ELMD3_HUMAN
ID ELMD3_HUMAN Reviewed; 381 AA.
AC Q96FG2; B8ZZD6; D6W5K4; Q2M1K3; Q2XSU3; Q2XSU4; Q8NAC1; Q8TCK4; Q8WV70;
AC Q8WY75; Q9H6Q8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=ELMO domain-containing protein 3;
DE AltName: Full=RNA-binding motif and ELMO domain-containing protein 1;
DE AltName: Full=RNA-binding motif protein 29;
DE AltName: Full=RNA-binding protein 29;
GN Name=ELMOD3; Synonyms=RBED1, RBM29; ORFNames=PP4068;
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] (ISOFORMS 2 AND 5).
RA Wang P., Deng W., Lu Y., He P., Gao X., Shi T., Ma D.;
RT "RBED1, an AP1-inhibiting protein.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hepatoma, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RC TISSUE=Brain, and Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-381 (ISOFORM 5).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP INVOLVEMENT IN DFNA88, VARIANT DFNB88 SER-265, FUNCTION, SUBCELLULAR
RP LOCATION, IDENTIFICATION OF ISOFORMS 1 AND 6, AND TISSUE SPECIFICITY.
RX PubMed=24039609; DOI=10.1371/journal.pgen.1003774;
RA Jaworek T.J., Richard E.M., Ivanova A.A., Giese A.P., Choo D.I., Khan S.N.,
RA Riazuddin S., Kahn R.A., Riazuddin S.;
RT "An alteration in ELMOD3, an Arl2 GTPase-activating protein, is associated
RT with hearing impairment in humans.";
RL PLoS Genet. 9:E1003774-E1003774(2013).
RN [9]
RP INVOLVEMENT IN DFNA81, VARIANT DFNA81 ARG-171, CHARACTERIZATION OF VARIANT
RP DFNA81 ARG-171, AND SUBCELLULAR LOCATION.
RX PubMed=29713870; DOI=10.1007/s00439-018-1885-0;
RA Li W., Sun J., Ling J., Li J., He C., Liu Y., Chen H., Men M., Niu Z.,
RA Deng Y., Li M., Li T., Wen J., Sang S., Li H., Wan Z., Richard E.M.,
RA Chapagain P., Yan D., Liu X.Z., Mei L., Feng Y.;
RT "ELMOD3, a novel causative gene, associated with human autosomal dominant
RT nonsyndromic and progressive hearing loss.";
RL Hum. Genet. 137:329-342(2018).
CC -!- FUNCTION: Acts as a GTPase-activating protein (GAP) for ARL2 with low
CC specific activity. {ECO:0000269|PubMed:24039609}.
CC -!- INTERACTION:
CC Q96FG2; P43360: MAGEA6; NbExp=3; IntAct=EBI-10285740, EBI-1045155;
CC -!- SUBCELLULAR LOCATION: Cell projection, stereocilium
CC {ECO:0000269|PubMed:24039609}. Cell projection, kinocilium
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24039609,
CC ECO:0000269|PubMed:29713870}. Note=Also present in the cuticular plate
CC of auditory hair cells. Expressed along the length of the stereocilia,
CC but excluded from the very tip (By similarity). Colocalizes with F-
CC actin cytoskeleton. {ECO:0000269|PubMed:29713870}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=B/C/D;
CC IsoId=Q96FG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96FG2-2; Sequence=VSP_022922, VSP_022923;
CC Name=3;
CC IsoId=Q96FG2-3; Sequence=VSP_022918;
CC Name=5;
CC IsoId=Q96FG2-5; Sequence=VSP_022919, VSP_022920;
CC Name=6; Synonyms=A;
CC IsoId=Q96FG2-6; Sequence=VSP_022924;
CC -!- TISSUE SPECIFICITY: Both isoform 1 and isoform 6 are widely expressed.
CC {ECO:0000269|PubMed:24039609}.
CC -!- DISEASE: Deafness, autosomal recessive, 88 (DFNB88) [MIM:615429]: A
CC form of non-syndromic deafness characterized by prelingual onset of
CC severe to profound mixed conductive and sensorineural hearing loss.
CC {ECO:0000269|PubMed:24039609}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, autosomal dominant, 81 (DFNA81) [MIM:619500]: A form
CC of non-syndromic, sensorineural hearing loss. Sensorineural hearing
CC loss results from damage to the neural receptors of the inner ear, the
CC nerve pathways to the brain, or the area of the brain that receives
CC sound information. DNFA81 is characterized by postlingual onset of
CC slowly progressive deafness. {ECO:0000269|PubMed:29713870}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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; DQ256726; ABB69067.1; -; mRNA.
DR EMBL; DQ256727; ABB69068.1; -; mRNA.
DR EMBL; AK025630; BAB15195.1; -; mRNA.
DR EMBL; AF258573; AAG23776.1; -; mRNA.
DR EMBL; AC062037; AAY24127.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99521.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99522.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99523.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99526.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99528.1; -; Genomic_DNA.
DR EMBL; BC001942; AAH01942.1; -; mRNA.
DR EMBL; BC010991; AAH10991.1; -; mRNA.
DR EMBL; BC018666; AAH18666.1; -; mRNA.
DR EMBL; BC112324; AAI12325.1; -; mRNA.
DR EMBL; AL713718; CAD28512.1; -; mRNA.
DR CCDS; CCDS46352.1; -. [Q96FG2-1]
DR RefSeq; NP_001128493.1; NM_001135021.1. [Q96FG2-1]
DR RefSeq; NP_001128494.1; NM_001135022.1. [Q96FG2-1]
DR RefSeq; NP_001128495.1; NM_001135023.1. [Q96FG2-1]
DR RefSeq; NP_001316720.1; NM_001329791.1. [Q96FG2-1]
DR RefSeq; NP_001316721.1; NM_001329792.1. [Q96FG2-1]
DR RefSeq; NP_001316722.1; NM_001329793.1. [Q96FG2-1]
DR AlphaFoldDB; Q96FG2; -.
DR BioGRID; 123927; 14.
DR IntAct; Q96FG2; 3.
DR MINT; Q96FG2; -.
DR STRING; 9606.ENSP00000318264; -.
DR iPTMnet; Q96FG2; -.
DR PhosphoSitePlus; Q96FG2; -.
DR BioMuta; ELMOD3; -.
DR DMDM; 313104101; -.
DR MassIVE; Q96FG2; -.
DR MaxQB; Q96FG2; -.
DR PaxDb; Q96FG2; -.
DR PeptideAtlas; Q96FG2; -.
DR PRIDE; Q96FG2; -.
DR ProteomicsDB; 76524; -. [Q96FG2-1]
DR ProteomicsDB; 76525; -. [Q96FG2-2]
DR ProteomicsDB; 76526; -. [Q96FG2-3]
DR ProteomicsDB; 76527; -. [Q96FG2-5]
DR ProteomicsDB; 76528; -. [Q96FG2-6]
DR Antibodypedia; 1572; 94 antibodies from 23 providers.
DR DNASU; 84173; -.
DR Ensembl; ENST00000315658.11; ENSP00000318264.7; ENSG00000115459.18. [Q96FG2-6]
DR Ensembl; ENST00000393852.8; ENSP00000377434.4; ENSG00000115459.18. [Q96FG2-1]
DR Ensembl; ENST00000409013.8; ENSP00000387139.3; ENSG00000115459.18. [Q96FG2-1]
DR Ensembl; ENST00000409344.7; ENSP00000386248.3; ENSG00000115459.18. [Q96FG2-1]
DR Ensembl; ENST00000409890.6; ENSP00000386304.2; ENSG00000115459.18. [Q96FG2-1]
DR Ensembl; ENST00000410106.5; ENSP00000387134.1; ENSG00000115459.18. [Q96FG2-5]
DR Ensembl; ENST00000414593.5; ENSP00000394774.1; ENSG00000115459.18. [Q96FG2-3]
DR Ensembl; ENST00000444108.7; ENSP00000401984.2; ENSG00000115459.18. [Q96FG2-2]
DR Ensembl; ENST00000446464.7; ENSP00000407599.3; ENSG00000115459.18. [Q96FG2-2]
DR GeneID; 84173; -.
DR KEGG; hsa:84173; -.
DR MANE-Select; ENST00000409013.8; ENSP00000387139.3; NM_001135022.2; NP_001128494.1.
DR UCSC; uc002spf.5; human. [Q96FG2-1]
DR CTD; 84173; -.
DR DisGeNET; 84173; -.
DR GeneCards; ELMOD3; -.
DR HGNC; HGNC:26158; ELMOD3.
DR HPA; ENSG00000115459; Low tissue specificity.
DR MalaCards; ELMOD3; -.
DR MIM; 615427; gene.
DR MIM; 615429; phenotype.
DR MIM; 619500; phenotype.
DR neXtProt; NX_Q96FG2; -.
DR OpenTargets; ENSG00000115459; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA164719009; -.
DR VEuPathDB; HostDB:ENSG00000115459; -.
DR eggNOG; KOG2998; Eukaryota.
DR GeneTree; ENSGT00390000009488; -.
DR HOGENOM; CLU_060970_0_0_1; -.
DR InParanoid; Q96FG2; -.
DR OMA; PHWENIG; -.
DR OrthoDB; 1282549at2759; -.
DR PhylomeDB; Q96FG2; -.
DR TreeFam; TF323472; -.
DR PathwayCommons; Q96FG2; -.
DR SignaLink; Q96FG2; -.
DR BioGRID-ORCS; 84173; 28 hits in 1082 CRISPR screens.
DR ChiTaRS; ELMOD3; human.
DR GenomeRNAi; 84173; -.
DR Pharos; Q96FG2; Tdark.
DR PRO; PR:Q96FG2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96FG2; protein.
DR Bgee; ENSG00000115459; Expressed in subcutaneous adipose tissue and 119 other tissues.
DR ExpressionAtlas; Q96FG2; baseline and differential.
DR Genevisible; Q96FG2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0060091; C:kinocilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR InterPro; IPR006816; ELMO_dom.
DR InterPro; IPR030731; ELMOD3.
DR PANTHER; PTHR12771:SF2; PTHR12771:SF2; 1.
DR Pfam; PF04727; ELMO_CED12; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW Deafness; Disease variant; GTPase activation; Non-syndromic deafness;
KW Reference proteome.
FT CHAIN 1..381
FT /note="ELMO domain-containing protein 3"
FT /id="PRO_0000274903"
FT DOMAIN 170..324
FT /note="ELMO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00664"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 162..381
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_022918"
FT VAR_SEQ 163..185
FT /note="GLDSQDPVHGRVLQTIYKKLTGS -> ECNASPQGSCCICGWARPCVLTL
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.1"
FT /id="VSP_022919"
FT VAR_SEQ 186..381
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.1"
FT /id="VSP_022920"
FT VAR_SEQ 247..254
FT /note="QFPFCLMS -> IERNQGKG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_022922"
FT VAR_SEQ 255..381
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_022923"
FT VAR_SEQ 315..381
FT /note="ELEVLAKKSPRRLLKTLELYLARVSKGQASLLGAQKCYGPEAPPFKDLTFTG
FT ESDLQSHSSEGVWLI -> GVLFLLGRPRLNAQCPRSREPKVVARLVLAAVLPHPHFLK
FT FQLTKISITHPLESASSPFSALTVALFWSYTYDKHIF (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022924"
FT VARIANT 66
FT /note="R -> C (in dbSNP:rs7564372)"
FT /id="VAR_030362"
FT VARIANT 70
FT /note="T -> I (in dbSNP:rs955592)"
FT /id="VAR_030363"
FT VARIANT 171
FT /note="H -> R (in DFNA81; perturbed subcellular location
FT with loss of colocalization with F-actin in the cytoplasm
FT and concentration in the nucleus; may also have a shorter
FT half-life than the wild-type protein)"
FT /evidence="ECO:0000269|PubMed:29713870"
FT /id="VAR_086112"
FT VARIANT 265
FT /note="L -> S (in DFNB88; perturbed subcellular location
FT with loss of targeting to stereocilia and concentration in
FT the nucleus; loss of ARL2 GAP activity; dbSNP:rs587777040)"
FT /evidence="ECO:0000269|PubMed:24039609"
FT /id="VAR_070125"
FT CONFLICT 40
FT /note="R -> K (in Ref. 2; BAB15195)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="S -> G (in Ref. 3; AAG23776)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="A -> T (in Ref. 6; AAI12325)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="R -> L (in Ref. 6; AAH10991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 43046 MW; F40FF95FE89BA6A0 CRC64;
MNEKSCSFHS KEELRDGQGE RLSAGYSPSY DKDKSVLAFR GIPISELKNH GILQALTTEA
YEWEPRVVST EVVRAQEEWE AVDTIQPETG SQASSEQPGQ LISFSEALQH FQTVDLSPFK
KRIQPTIRRT GLAALRHYLF GPPKLHQRLR EERDLVLTIA QCGLDSQDPV HGRVLQTIYK
KLTGSKFDCA LHGNHWEDLG FQGANPATDL RGAGFLALLH LLYLVMDSKT LPMAQEIFRL
SRHHIQQFPF CLMSVNITHI AIQALREECL SRECNRQQKV IPVVNSFYAA TFLHLAHVWR
TQRKTISDSG FVLKELEVLA KKSPRRLLKT LELYLARVSK GQASLLGAQK CYGPEAPPFK
DLTFTGESDL QSHSSEGVWL I
