61160; MM.
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:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005634; C:nucleus; 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: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: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:0097202; P:activation of cysteine-type endopeptidase activity; 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:2000454; P:positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation; IMP:UniProtKB.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
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:0060544; P:regulation of necroptotic process; ISO:MGI.
DR GO; GO:0043278; P:response to morphine; 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 Gene3D; 1.10.533.10; -; 2.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR001875; DED_dom.
DR InterPro; IPR016729; FADD.
DR PANTHER; PTHR15077; PTHR15077; 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; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS50168; DED; 1.
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
