ID EDAD_HUMAN Reviewed; 215 AA. AC Q8WWZ3; A2VCK5; A8K7B5; B1AL54; B9ZVW5; Q5VYJ7; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 3. DT 24-JAN-2024, entry version 167. DE RecName: Full=Ectodysplasin-A receptor-associated adapter protein; DE AltName: Full=EDAR-associated death domain protein; DE AltName: Full=Protein crinkled homolog; GN Name=EDARADD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND VARIANT ECTD11B LYS-152. RX PubMed=11780064; DOI=10.1038/414913a; RA Headon D.J., Emmal S.A., Ferguson B.M., Tucker A.S., Justice M.J., RA Sharpe P.T., Zonana J., Overbeek P.A.; RT "Gene defect in ectodermal dysplasia implicates a DEATH domain adapter in RT development."; RL Nature 414:913-916(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND FUNCTION. RC TISSUE=Skin; RX PubMed=11882293; DOI=10.1016/s0960-9822(02)00687-5; RA Yan M., Zhang Z., Brady J.R., Schilbach S., Fairbrother W.J., Dixit V.M.; RT "Identification of a novel DEATH domain-containing adaptor molecule for RT ectodysplasin-A receptor that is mutated in crinkled mice."; RL Curr. Biol. 12:409-413(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), NUCLEOTIDE SEQUENCE [GENOMIC DNA], RP AND VARIANT ILE-9. RA Emmal S.A., Ferguson B.M., Zonana J.; RT "A novel death domain adapter required for ectodermal development."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B), AND VARIANT RP ILE-9. RC TISSUE=Mammary gland, and Placenta; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT ILE-9. 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 [8] RP VARIANT ECTD11A ARG-122, CHARACTERIZATION OF VARIANT ECTD11A ARG-122, AND RP CHARACTERIZATION OF VARIANT ECTD11B LYS-152. RX PubMed=17354266; DOI=10.1002/humu.20500; RA Bal E., Baala L., Cluzeau C., El Kerch F., Ouldim K., Hadj-Rabia S., RA Bodemer C., Munnich A., Courtois G., Sefiani A., Smahi A.; RT "Autosomal dominant anhidrotic ectodermal dysplasias at the EDARADD RT locus."; RL Hum. Mutat. 28:703-709(2007). RN [9] RP VARIANT PHE-103. RX PubMed=18231121; DOI=10.1038/sj.ejhg.5202012; RA van der Hout A.H., Oudesluijs G.G., Venema A., Verheij J.B.G.M., RA Mol B.G.J., Rump P., Brunner H.G., Vos Y.J., van Essen A.J.; RT "Mutation screening of the ectodysplasin-A receptor gene EDAR in RT hypohidrotic ectodermal dysplasia."; RL Eur. J. Hum. Genet. 16:673-679(2008). RN [10] RP VARIANT ECTD11B 135-THR-VAL-136 DEL, AND CHARACTERIZATION OF VARIANT RP ECTD11B 135-THR-VAL-136 DEL. RX PubMed=20222921; DOI=10.1111/j.1365-2133.2010.09670.x; RA Chassaing N., Cluzeau C., Bal E., Guigue P., Vincent M.C., Viot G., RA Ginisty D., Munnich A., Smahi A., Calvas P.; RT "Mutations in EDARADD account for a small proportion of hypohidrotic RT ectodermal dysplasia cases."; RL Br. J. Dermatol. 162:1044-1048(2010). RN [11] RP VARIANT ECTD11A TYR-114. RX PubMed=20979233; DOI=10.1002/humu.21384; RA Cluzeau C., Hadj-Rabia S., Jambou M., Mansour S., Guigue P., Masmoudi S., RA Bal E., Chassaing N., Vincent M.C., Viot G., Clauss F., Maniere M.C., RA Toupenay S., Le Merrer M., Lyonnet S., Cormier-Daire V., Amiel J., RA Faivre L., de Prost Y., Munnich A., Bonnefont J.P., Bodemer C., Smahi A.; RT "Only four genes (EDA1, EDAR, EDARADD, and WNT10A) account for 90% of RT hypohidrotic/anhidrotic ectodermal dysplasia cases."; RL Hum. Mutat. 32:70-72(2011). CC -!- FUNCTION: Adapter protein that interacts with EDAR DEATH domain and CC couples the receptor to EDA signaling pathway during morphogenesis of CC ectodermal organs. Mediates the activation of NF-kappa-B. CC {ECO:0000269|PubMed:11882293}. CC -!- SUBUNIT: Self-associates and binds EDAR, TRAF1, TRAF2 and TRAF3. CC -!- INTERACTION: CC Q8WWZ3; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-2949647, EBI-741158; CC Q8WWZ3; Q6ZNA4: RNF111; NbExp=3; IntAct=EBI-2949647, EBI-2129175; CC Q8WWZ3; O00560: SDCBP; NbExp=3; IntAct=EBI-2949647, EBI-727004; CC Q8WWZ3; Q149N8: SHPRH; NbExp=3; IntAct=EBI-2949647, EBI-714105; CC Q8WWZ3; P63165: SUMO1; NbExp=5; IntAct=EBI-2949647, EBI-80140; CC Q8WWZ3; G2XKQ0: SUMO1P1; NbExp=5; IntAct=EBI-2949647, EBI-10175576; CC Q8WWZ3; Q12933: TRAF2; NbExp=5; IntAct=EBI-2949647, EBI-355744; CC Q8WWZ3; Q9Y4K3: TRAF6; NbExp=5; IntAct=EBI-2949647, EBI-359276; CC Q8WWZ3; P63279: UBE2I; NbExp=3; IntAct=EBI-2949647, EBI-80168; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q8WWZ3-1; Sequence=Displayed; CC Name=B; CC IsoId=Q8WWZ3-2; Sequence=VSP_003861; CC -!- TISSUE SPECIFICITY: Detected in adult pancreas, placenta and fetal CC skin, and at lower levels in lung, thymus, prostate and testis. CC -!- DISEASE: Ectodermal dysplasia 11A, hypohidrotic/hair/nail type, CC autosomal dominant (ECTD11A) [MIM:614940]: A form of ectodermal CC dysplasia, a heterogeneous group of disorders due to abnormal CC development of two or more ectodermal structures. It is an autosomal CC dominant condition characterized by hypotrichosis, abnormal or missing CC teeth, and hypohidrosis due to the absence of sweat glands. CC {ECO:0000269|PubMed:17354266, ECO:0000269|PubMed:20979233}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Ectodermal dysplasia 11B, hypohidrotic/hair/tooth type, CC autosomal recessive (ECTD11B) [MIM:614941]: A disorder due to abnormal CC development of two or more ectodermal structures, and characterized by CC sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth CC and the inability to sweat due to the absence of sweat glands. CC {ECO:0000269|PubMed:11780064, ECO:0000269|PubMed:17354266, CC ECO:0000269|PubMed:20222921}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; AY028914; AAK40288.1; -; mRNA. DR EMBL; AY071862; AAL60590.1; -; mRNA. DR EMBL; AY028912; AAK40285.1; -; Genomic_DNA. DR EMBL; AY028906; AAK40285.1; JOINED; Genomic_DNA. DR EMBL; AY028908; AAK40285.1; JOINED; Genomic_DNA. DR EMBL; AY028909; AAK40285.1; JOINED; Genomic_DNA. DR EMBL; AY028910; AAK40285.1; JOINED; Genomic_DNA. DR EMBL; AY028911; AAK40285.1; JOINED; Genomic_DNA. DR EMBL; AY028912; AAK40286.1; -; Genomic_DNA. DR EMBL; AY028907; AAK40286.1; JOINED; Genomic_DNA. DR EMBL; AY028908; AAK40286.1; JOINED; Genomic_DNA. DR EMBL; AY028909; AAK40286.1; JOINED; Genomic_DNA. DR EMBL; AY028910; AAK40286.1; JOINED; Genomic_DNA. DR EMBL; AY028911; AAK40286.1; JOINED; Genomic_DNA. DR EMBL; AY028913; AAK40287.1; -; mRNA. DR EMBL; AK290862; BAF83551.1; -; mRNA. DR EMBL; AK291930; BAF84619.1; -; mRNA. DR EMBL; AK314634; BAG37197.1; -; mRNA. DR EMBL; AL354693; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL136105; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471098; EAW70052.1; -; Genomic_DNA. DR EMBL; BC128082; AAI28083.1; -; mRNA. DR CCDS; CCDS1610.1; -. [Q8WWZ3-1] DR CCDS; CCDS31065.1; -. [Q8WWZ3-2] DR RefSeq; NP_542776.1; NM_080738.3. [Q8WWZ3-2] DR RefSeq; NP_665860.2; NM_145861.2. [Q8WWZ3-1] DR AlphaFoldDB; Q8WWZ3; -. DR SMR; Q8WWZ3; -. DR BioGRID; 126096; 15. DR IntAct; Q8WWZ3; 12. DR STRING; 9606.ENSP00000335076; -. DR iPTMnet; Q8WWZ3; -. DR PhosphoSitePlus; Q8WWZ3; -. DR BioMuta; EDARADD; -. DR DMDM; 212276512; -. DR EPD; Q8WWZ3; -. DR jPOST; Q8WWZ3; -. DR MassIVE; Q8WWZ3; -. DR MaxQB; Q8WWZ3; -. DR PaxDb; 9606-ENSP00000335076; -. DR PeptideAtlas; Q8WWZ3; -. DR ProteomicsDB; 74963; -. [Q8WWZ3-1] DR ProteomicsDB; 74964; -. [Q8WWZ3-2] DR Pumba; Q8WWZ3; -. DR Antibodypedia; 20814; 55 antibodies from 15 providers. DR DNASU; 128178; -. DR Ensembl; ENST00000334232.9; ENSP00000335076.4; ENSG00000186197.15. [Q8WWZ3-1] DR Ensembl; ENST00000359362.6; ENSP00000352320.4; ENSG00000186197.15. [Q8WWZ3-2] DR GeneID; 128178; -. DR KEGG; hsa:128178; -. DR MANE-Select; ENST00000334232.9; ENSP00000335076.4; NM_145861.4; NP_665860.2. DR UCSC; uc001hxu.2; human. [Q8WWZ3-1] DR AGR; HGNC:14341; -. DR CTD; 128178; -. DR DisGeNET; 128178; -. DR GeneCards; EDARADD; -. DR GeneReviews; EDARADD; -. DR HGNC; HGNC:14341; EDARADD. DR HPA; ENSG00000186197; Tissue enhanced (urinary). DR MalaCards; EDARADD; -. DR MIM; 606603; gene. DR MIM; 614940; phenotype. DR MIM; 614941; phenotype. DR neXtProt; NX_Q8WWZ3; -. DR OpenTargets; ENSG00000186197; -. DR Orphanet; 1810; Autosomal dominant hypohidrotic ectodermal dysplasia. DR Orphanet; 248; Autosomal recessive hypohidrotic ectodermal dysplasia. DR Orphanet; 99798; Oligodontia. DR PharmGKB; PA27603; -. DR VEuPathDB; HostDB:ENSG00000186197; -. DR eggNOG; KOG4602; Eukaryota. DR GeneTree; ENSGT00390000001136; -. DR HOGENOM; CLU_085398_0_0_1; -. DR InParanoid; Q8WWZ3; -. DR OMA; DEEYQTD; -. DR OrthoDB; 4629855at2759; -. DR PhylomeDB; Q8WWZ3; -. DR TreeFam; TF335658; -. DR PathwayCommons; Q8WWZ3; -. DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors. DR SignaLink; Q8WWZ3; -. DR BioGRID-ORCS; 128178; 12 hits in 1149 CRISPR screens. DR ChiTaRS; EDARADD; human. DR GeneWiki; EDARADD; -. DR GenomeRNAi; 128178; -. DR Pharos; Q8WWZ3; Tbio. DR PRO; PR:Q8WWZ3; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8WWZ3; Protein. DR Bgee; ENSG00000186197; Expressed in islet of Langerhans and 95 other cell types or tissues. DR ExpressionAtlas; Q8WWZ3; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR000488; Death_domain. DR InterPro; IPR039200; EDARADD. DR PANTHER; PTHR28469; ECTODYSPLASIN-A RECEPTOR-ASSOCIATED ADAPTER PROTEIN; 1. DR PANTHER; PTHR28469:SF1; ECTODYSPLASIN-A RECEPTOR-ASSOCIATED ADAPTER PROTEIN; 1. DR Pfam; PF00531; Death; 1. DR SUPFAM; SSF47986; DEATH domain; 1. DR Genevisible; Q8WWZ3; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation; KW Disease variant; Ectodermal dysplasia; Reference proteome. FT CHAIN 1..215 FT /note="Ectodysplasin-A receptor-associated adapter protein" FT /id="PRO_0000086928" FT DOMAIN 123..202 FT /note="Death" FT REGION 1..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 62..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 14..29 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 62..79 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..20 FT /note="MGLRTTKQMGRGTKAPGHQE -> MASPDDPLRA (in isoform B)" FT /evidence="ECO:0000303|PubMed:11780064, FT ECO:0000303|PubMed:11882293, ECO:0000303|PubMed:14702039" FT /id="VSP_003861" FT VARIANT 9 FT /note="M -> I (in dbSNP:rs966365)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_050963" FT VARIANT 103 FT /note="S -> F (in dbSNP:rs114632254)" FT /evidence="ECO:0000269|PubMed:18231121" FT /id="VAR_054509" FT VARIANT 114 FT /note="D -> Y (in ECTD11A)" FT /evidence="ECO:0000269|PubMed:20979233" FT /id="VAR_064835" FT VARIANT 122 FT /note="L -> R (in ECTD11A; severely impairs NF-kappa-B FT activation and acted in a dominant-negative manner; FT dbSNP:rs121908116)" FT /evidence="ECO:0000269|PubMed:17354266" FT /id="VAR_054510" FT VARIANT 135..136 FT /note="Missing (in ECTD11B; impairs the interaction with FT EDAR and severely inhibits NF-kappa-B activity)" FT /evidence="ECO:0000269|PubMed:20222921" FT /id="VAR_064836" FT VARIANT 152 FT /note="E -> K (in ECTD11B; may reduce binding to EDAR; FT impairs NF-kappa-B activation by about 50%; FT dbSNP:rs74315309)" FT /evidence="ECO:0000269|PubMed:11780064, FT ECO:0000269|PubMed:17354266" FT /id="VAR_013482" SQ SEQUENCE 215 AA; 24802 MW; 25C198E3CA1F68F2 CRC64; MGLRTTKQMG RGTKAPGHQE DHMVKEPVED TDPSTLSFNM SDKYPIQDTE LPKAEECDTI TLNCPRNSDM KNQGEENGFP DSTGDPLPEI SKDNSCKENC TCSSCLLRAP TISDLLNDQD LLDVIRIKLD PCHPTVKNWR NFASKWGMSY DELCFLEQRP QSPTLEFLLR NSQRTVGQLM ELCRLYHRAD VEKVLRRWVD EEWPKRERGD PSRHF //