ID USH1G_HUMAN Reviewed; 461 AA. AC Q495M9; Q8N251; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 25-MAY-2022, entry version 156. DE RecName: Full=Usher syndrome type-1G protein; DE AltName: Full=Scaffold protein containing ankyrin repeats and SAM domain; GN Name=USH1G; Synonyms=SANS; 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 [LARGE SCALE MRNA]. 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., 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP INTERACTION WITH PDZD7. RX PubMed=19028668; DOI=10.1093/hmg/ddn395; RA Schneider E., Marker T., Daser A., Frey-Mahn G., Beyer V., Farcas R., RA Schneider-Ratzke B., Kohlschmidt N., Grossmann B., Bauss K., Napiontek U., RA Keilmann A., Bartsch O., Zechner U., Wolfrum U., Haaf T.; RT "Homozygous disruption of PDZD7 by reciprocal translocation in a RT consanguineous family: a new member of the Usher syndrome protein RT interactome causing congenital hearing impairment."; RL Hum. Mol. Genet. 18:655-666(2009). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH MYO7A; RP USH1C AND USH1G. RX PubMed=21709241; DOI=10.1073/pnas.1104161108; RA Grati M., Kachar B.; RT "Myosin VIIa and sans localization at stereocilia upper tip-link density RT implicates these Usher syndrome proteins in mechanotransduction."; RL Proc. Natl. Acad. Sci. U.S.A. 108:11476-11481(2011). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 388-461 IN COMPLEX WITH USH1C, RP INTERACTION WITH USH1C, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF RP VARIANT USH1G VAL-458. RX PubMed=20142502; DOI=10.1073/pnas.0911385107; RA Yan J., Pan L., Chen X., Wu L., Zhang M.; RT "The structure of the harmonin/sans complex reveals an unexpected RT interaction mode of the two Usher syndrome proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 107:4040-4045(2010). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 295-390 IN COMPLEX WITH MYO7A, RP STRUCTURE BY NMR OF 370-380, INTERACTION WITH MYO7A, AND MUTAGENESIS OF RP PHE-307; PHE-317 AND TRP-374. RX PubMed=21311020; DOI=10.1126/science.1198848; RA Wu L., Pan L., Wei Z., Zhang M.; RT "Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo."; RL Science 331:757-760(2011). RN [7] RP VARIANT USH1G PRO-48, INTERACTION WITH USH1C, TISSUE SPECIFICITY, AND RP POSSIBLE FUNCTION. RX PubMed=12588794; DOI=10.1093/hmg/ddg051; RA Weil D., El-Amraoui A., Masmoudi S., Mustapha M., Kikkawa Y., Laine S., RA Delmaghani S., Adato A., Nadifi S., Zina Z.B., Hamel C., Gal A., Ayadi H., RA Yonekawa H., Petit C.; RT "Usher syndrome type I G (USH1G) is caused by mutations in the gene RT encoding SANS, a protein that associates with the USH1C protein, RT harmonin."; RL Hum. Mol. Genet. 12:463-471(2003). RN [8] RP VARIANT USH1G VAL-458. RX PubMed=16283141; DOI=10.1007/s00109-005-0719-4; RA Kalay E., de Brouwer A.P.M., Caylan R., Nabuurs S.B., Wollnik B., RA Karaguzel A., Heister J.G.A.M., Erdol H., Cremers F.P.M., Cremers C.W.R.J., RA Brunner H.G., Kremer H.; RT "A novel D458V mutation in the SANS PDZ binding motif causes atypical Usher RT syndrome."; RL J. Mol. Med. 83:1025-1032(2005). RN [9] RP INVOLVEMENT IN NON-SYNDROMIC SENSORINEURAL HEARING LOSS, AND VARIANT RP VAL-104. RX PubMed=25255398; DOI=10.1097/aud.0000000000000095; RA Oonk A.M., van Huet R.A., Leijendeckers J.M., Oostrik J., Venselaar H., RA van Wijk E., Beynon A., Kunst H.P., Hoyng C.B., Kremer H., Schraders M., RA Pennings R.J.; RT "Nonsyndromic hearing loss caused by USH1G mutations: widening the USH1G RT disease spectrum."; RL Ear Hear. 36:205-211(2015). CC -!- FUNCTION: Required for normal development and maintenance of cochlear CC hair cell bundles. Anchoring/scaffolding protein that is a part of the CC functional network formed by USH1C, USH1G, CDH23 and MYO7A that CC mediates mechanotransduction in cochlear hair cells. Required for CC normal hearing. {ECO:0000269|PubMed:21709241}. CC -!- SUBUNIT: Interacts with CDH23 and PCDH15; these interactions may CC recruit USH1G to the plasma membrane (By similarity). Interacts with CC USH1C (via the first PDZ domain) and with USH1G. Interacts with PDZD7. CC Interacts with MYO7A. Part of a complex composed of USH1C, USH1G and CC MYO7A. {ECO:0000250, ECO:0000269|PubMed:12588794, CC ECO:0000269|PubMed:19028668, ECO:0000269|PubMed:20142502, CC ECO:0000269|PubMed:21311020, ECO:0000269|PubMed:21709241}. CC -!- INTERACTION: CC Q495M9; X5D778: ANKRD11; NbExp=3; IntAct=EBI-8601749, EBI-17183751; CC Q495M9; Q13895: BYSL; NbExp=3; IntAct=EBI-8601749, EBI-358049; CC Q495M9; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-8601749, EBI-8643161; CC Q495M9; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-8601749, EBI-11530605; CC Q495M9; Q9HC52: CBX8; NbExp=3; IntAct=EBI-8601749, EBI-712912; CC Q495M9; Q9UER7: DAXX; NbExp=3; IntAct=EBI-8601749, EBI-77321; CC Q495M9; P26196: DDX6; NbExp=3; IntAct=EBI-8601749, EBI-351257; CC Q495M9; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-8601749, EBI-744099; CC Q495M9; Q96MY7: FAM161B; NbExp=4; IntAct=EBI-8601749, EBI-7225287; CC Q495M9; P22607: FGFR3; NbExp=3; IntAct=EBI-8601749, EBI-348399; CC Q495M9; P55040: GEM; NbExp=3; IntAct=EBI-8601749, EBI-744104; CC Q495M9; P09067: HOXB5; NbExp=3; IntAct=EBI-8601749, EBI-3893317; CC Q495M9; P01112: HRAS; NbExp=3; IntAct=EBI-8601749, EBI-350145; CC Q495M9; O43464: HTRA2; NbExp=3; IntAct=EBI-8601749, EBI-517086; CC Q495M9; P42858: HTT; NbExp=3; IntAct=EBI-8601749, EBI-466029; CC Q495M9; Q9C086: INO80B; NbExp=3; IntAct=EBI-8601749, EBI-715611; CC Q495M9; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-8601749, EBI-14069005; CC Q495M9; P25791-3: LMO2; NbExp=3; IntAct=EBI-8601749, EBI-11959475; CC Q495M9; I6L9F6: NEFL; NbExp=3; IntAct=EBI-8601749, EBI-10178578; CC Q495M9; P54646: PRKAA2; NbExp=3; IntAct=EBI-8601749, EBI-1383852; CC Q495M9; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-8601749, EBI-1567797; CC Q495M9; P41219: PRPH; NbExp=3; IntAct=EBI-8601749, EBI-752074; CC Q495M9; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-8601749, EBI-748391; CC Q495M9; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-8601749, EBI-11955057; CC Q495M9; Q9Y6N9: USH1C; NbExp=13; IntAct=EBI-8601749, EBI-954308; CC Q495M9; Q495M9: USH1G; NbExp=2; IntAct=EBI-8601749, EBI-8601749; CC Q495M9; Q9Y649; NbExp=3; IntAct=EBI-8601749, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. CC Note=Detected at the tip of cochlear hair cell stereocilia. Recruited CC to the cell membrane via interaction with CDH23 or PCDH15 (By CC similarity). {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in vestibule of the inner ear, eye and CC small intestine. {ECO:0000269|PubMed:12588794}. CC -!- DISEASE: Usher syndrome 1G (USH1G) [MIM:606943]: USH is a genetically CC heterogeneous condition characterized by the association of retinitis CC pigmentosa with sensorineural deafness. Age at onset and differences in CC auditory and vestibular function distinguish Usher syndrome type 1 CC (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). CC USH1 is characterized by profound congenital sensorineural deafness, CC absent vestibular function and prepubertal onset of progressive CC retinitis pigmentosa leading to blindness. CC {ECO:0000269|PubMed:12588794, ECO:0000269|PubMed:16283141, CC ECO:0000269|PubMed:20142502}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Note=The first cases with non-syndromic sensorineural hearing CC loss based on mutations in USH1G. The hearing loss has an onset during CC early childhood, is progressive, and has a downsloping audiogram CC configuration. Ophthalmic and vestibular abnormalities are absent. CC {ECO:0000269|PubMed:25255398}. 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; AK091243; BAC03619.1; -; mRNA. DR EMBL; BC101096; AAI01097.1; -; mRNA. DR EMBL; BC101097; AAI01098.1; -; mRNA. DR EMBL; BC101098; AAI01099.1; -; mRNA. DR EMBL; BC101099; AAI01100.1; -; mRNA. DR CCDS; CCDS32725.1; -. DR RefSeq; NP_001269418.1; NM_001282489.2. DR RefSeq; NP_775748.2; NM_173477.4. DR PDB; 2L7T; NMR; -; A=370-380. DR PDB; 3K1R; X-ray; 2.30 A; B=388-461. DR PDB; 3PVL; X-ray; 2.80 A; B=295-390. DR PDBsum; 2L7T; -. DR PDBsum; 3K1R; -. DR PDBsum; 3PVL; -. DR AlphaFoldDB; Q495M9; -. DR SMR; Q495M9; -. DR BioGRID; 125876; 22. DR CORUM; Q495M9; -. DR DIP; DIP-41617N; -. DR ELM; Q495M9; -. DR IntAct; Q495M9; 28. DR MINT; Q495M9; -. DR STRING; 9606.ENSP00000480279; -. DR iPTMnet; Q495M9; -. DR PhosphoSitePlus; Q495M9; -. DR BioMuta; USH1G; -. DR DMDM; 81175048; -. DR MassIVE; Q495M9; -. DR PaxDb; Q495M9; -. DR PeptideAtlas; Q495M9; -. DR PRIDE; Q495M9; -. DR ProteomicsDB; 61966; -. DR Antibodypedia; 19482; 51 antibodies from 17 providers. DR DNASU; 124590; -. DR Ensembl; ENST00000614341.5; ENSP00000480279.1; ENSG00000182040.9. DR GeneID; 124590; -. DR KEGG; hsa:124590; -. DR MANE-Select; ENST00000614341.5; ENSP00000480279.1; NM_173477.5; NP_775748.2. DR UCSC; uc032fra.2; human. DR CTD; 124590; -. DR DisGeNET; 124590; -. DR GeneCards; USH1G; -. DR GeneReviews; USH1G; -. DR HGNC; HGNC:16356; USH1G. DR HPA; ENSG00000182040; Tissue enhanced (esophagus). DR MalaCards; USH1G; -. DR MIM; 276900; phenotype. DR MIM; 606943; phenotype. DR MIM; 607696; gene. DR neXtProt; NX_Q495M9; -. DR OpenTargets; ENSG00000182040; -. DR Orphanet; 231169; Usher syndrome type 1. DR PharmGKB; PA38126; -. DR VEuPathDB; HostDB:ENSG00000182040; -. DR eggNOG; KOG0504; Eukaryota. DR GeneTree; ENSGT00390000017548; -. DR HOGENOM; CLU_028071_0_0_1; -. DR InParanoid; Q495M9; -. DR OMA; HSSTCPH; -. DR OrthoDB; 1344159at2759; -. DR PhylomeDB; Q495M9; -. DR TreeFam; TF324946; -. DR PathwayCommons; Q495M9; -. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea. DR SignaLink; Q495M9; -. DR SIGNOR; Q495M9; -. DR BioGRID-ORCS; 124590; 96 hits in 1067 CRISPR screens. DR EvolutionaryTrace; Q495M9; -. DR GeneWiki; USH1G; -. DR GenomeRNAi; 124590; -. DR Pharos; Q495M9; Tbio. DR PRO; PR:Q495M9; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q495M9; protein. DR Bgee; ENSG00000182040; Expressed in lower esophagus mucosa and 49 other tissues. DR ExpressionAtlas; Q495M9; baseline and differential. DR Genevisible; Q495M9; HS. DR GO; GO:0015629; C:actin cytoskeleton; ISS:HGNC-UCL. DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl. DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0030507; F:spectrin binding; IDA:MGI. DR GO; GO:0050957; P:equilibrioception; IMP:HGNC-UCL. DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl. DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl. DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:HGNC-UCL. DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:HGNC-UCL. DR GO; GO:0007605; P:sensory perception of sound; IMP:HGNC-UCL. DR CDD; cd09586; SAM_USH1G; 1. DR Gene3D; 1.10.150.50; -; 1. DR Gene3D; 1.25.40.20; -; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR037602; USH1G_SAM. DR Pfam; PF12796; Ank_2; 1. DR Pfam; PF00536; SAM_1; 1. DR SMART; SM00248; ANK; 3. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF47769; SSF47769; 1. DR SUPFAM; SSF48403; SSF48403; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 2. PE 1: Evidence at protein level; KW 3D-structure; ANK repeat; Cell membrane; Cytoplasm; Cytoskeleton; Deafness; KW Disease variant; Hearing; Membrane; Reference proteome; Repeat; KW Retinitis pigmentosa; Usher syndrome. FT CHAIN 1..461 FT /note="Usher syndrome type-1G protein" FT /id="PRO_0000067077" FT REPEAT 31..60 FT /note="ANK 1" FT REPEAT 64..93 FT /note="ANK 2" FT REPEAT 97..126 FT /note="ANK 3" FT DOMAIN 385..447 FT /note="SAM" FT REGION 208..243 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 332..368 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 221..239 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 349..366 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 48 FT /note="L -> P (in USH1G; dbSNP:rs104894651)" FT /evidence="ECO:0000269|PubMed:12588794" FT /id="VAR_023739" FT VARIANT 104 FT /note="M -> V (probable disease-associated variant found in FT patients with non-syndromic sensorineural hearing loss; FT dbSNP:rs149529031)" FT /evidence="ECO:0000269|PubMed:25255398" FT /id="VAR_072369" FT VARIANT 458 FT /note="D -> V (in USH1G; atypical form with mild retinitis FT pigmentosa and normal vestibular function; also found in FT patients with autosomal recessive non-syndromic deafness; FT strongly reduced affinity for USH1C; dbSNP:rs397517925)" FT /evidence="ECO:0000269|PubMed:16283141, FT ECO:0000269|PubMed:20142502" FT /id="VAR_060468" FT MUTAGEN 307 FT /note="F->E: Reduced affinity for MYO7A." FT /evidence="ECO:0000269|PubMed:21311020" FT MUTAGEN 317 FT /note="F->E: Reduced affinity for MYO7A." FT /evidence="ECO:0000269|PubMed:21311020" FT MUTAGEN 374 FT /note="W->Q: Strongly reduced affinity for MYO7A." FT /evidence="ECO:0000269|PubMed:21311020" FT CONFLICT 300 FT /note="D -> N (in Ref. 1; BAC03619)" FT /evidence="ECO:0000305" FT CONFLICT 402 FT /note="E -> G (in Ref. 1; BAC03619)" FT /evidence="ECO:0000305" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:3PVL" FT TURN 310..312 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 313..315 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:2L7T" FT HELIX 391..397 FT /evidence="ECO:0007829|PDB:3K1R" FT TURN 398..400 FT /evidence="ECO:0007829|PDB:3K1R" FT HELIX 402..404 FT /evidence="ECO:0007829|PDB:3K1R" FT HELIX 405..410 FT /evidence="ECO:0007829|PDB:3K1R" FT HELIX 415..418 FT /evidence="ECO:0007829|PDB:3K1R" FT HELIX 423..428 FT /evidence="ECO:0007829|PDB:3K1R" FT HELIX 433..451 FT /evidence="ECO:0007829|PDB:3K1R" FT STRAND 459..461 FT /evidence="ECO:0007829|PDB:3K1R" SQ SEQUENCE 461 AA; 51489 MW; B0ABB9F5711A5095 CRC64; MNDQYHRAAR DGYLELLKEA TRKELNAPDE DGMTPTLWAA YHGNLESLRL IVSRGGDPDK CDIWGNTPLH LAASNGHLHC LSFLVSFGAN IWCLDNDYHT PLDMAAMKGH MECVRYLDSI AAKQSSLNPK LVGKLKDKAF REAERRIREC AKLQRRHHER MERRYRRELA ERSDTLSFSS LTSSTLSRRL QHLALGSHLP YSQATLHGTA RGKTKMQKKL ERRKQGGEGT FKVSEDGRKS ARSLSGLQLG SDVMFVRQGT YANPKEWGRA PLRDMFLSDE DSVSRATLAA EPAHSEVSTD SGHDSLFTRP GLGTMVFRRN YLSSGLHGLG REDGGLDGVG APRGRLQSSP SLDDDSLGSA NSLQDRSCGE ELPWDELDLG LDEDLEPETS PLETFLASLH MEDFAALLRQ EKIDLEALML CSDLDLRSIS VPLGPRKKIL GAVRRRRQAM ERPPALEDTE L //