DHX37_HUMAN
ID DHX37_HUMAN Reviewed; 1157 AA.
AC Q8IY37; Q9BUI7; Q9P211;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Probable ATP-dependent RNA helicase DHX37;
DE EC=3.6.4.13 {ECO:0000269|PubMed:30582406};
DE AltName: Full=DEAH box protein 37;
GN Name=DHX37; Synonyms=DDX37, KIAA1517;
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], AND VARIANTS GLY-869 AND GLN-1081.
RC TISSUE=Brain, and Duodenum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-1157.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4]
RP INVOLVEMENT IN NEDBAVC, AND VARIANTS NEDBAVC LYS-419 AND HIS-487.
RX PubMed=26539891; DOI=10.1016/j.neuron.2015.09.048;
RA Karaca E., Harel T., Pehlivan D., Jhangiani S.N., Gambin T.,
RA Coban Akdemir Z., Gonzaga-Jauregui C., Erdin S., Bayram Y., Campbell I.M.,
RA Hunter J.V., Atik M.M., Van Esch H., Yuan B., Wiszniewski W., Isikay S.,
RA Yesil G., Yuregir O.O., Tug Bozdogan S., Aslan H., Aydin H., Tos T.,
RA Aksoy A., De Vivo D.C., Jain P., Geckinli B.B., Sezer O., Gul D.,
RA Durmaz B., Cogulu O., Ozkinay F., Topcu V., Candan S., Cebi A.H., Ikbal M.,
RA Yilmaz Gulec E., Gezdirici A., Koparir E., Ekici F., Coskun S., Cicek S.,
RA Karaer K., Koparir A., Duz M.B., Kirat E., Fenercioglu E., Ulucan H.,
RA Seven M., Guran T., Elcioglu N., Yildirim M.S., Aktas D., Alikasifoglu M.,
RA Ture M., Yakut T., Overton J.D., Yuksel A., Ozen M., Muzny D.M.,
RA Adams D.R., Boerwinkle E., Chung W.K., Gibbs R.A., Lupski J.R.;
RT "Genes that affect brain structure and function identified by rare variant
RT analyses of mendelian neurologic disease.";
RL Neuron 88:499-513(2015).
RN [5]
RP INVOLVEMENT IN SRXY11, VARIANTS SRXY11 MET-304; GLN-308; PHE-595 AND
RP TRP-674, AND FUNCTION.
RX PubMed=31287541; DOI=10.1210/jc.2019-00984;
RA da Silva T.E., Gomes N.L., Lerario A.M., Keegan C.E., Nishi M.Y.,
RA Carvalho F.M., Vilain E., Barseghyan H., Martinez-Aguayo A., Forclaz M.V.,
RA Papazian R., Pedroso de Paula L.C., Costa E.C., Carvalho L.R.,
RA Jorge A.A.L., Elias F.M., Mitchell R., Costa E.M.F., Mendonca B.B.,
RA Domenice S.;
RT "Genetic evidence of the association of DEAH-box helicase 37 defects with
RT 46,XY gonadal dysgenesis spectrum.";
RL J. Clin. Endocrinol. Metab. 104:5923-5934(2019).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP UTP14A, AND MUTAGENESIS OF THR-282.
RX PubMed=30582406; DOI=10.1080/15476286.2018.1556149;
RA Choudhury P., Hackert P., Memet I., Sloan K.E., Bohnsack M.T.;
RT "The human RNA helicase DHX37 is required for release of the U3 snoRNP from
RT pre-ribosomal particles.";
RL RNA Biol. 16:54-68(2019).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND VARIANTS NEDBAVC GLN-93; SER-167;
RP GLY-382; LYS-419; VAL-467; MET-731 AND MET-1094.
RX PubMed=31256877; DOI=10.1016/j.ajhg.2019.06.001;
RG University of Washington Center for Mendelian Genomics, Baylor-Hopkins Center for Mendelian Genomics, Telethon Undiagnosed Diseases Program;
RA Paine I., Posey J.E., Grochowski C.M., Jhangiani S.N., Rosenheck S.,
RA Kleyner R., Marmorale T., Yoon M., Wang K., Robison R., Cappuccio G.,
RA Pinelli M., Magli A., Coban Akdemir Z., Hui J., Yeung W.L., Wong B.K.Y.,
RA Ortega L., Bekheirnia M.R., Bierhals T., Hempel M., Johannsen J.,
RA Santer R., Aktas D., Alikasifoglu M., Bozdogan S., Aydin H., Karaca E.,
RA Bayram Y., Ityel H., Dorschner M., White J.J., Wilichowski E.,
RA Wortmann S.B., Casella E.B., Kitajima J.P., Kok F., Monteiro F.,
RA Muzny D.M., Bamshad M., Gibbs R.A., Sutton V.R., Van Esch H.,
RA Brunetti-Pierri N., Hildebrandt F., Brautbar A., Van den Veyver I.B.,
RA Glass I., Lessel D., Lyon G.J., Lupski J.R.;
RT "Paralog studies augment gene discovery: DDX and DHX genes.";
RL Am. J. Hum. Genet. 105:302-316(2019).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANTS SRXY11
RP MET-304; GLN-308; LEU-334; TRP-334; LEU-626; GLN-674 AND GLU-1030.
RX PubMed=31337883; DOI=10.1038/s41436-019-0606-y;
RA McElreavey K., Jorgensen A., Eozenou C., Merel T., Bignon-Topalovic J.,
RA Tan D.S., Houzelstein D., Buonocore F., Warr N., Kay R.G.G., Peycelon M.,
RA Siffroi J.P., Mazen I., Achermann J.C., Shcherbak Y., Leger J., Sallai A.,
RA Carel J.C., Martinerie L., Le Ru R., Conway G.S., Mignot B.,
RA Van Maldergem L., Bertalan R., Globa E., Brauner R., Jauch R., Nef S.,
RA Greenfield A., Bashamboo A.;
RT "Pathogenic variants in the DEAH-box RNA helicase DHX37 are a frequent
RT cause of 46,XY gonadal dysgenesis and 46,XY testicular regression
RT syndrome.";
RL Genet. Med. 22:150-159(2020).
CC -!- FUNCTION: ATP-binding RNA helicase that plays a role in maturation of
CC the small ribosomal subunit in ribosome biogenesis (PubMed:30582406).
CC Required for the release of the U3 snoRNP from pre-ribosomal particles
CC (PubMed:30582406). Plays a role in early testis development
CC (PubMed:31287541, PubMed:31337883). Probably also plays a role in brain
CC development (PubMed:31256877). {ECO:0000269|PubMed:30582406,
CC ECO:0000269|PubMed:31256877, ECO:0000269|PubMed:31287541,
CC ECO:0000269|PubMed:31337883}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:30582406};
CC -!- SUBUNIT: Interacts with UTP14A. {ECO:0000269|PubMed:30582406}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:30582406,
CC ECO:0000269|PubMed:31337883}. Cytoplasm {ECO:0000269|PubMed:31337883}.
CC Nucleus membrane {ECO:0000269|PubMed:31337883}.
CC -!- TISSUE SPECIFICITY: Expressed in the fallopian tube, ovary, uterus and
CC testis. Also expressed in the brain. {ECO:0000269|PubMed:31256877,
CC ECO:0000269|PubMed:31337883}.
CC -!- DISEASE: Neurodevelopmental disorder with brain anomalies and with or
CC without vertebral or cardiac anomalies (NEDBAVC) [MIM:618731]: An
CC autosomal recessive neurodevelopmental disorder characterized by severe
CC developmental delay, impaired intellectual development, hypotonia,
CC brain anomalies including cortical volume loss, corpus callosum
CC dysgenesis and cerebellar hypoplasia, and variable dysmorphic features.
CC Patients may have platyspondyly, scoliosis, and cardiac anomalies.
CC {ECO:0000269|PubMed:26539891, ECO:0000269|PubMed:31256877}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- DISEASE: 46,XY sex reversal 11 (SRXY11) [MIM:273250]: An autosomal
CC dominant disorder of sex development. Affected individuals have a 46,XY
CC karyotype and a genital phenotype that may range from predominantly
CC female to predominantly male, including marked sex ambiguity.
CC Approximately half of patients present with micropenis and bilateral or
CC unilateral cryptorchidism, and half present with female-appearing or
CC ambiguous external genitalia. {ECO:0000269|PubMed:31287541,
CC ECO:0000269|PubMed:31337883}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; BC002575; AAH02575.2; -; mRNA.
DR EMBL; BC037964; AAH37964.1; -; mRNA.
DR EMBL; AB040950; BAA96041.1; -; mRNA.
DR CCDS; CCDS9261.1; -.
DR RefSeq; NP_116045.2; NM_032656.3.
DR PDB; 7MQA; EM; 2.70 A; NS=1-1157.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q8IY37; -.
DR SMR; Q8IY37; -.
DR BioGRID; 121684; 172.
DR IntAct; Q8IY37; 19.
DR MINT; Q8IY37; -.
DR STRING; 9606.ENSP00000311135; -.
DR iPTMnet; Q8IY37; -.
DR MetOSite; Q8IY37; -.
DR PhosphoSitePlus; Q8IY37; -.
DR BioMuta; DHX37; -.
DR DMDM; 38257651; -.
DR EPD; Q8IY37; -.
DR jPOST; Q8IY37; -.
DR MassIVE; Q8IY37; -.
DR MaxQB; Q8IY37; -.
DR PaxDb; Q8IY37; -.
DR PeptideAtlas; Q8IY37; -.
DR PRIDE; Q8IY37; -.
DR ProteomicsDB; 71103; -.
DR Antibodypedia; 31893; 46 antibodies from 13 providers.
DR DNASU; 57647; -.
DR Ensembl; ENST00000308736.7; ENSP00000311135.2; ENSG00000150990.9.
DR GeneID; 57647; -.
DR KEGG; hsa:57647; -.
DR MANE-Select; ENST00000308736.7; ENSP00000311135.2; NM_032656.4; NP_116045.2.
DR UCSC; uc001ugy.4; human.
DR CTD; 57647; -.
DR DisGeNET; 57647; -.
DR GeneCards; DHX37; -.
DR HGNC; HGNC:17210; DHX37.
DR HPA; ENSG00000150990; Low tissue specificity.
DR MalaCards; DHX37; -.
DR MIM; 273250; phenotype.
DR MIM; 617362; gene.
DR MIM; 618731; phenotype.
DR neXtProt; NX_Q8IY37; -.
DR OpenTargets; ENSG00000150990; -.
DR Orphanet; 242; 46,XY complete gonadal dysgenesis.
DR Orphanet; 251510; 46,XY partial gonadal dysgenesis.
DR Orphanet; 983; Testicular regression syndrome.
DR PharmGKB; PA27224; -.
DR VEuPathDB; HostDB:ENSG00000150990; -.
DR eggNOG; KOG0926; Eukaryota.
DR GeneTree; ENSGT00550000074985; -.
DR InParanoid; Q8IY37; -.
DR OMA; QICAAGF; -.
DR OrthoDB; 354219at2759; -.
DR PhylomeDB; Q8IY37; -.
DR TreeFam; TF105654; -.
DR PathwayCommons; Q8IY37; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q8IY37; -.
DR BioGRID-ORCS; 57647; 747 hits in 1050 CRISPR screens.
DR ChiTaRS; DHX37; human.
DR GenomeRNAi; 57647; -.
DR Pharos; Q8IY37; Tdark.
DR PRO; PR:Q8IY37; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8IY37; protein.
DR Bgee; ENSG00000150990; Expressed in tendon of biceps brachii and 164 other tissues.
DR ExpressionAtlas; Q8IY37; baseline and differential.
DR Genevisible; Q8IY37; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:2000020; P:positive regulation of male gonad development; IDA:UniProtKB.
DR GO; GO:0042255; P:ribosome assembly; IDA:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Disease variant; Helicase; Hydrolase;
KW Intellectual disability; Membrane; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1157
FT /note="Probable ATP-dependent RNA helicase DHX37"
FT /id="PRO_0000055172"
FT DOMAIN 262..429
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 459..716
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 372..375
FT /note="DEAH box"
FT COMPBIAS 161..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..573
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 275..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VARIANT 93
FT /note="R -> Q (in NEDBAVC; unknown pathological
FT significance; dbSNP:rs575837056)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083628"
FT VARIANT 96
FT /note="M -> I (in dbSNP:rs11558556)"
FT /id="VAR_061826"
FT VARIANT 167
FT /note="E -> S (in NEDBAVC; unknown pathological
FT significance; requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083629"
FT VARIANT 304
FT /note="T -> M (in SRXY11)"
FT /evidence="ECO:0000269|PubMed:31287541,
FT ECO:0000269|PubMed:31337883"
FT /id="VAR_083630"
FT VARIANT 308
FT /note="R -> Q (in SRXY11; dbSNP:rs1384892917)"
FT /evidence="ECO:0000269|PubMed:31287541,
FT ECO:0000269|PubMed:31337883"
FT /id="VAR_083631"
FT VARIANT 334
FT /note="R -> L (in SRXY11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31337883"
FT /id="VAR_083632"
FT VARIANT 334
FT /note="R -> W (in SRXY11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31337883"
FT /id="VAR_083633"
FT VARIANT 382
FT /note="D -> G (in NEDBAVC; unknown pathological
FT significance; dbSNP:rs1424699115)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083634"
FT VARIANT 419
FT /note="N -> K (in NEDBAVC; unknown pathological
FT significance; dbSNP:rs1060499737)"
FT /evidence="ECO:0000269|PubMed:26539891,
FT ECO:0000269|PubMed:31256877"
FT /id="VAR_083635"
FT VARIANT 458
FT /note="R -> Q (in dbSNP:rs11057939)"
FT /id="VAR_052185"
FT VARIANT 467
FT /note="L -> V (in NEDBAVC; unknown pathological
FT significance; dbSNP:rs149331610)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083636"
FT VARIANT 487
FT /note="R -> H (in NEDBAVC; unknown pathological
FT significance; dbSNP:rs779613772)"
FT /evidence="ECO:0000269|PubMed:26539891"
FT /id="VAR_083637"
FT VARIANT 508
FT /note="K -> N (in dbSNP:rs35165507)"
FT /id="VAR_052186"
FT VARIANT 595
FT /note="S -> F (in SRXY11)"
FT /evidence="ECO:0000269|PubMed:31287541"
FT /id="VAR_083638"
FT VARIANT 626
FT /note="S -> L (in SRXY11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31337883"
FT /id="VAR_083639"
FT VARIANT 674
FT /note="R -> Q (in SRXY11)"
FT /evidence="ECO:0000269|PubMed:31337883"
FT /id="VAR_083640"
FT VARIANT 674
FT /note="R -> W (in SRXY11)"
FT /evidence="ECO:0000269|PubMed:31287541"
FT /id="VAR_083641"
FT VARIANT 717
FT /note="V -> I (in dbSNP:rs35016004)"
FT /id="VAR_052187"
FT VARIANT 731
FT /note="V -> M (in NEDBAVC; unknown pathological
FT significance; dbSNP:rs754186165)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083642"
FT VARIANT 869
FT /note="S -> G (in dbSNP:rs4516060)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052188"
FT VARIANT 1030
FT /note="G -> E (in SRXY11; unknown pathological
FT significance; dbSNP:rs754141645)"
FT /evidence="ECO:0000269|PubMed:31337883"
FT /id="VAR_083643"
FT VARIANT 1081
FT /note="R -> Q (in dbSNP:rs4447263)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052189"
FT VARIANT 1094
FT /note="T -> M (in NEDBAVC; unknown pathological
FT significance; dbSNP:rs1277857720)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083644"
FT MUTAGEN 282
FT /note="T->A: Impairs the catalytic activity of the
FT helicase."
FT /evidence="ECO:0000269|PubMed:30582406"
FT CONFLICT 174
FT /note="E -> R (in Ref. 1; AAH02575)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="A -> S (in Ref. 2; BAA96041)"
FT /evidence="ECO:0000305"
FT CONFLICT 1130..1157
FT /note="YLLAEYCEWLPQAMHPDIEKAWPPTTVH -> CEFDQGQGVGVDRMGSLRQG
FT LCALCTVSPGLAEGSGPTAAGQLFAT (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1157 AA; 129545 MW; 49332175221B30C5 CRC64;
MGKLRRRYNI KGRQQAGPGP SKGPPEPPPV QLELEDKDTL KGVDASNALV LPGKKKKKTK
APPLSKKEKK PLTKKEKKVL QKILEQKEKK SQRAEMLQKL SEVQASEAEM RLFYTTSKLG
TGNRMYHTKE KADEVVAPGQ EKISSLSGAH RKRRRWPSAE EEEEEEEESE SELEEESELD
EDPAAEPAEA GVGTTVAPLP PAPAPSSQPV PAGMTVPPPP AAAPPLPRAL AKPAVFIPVN
RSPEMQEERL KLPILSEEQV IMEAVAEHPI VIVCGETGSG KTTQVPQFLY EAGFSSEDSI
IGVTEPRRVA AVAMSQRVAK EMNLSQRVVS YQIRYEGNVT EETRIKFMTD GVLLKEIQKD
FLLLRYKVVI IDEAHERSVY TDILIGLLSR IVTLRAKRNL PLKLLIMSAT LRVEDFTQNP
RLFAKPPPVI KVESRQFPVT VHFNKRTPLE DYSGECFRKV CKIHRMLPAG GILVFLTGQA
EVHALCRRLR KAFPPSRARP QEKDDDQKDS VEEMRKFKKS RARAKKARAE VLPQINLDHY
SVLPAGEGDE DREAEVDEEE GALDSDLDLD LGDGGQDGGE QPDASLPLHV LPLYSLLAPE
KQAQVFKPPP EGTRLCVVAT NVAETSLTIP GIKYVVDCGK VKKRYYDRVT GVSSFRVTWV
SQASADQRAG RAGRTEPGHC YRLYSSAVFG DFEQFPPPEI TRRPVEDLIL QMKALNVEKV
INFPFPTPPS VEALLAAEEL LIALGALQPP QKAERVKQLQ ENRLSCPITA LGRTMATFPV
APRYAKMLAL SRQHGCLPYA ITIVASMTVR ELFEELDRPA ASDEELTRLK SKRARVAQMK
RTWAGQGASL KLGDLMVLLG AVGACEYASC TPQFCEANGL RYKAMMEIRR LRGQLTTAVN
AVCPEAELFV DPKMQPPTES QVTYLRQIVT AGLGDHLARR VQSEEMLEDK WRNAYKTPLL
DDPVFIHPSS VLFKELPEFV VYQEIVETTK MYMKGVSSVE VQWIPALLPS YCQFDKPLEE
PAPTYCPERG RVLCHRASVF YRVGWPLPAI EVDFPEGIDR YKHFARFLLE GQVFRKLASY
RSCLLSSPGT MLKTWARLQP RTESLLRALV AEKADCHEAL LAAWKKNPKY LLAEYCEWLP
QAMHPDIEKA WPPTTVH
