ID   TDRD9_HUMAN             Reviewed;        1382 AA.
AC   Q8NDG6; A1A4S7; Q6ZU54; Q8N7T3; Q8N827; Q8N9V5; Q96AS9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 3.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=ATP-dependent RNA helicase TDRD9 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:Q14BI7};
DE   AltName: Full=Tudor domain-containing protein 9 {ECO:0000305};
GN   Name=TDRD9 {ECO:0000312|HGNC:HGNC:20122};
GN   Synonyms=C14orf75 {ECO:0000312|HGNC:HGNC:20122};
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 GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-1382 (ISOFORM 1).
RC   TISSUE=Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-1382 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 635-1382 (ISOFORM 1).
RC   TISSUE=Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-1382 (ISOFORM 1).
RC   TISSUE=Bone marrow;
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   INVOLVEMENT IN SPGF30, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=28536242; DOI=10.1136/jmedgenet-2017-104514;
RA   Arafat M., Har-Vardi I., Harlev A., Levitas E., Zeadna A., Abofoul-Azab M.,
RA   Dyomin V., Sheffield V.C., Lunenfeld E., Huleihel M., Parvari R.;
RT   "Mutation in TDRD9 causes non-obstructive azoospermia in infertile men.";
RL   J. Med. Genet. 54:633-639(2017).
CC   -!- FUNCTION: ATP-binding RNA helicase required during spermatogenesis
CC       (PubMed:28536242). Required to repress transposable elements and
CC       prevent their mobilization, which is essential for the germline
CC       integrity. Acts via the piRNA metabolic process, which mediates the
CC       repression of transposable elements during meiosis by forming complexes
CC       composed of piRNAs and Piwi proteins and governs the methylation and
CC       subsequent repression of transposons. Acts downstream of piRNA
CC       biogenesis: exclusively required for transposon silencing in the
CC       nucleus, suggesting that it acts as a nuclear effector in the nucleus
CC       together with PIWIL4. {ECO:0000250|UniProtKB:Q14BI7,
CC       ECO:0000269|PubMed:28536242}.
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:0000250|UniProtKB:Q14BI7};
CC   -!- SUBUNIT: Interacts with piRNA-associated proteins PIWIL1 and PIWIL4.
CC       {ECO:0000269|PubMed:28536242}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28536242}. Nucleus
CC       {ECO:0000250|UniProtKB:Q14BI7}. Note=Component of the nuage, also named
CC       P granule, a germ-cell-specific organelle required to repress
CC       transposon activity during meiosis. Specifically localizes to piP-
CC       bodies, a subset of the nuage which contains secondary piRNAs. PIWIL2
CC       is required for its localization to piP-bodies.
CC       {ECO:0000250|UniProtKB:Q14BI7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8NDG6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NDG6-2; Sequence=VSP_033552;
CC   -!- DISEASE: Spermatogenic failure 30 (SPGF30) [MIM:618110]: An autosomal
CC       recessive infertility disorder caused by spermatogenesis defects that
CC       result in non-obstructive azoospermia or cryptozoospermia.
CC       {ECO:0000269|PubMed:28536242}. 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI28058.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI28058.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC04182.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC05047.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC05144.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC86372.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL132712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL136001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL833915; CAD38771.1; -; mRNA.
DR   EMBL; AK093483; BAC04182.1; ALT_INIT; mRNA.
DR   EMBL; AK097429; BAC05047.1; ALT_INIT; mRNA.
DR   EMBL; AK097699; BAC05144.1; ALT_INIT; mRNA.
DR   EMBL; AK125978; BAC86372.1; ALT_INIT; mRNA.
DR   EMBL; BC016796; AAH16796.1; -; mRNA.
DR   EMBL; BC128057; AAI28058.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS9987.2; -. [Q8NDG6-1]
DR   PIR; G02632; G02632.
DR   RefSeq; NP_694591.2; NM_153046.2. [Q8NDG6-1]
DR   AlphaFoldDB; Q8NDG6; -.
DR   SMR; Q8NDG6; -.
DR   BioGRID; 125766; 8.
DR   IntAct; Q8NDG6; 1.
DR   STRING; 9606.ENSP00000387303; -.
DR   iPTMnet; Q8NDG6; -.
DR   PhosphoSitePlus; Q8NDG6; -.
DR   BioMuta; TDRD9; -.
DR   EPD; Q8NDG6; -.
DR   MassIVE; Q8NDG6; -.
DR   PaxDb; 9606-ENSP00000387303; -.
DR   PeptideAtlas; Q8NDG6; -.
DR   ProteomicsDB; 73024; -. [Q8NDG6-1]
DR   ProteomicsDB; 73025; -. [Q8NDG6-2]
DR   Pumba; Q8NDG6; -.
DR   Antibodypedia; 47449; 91 antibodies from 16 providers.
DR   DNASU; 122402; -.
DR   Ensembl; ENST00000409874.9; ENSP00000387303.4; ENSG00000156414.20. [Q8NDG6-1]
DR   GeneID; 122402; -.
DR   KEGG; hsa:122402; -.
DR   MANE-Select; ENST00000409874.9; ENSP00000387303.4; NM_153046.3; NP_694591.2.
DR   UCSC; uc001yom.5; human. [Q8NDG6-1]
DR   AGR; HGNC:20122; -.
DR   CTD; 122402; -.
DR   DisGeNET; 122402; -.
DR   GeneCards; TDRD9; -.
DR   HGNC; HGNC:20122; TDRD9.
DR   HPA; ENSG00000156414; Group enriched (parathyroid gland, testis).
DR   MalaCards; TDRD9; -.
DR   MIM; 617963; gene.
DR   MIM; 618110; phenotype.
DR   neXtProt; NX_Q8NDG6; -.
DR   OpenTargets; ENSG00000156414; -.
DR   Orphanet; 399805; Male infertility with azoospermia or oligozoospermia due to single gene mutation.
DR   PharmGKB; PA134890186; -.
DR   VEuPathDB; HostDB:ENSG00000156414; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   GeneTree; ENSGT00940000157035; -.
DR   HOGENOM; CLU_002601_1_0_1; -.
DR   InParanoid; Q8NDG6; -.
DR   OMA; FWMHYIF; -.
DR   OrthoDB; 21853at2759; -.
DR   PhylomeDB; Q8NDG6; -.
DR   TreeFam; TF324869; -.
DR   PathwayCommons; Q8NDG6; -.
DR   Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR   SignaLink; Q8NDG6; -.
DR   BioGRID-ORCS; 122402; 7 hits in 1151 CRISPR screens.
DR   ChiTaRS; TDRD9; human.
DR   GenomeRNAi; 122402; -.
DR   Pharos; Q8NDG6; Tbio.
DR   PRO; PR:Q8NDG6; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q8NDG6; Protein.
DR   Bgee; ENSG00000156414; Expressed in right testis and 126 other cell types or tissues.
DR   ExpressionAtlas; Q8NDG6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0071547; C:piP-body; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR   GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR   GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0034587; P:piRNA processing; ISS:UniProtKB.
DR   GO; GO:0141006; P:piRNA-mediated retrotransposon silencing by heterochromatin formation; ISS:UniProtKB.
DR   GO; GO:0141007; P:siRNA-mediated retrotransposon silencing by heterochromatin formation; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR   CDD; cd17988; DEXHc_TDRD9; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   CDD; cd20431; Tudor_TDRD9; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 2.40.50.90; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR047384; Tudor_TDRD9.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF113; ATP-DEPENDENT RNA HELICASE TDRD9; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50304; TUDOR; 1.
DR   Genevisible; Q8NDG6; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW   Differentiation; Helicase; Hydrolase; Meiosis; Nucleotide-binding; Nucleus;
KW   Reference proteome; RNA-mediated gene silencing; Spermatogenesis.
FT   CHAIN           1..1382
FT                   /note="ATP-dependent RNA helicase TDRD9"
FT                   /id="PRO_0000333813"
FT   DOMAIN          142..308
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          377..544
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          944..1004
FT                   /note="Tudor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   REGION          36..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           254..257
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000250|UniProtKB:Q14BI7"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   VAR_SEQ         1095..1285
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033552"
FT   CONFLICT        758
FT                   /note="P -> L (in Ref. 3; BAC05047)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1260
FT                   /note="T -> G (in Ref. 4; AAH16796)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1276
FT                   /note="V -> F (in Ref. 3; BAC05144)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1382 AA;  155683 MW;  8A48E71E4A12041F CRC64;
     MLRKLTIEQI NDWFTIGKTV TNVELLGAPP AFPAGAAREE VQRQDVAPGA GPAAQAPALA
     QAPARPAAAF ERSLSQRSSE VEYINKYRQL EAQELDVCRS VQPTSGPGPR PSLAKLSSVT
     CIPGTTYKYP DLPISRYKEE VVSLIESNSV VIIHGATGSG KSTQLPQYIL DHYVQRSAYC
     SIVVTQPRKI GASSIARWIS KERAWTLGGV VGYQVGLEKI ATEDTRLIYM TTGVLLQKIV
     SAKSLMEFTH IIIDEVHERT EEMDFLLLVV RKLLRTNSRF VKVVLMSATI SCKEFADYFA
     VPVQNKMNPA YIFEVEGKPH SVEEYYLNDL EHIHHSKLSP HLLEEPVITK DIYEVAVSLI
     QMFDDLDMKE SGNKAWSGAQ FVLERSSVLV FLPGLGEINY MHELLTSLVH KRLQVYPLHS
     SVALEEQNNV FLSPVPGYRK IILSTNIAES SVTVPDVKYV IDFCLTRTLV CDEDTNYQSL
     RLSWASKTSC NQRKGRAGRV SRGYCYRLVH KDFWDNSIPD HVVPEMLRCP LGSTILKVKL
     LDMGEPRALL ATALSPPGLS DIERTILLLK EVGALAVSGQ REDENPHDGE LTFLGRVLAQ
     LPVNQQLGKL IVLGHVFGCL DECLIIAAAL SLKNFFAMPF RQHLDGYRNK VNFSGSSKSD
     CIALVEAFKT WKACRQTGEL RYPKDELNWG RLNYIQIKRI REVAELYEEL KTRISQFNMH
     VDSRRPVMDQ EYIYKQRFIL QVVLAGAFYP NYFTFGQPDE EMAVRELAGK DPKTTVVLKH
     IPPYGFLYYK QLQSLFRQCG QVKSIVFDGA KAFVEFSRNP TERFKTLPAV YMAIKMSQLK
     VSLELSVHSA EEIEGKVQGM NVSKLRNTRV NVDFQKQTVD PMQVSFNTSD RSQTVTDLLL
     TIDVTEVVEV GHFWGYRIDE NNSEILKKLT AEINQLTLVP LPTHPHPDLV CLAPFADFDK
     QRYFRAQVLY VSGNSAEVFF VDYGNKSHVD LHLLMEIPCQ FLELPFQALE FKICKMRPSA
     KSLVCGKHWS DGASQWFASL VSGCTLLVKV FSVVHSVLHV DVYQYSGVQD AINIRDVLIQ
     QGYAELTEES YESKQSHEVL KGLFSKSVEN MTDGSVPFPM KDDEKYLIRI LLESFSTNKL
     GTPNCKAELH GPFNPYELKC HSLTRISKFR CVWIEKESIN SVIISDAPED LHQRMLVAAS
     LSINATGSTM LLRETSLMPH IPGLPALLSM LFAPVIELRI DQNGKYYTGV LCGLGWNPAT
     GASILPEHDM ELAFDVQFSV EDVVEVNILR AAINKLVCDG PNGCKCLGPE RVAQLQDIAR
     QKLLGLFCQS KPREKIVPKW HEKPYEWNQV DPKLVMEQAD RESSRGKNTF LYQLHKLVVL
     GT
//