TTLL8_MOUSE
ID TTLL8_MOUSE Reviewed; 832 AA.
AC A4Q9F1; Q14B76; Q8C0N7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein monoglycylase TTLL8 {ECO:0000303|PubMed:19524510};
DE EC=6.3.2.- {ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:28576883};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 8 {ECO:0000303|PubMed:19524510};
GN Name=Ttll8 {ECO:0000312|EMBL:CAM84329.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:CAM84329.1};
RC TISSUE=Testis {ECO:0000312|EMBL:CAM84329.1};
RX PubMed=17499049; DOI=10.1016/j.molcel.2007.04.012;
RA van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.;
RT "A targeted multienzyme mechanism for selective microtubule
RT polyglutamylation.";
RL Mol. Cell 26:437-448(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26811.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC26811.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-832.
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19427864; DOI=10.1016/j.febslet.2009.05.003;
RA Ikegami K., Setou M.;
RT "TTLL10 can perform tubulin glycylation when co-expressed with TTLL8.";
RL FEBS Lett. 583:1957-1963(2009).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23897886; DOI=10.1083/jcb.201305041;
RA Bosch Grau M., Gonzalez Curto G., Rocha C., Magiera M.M., Marques Sousa P.,
RA Giordano T., Spassky N., Janke C.;
RT "Tubulin glycylases and glutamylases have distinct functions in
RT stabilization and motility of ependymal cilia.";
RL J. Cell Biol. 202:441-451(2013).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25180231; DOI=10.15252/embj.201488466;
RA Rocha C., Papon L., Cacheux W., Marques Sousa P., Lascano V., Tort O.,
RA Giordano T., Vacher S., Lemmers B., Mariani P., Meseure D., Medema J.P.,
RA Bieche I., Hahne M., Janke C.;
RT "Tubulin glycylases are required for primary cilia, control of cell
RT proliferation and tumor development in colon.";
RL EMBO J. 33:2247-2260(2014).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-93; ARG-96; LYS-104;
RP ARG-106; LYS-185; HIS-192; LYS-205; TRP-224; TYR-225; ASP-328; ASP-330;
RP ARG-619 AND ARG-631.
RX PubMed=28576883; DOI=10.1073/pnas.1617286114;
RA Garnham C.P., Yu I., Li Y., Roll-Mecak A.;
RT "Crystal structure of tubulin tyrosine ligase-like 3 reveals essential
RT architectural elements unique to tubulin monoglycylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6545-6550(2017).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=33414192; DOI=10.1126/science.abd4914;
RA Gadadhar S., Alvarez Viar G., Hansen J.N., Gong A., Kostarev A.,
RA Ialy-Radio C., Leboucher S., Whitfield M., Ziyyat A., Toure A., Alvarez L.,
RA Pigino G., Janke C.;
RT "Tubulin glycylation controls axonemal dynein activity, flagellar beat, and
RT male fertility.";
RL Science 371:0-0(2021).
CC -!- FUNCTION: Monoglycylase which modifies both tubulin and non-tubulin
CC proteins, adding a single glycine on the gamma-carboxyl groups of
CC specific glutamate residues to generate monoglycine side chains within
CC the C-terminal tail of target proteins (PubMed:19524510,
CC PubMed:28576883). Not involved in elongation step of the
CC polyglycylation reaction (PubMed:19524510). Preferentially
CC monoglycylates alpha-tubulin over beta-tubulin (PubMed:19524510).
CC Together with TTLL3, mediates microtubule glycylation of primary and
CC motile cilia, which is essential for their stability and maintenance
CC (PubMed:19524510, PubMed:23897886, PubMed:25180231). Together with
CC TTLL3, glycylates sperm flagella which regulates axonemal dynein motor
CC activity, thereby controlling flagellar beat, directional sperm
CC swimming and male fertility (PubMed:33414192). Monoglycylates non-
CC tubulin proteins such as ANP32A, ANP32B, SET, NCL and NAP1
CC (PubMed:19524510, PubMed:19427864). {ECO:0000269|PubMed:19427864,
CC ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:23897886,
CC ECO:0000269|PubMed:25180231, ECO:0000269|PubMed:28576883,
CC ECO:0000269|PubMed:33414192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-
CC glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180,
CC Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:28576883};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181;
CC Evidence={ECO:0000305|PubMed:19524510, ECO:0000305|PubMed:28576883};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510,
CC ECO:0000269|PubMed:33414192}. Cell projection, cilium
CC {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000269|PubMed:33414192}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis (PubMed:17499049,
CC PubMed:25180231). Expressed in brain, heart, kidney, liver, lung,
CC muscle, spleen and trachea (PubMed:17499049, PubMed:25180231,
CC PubMed:33414192). Expressed in sperm flagellum (PubMed:33414192). In
CC the brain, specifically expressed in ependymal cilia (PubMed:23897886).
CC {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:23897886,
CC ECO:0000269|PubMed:25180231, ECO:0000269|PubMed:33414192}.
CC -!- DOMAIN: Two conserved structural elements specific among
CC monoglycylases, IS1 and IS2, are involved in glycyl chains initiation.
CC Two conserved structural interfaces likely constitute the binding
CC platforms for tubulin tail and microtubule.
CC {ECO:0000269|PubMed:28576883}.
CC -!- DOMAIN: Arg-403 is the main determinant for regioselectivity, which
CC segregates between initiases and elongases in all tubulin--tyrosine
CC ligase family. A glutamine residue at this position is found in
CC elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-
CC chain elongation, whereas an arginine residue is found in initiases
CC TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
CC {ECO:0000250|UniProtKB:A4Q9E8}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous TTLL3 and TTLL8 knockout mice are
CC subfertile owing to aberrant beat patterns of their sperm flagella,
CC which impeded the straight swimming of sperm cells.
CC {ECO:0000269|PubMed:33414192}.
CC -!- CAUTION: TTLL3 and TTLL8 monoglycylase-mediated glycylation of tubulin
CC was initially reported to play a role in ependymal motile ciliary
CC maintenance (PubMed:23897886). However, contradictory results were
CC later observed (PubMed:33414192). {ECO:0000269|PubMed:23897886,
CC ECO:0000269|PubMed:33414192}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI16294.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI16295.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC26811.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM690752; CAM84329.1; -; mRNA.
DR EMBL; AK030151; BAC26811.1; ALT_INIT; mRNA.
DR EMBL; BC116293; AAI16294.1; ALT_INIT; mRNA.
DR EMBL; BC116294; AAI16295.1; ALT_FRAME; mRNA.
DR CCDS; CCDS27735.2; -.
DR RefSeq; NP_766406.2; NM_172818.3.
DR RefSeq; XP_006521019.1; XM_006520956.3.
DR RefSeq; XP_006521020.1; XM_006520957.2.
DR AlphaFoldDB; A4Q9F1; -.
DR SMR; A4Q9F1; -.
DR STRING; 10090.ENSMUSP00000104996; -.
DR iPTMnet; A4Q9F1; -.
DR PhosphoSitePlus; A4Q9F1; -.
DR PaxDb; A4Q9F1; -.
DR PRIDE; A4Q9F1; -.
DR ProteomicsDB; 297755; -.
DR Antibodypedia; 28278; 44 antibodies from 11 providers.
DR DNASU; 239591; -.
DR Ensembl; ENSMUST00000109371; ENSMUSP00000104996; ENSMUSG00000022388.
DR GeneID; 239591; -.
DR KEGG; mmu:239591; -.
DR UCSC; uc007xet.2; mouse.
DR CTD; 164714; -.
DR MGI; MGI:1922902; Ttll8.
DR VEuPathDB; HostDB:ENSMUSG00000022388; -.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000162265; -.
DR HOGENOM; CLU_010131_5_4_1; -.
DR InParanoid; A4Q9F1; -.
DR OMA; RMAFIED; -.
DR OrthoDB; 1137333at2759; -.
DR PhylomeDB; A4Q9F1; -.
DR TreeFam; TF313087; -.
DR Reactome; R-MMU-8955332; Carboxyterminal post-translational modifications of tubulin.
DR BioGRID-ORCS; 239591; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ttll8; mouse.
DR PRO; PR:A4Q9F1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; A4Q9F1; protein.
DR Bgee; ENSMUSG00000022388; Expressed in testis and 15 other tissues.
DR ExpressionAtlas; A4Q9F1; baseline and differential.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070735; F:protein-glycine ligase activity; IDA:UniProtKB.
DR GO; GO:0070736; F:protein-glycine ligase activity, initiating; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0003341; P:cilium movement; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0018094; P:protein polyglycylation; IDA:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Flagellum;
KW Ligase; Magnesium; Metal-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..832
FT /note="Protein monoglycylase TTLL8"
FT /id="PRO_0000326164"
FT DOMAIN 271..624
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 403..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 403
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:29973"
FT /ligand_part_note="L-glutamate acceptor residue in protein
FT target"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 435..438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:B2GUB3"
FT BINDING 448..450
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 492..493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 570
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:B2GUB3"
FT BINDING 583
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 583
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 585
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 403
FT /note="Essential for specifying initiation versus
FT elongation step of the polyglycylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT MUTAGEN 93
FT /note="K->E: Decreased monoglycylation activity; when
FT associated with E-96."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 96
FT /note="R->E: Decreased monoglycylation activity; when
FT associated with E-93."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 104
FT /note="K->E: Decreased monoglycylation activity; when
FT associated with E-106."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 106
FT /note="R->E: Decreased monoglycylation activity; when
FT associated with E-104."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 185
FT /note="K->E: Decreased monoglycylation activity."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 192
FT /note="H->E: Decreased monoglycylation activity."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 205
FT /note="K->E: Decreased monoglycylation activity."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 224
FT /note="W->A: Decreased monoglycylation activity."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 225
FT /note="Y->A: Decreased monoglycylation activity."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 328
FT /note="D->N: Decreased monoglycylation activity; when
FT associated with N-330."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 330
FT /note="D->N: Decreased monoglycylation activity; when
FT associated with N-328."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 619
FT /note="R->E: Decreased monoglycylation activity."
FT /evidence="ECO:0000269|PubMed:28576883"
FT MUTAGEN 631
FT /note="R->E: Decreased monoglycylation activity."
FT /evidence="ECO:0000269|PubMed:28576883"
SQ SEQUENCE 832 AA; 94915 MW; 086956A17633B1D7 CRC64;
MSCPPTPNPP FRPPSHTRVL RTPPLPPWVC LNSKSLSTGV GGQKNQLREA SMENGERKKL
SSTLSDGDHK EENKLKQGIP QDLSSSPKLD RYKIARQLTE KAIKERKIFS IYGHYPVIRA
TLRRKGWVEK KFNFFPKALQ NLGSEDKSAE TKENQEIALE RFDDIHDVMS RLVKNEIPYL
LWTIKRDVVD YHSLTCDQML NHYGKTASFT TKIGLCLNMR SLPWYVQANP NTFFPRCYGL
CTESEKQEFL DDFRRTVAAS ILKWVVLHQN YCSKVKGKSK KEEAKNSDPS PKKDPENPDL
KLPSLSGQVV DTACKVCQAY LGQLEHEDID VSEASTEALS EEEWNDLTQQ YYLLVHGNAS
ITDSKSYFAQ CQALLSKISS VNPQTEIDGI RNIWIIKPAA KSRGRDIVCM DRVENILSLV
AADSQTTKDN KWVVQKYIET PMLIYDTKFD IRQWFLVTDW NPLTIWFYKE SYLRFSTQRF
SLDKLDSAIH LCNNSIQRRL KNDKERSPLL PCHNMWTSTR FQEYLQKRGR GGTWGSIIYP
SMKRAVTNAM RVAQDHVEAR KNSFELYGAD FILGRDFKPW LIEINSSPTM HPSTPVTAQL
CAQVQEDTIK VVVDRKLDRN CDIGNFELLW RQPAVELPPF NGSDLCVEGI SVKKAKKQMP
PIASVGLSES LLDAPPKVRS ARALMETVIR PPRTTVRQDW KREEAKVLST TWSMPVMDAE
VRGRAKPIYA FEVNDYQHVD NKSHKSGYTR VQSSKVPGVT LTSAQHPALF AQTMKPTQMT
SSPPPTASGN HRDSSPFCPI VFEELWLHPN SQRRPSSCIL QSRAQGWIRG IP
