TTLL5_MOUSE
ID TTLL5_MOUSE Reviewed; 1328 AA.
AC Q8CHB8; A4Q9E7; Q3V468; Q8C1F0; Q8CFV5; Q9CVS6;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Tubulin polyglutamylase TTLL5 {ECO:0000303|PubMed:17499049};
DE EC=6.3.2.- {ECO:0000269|PubMed:17499049};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 5;
GN Name=Ttll5 {ECO:0000312|MGI:MGI:2443657}; Synonyms=Kiaa0998;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 463-1328 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Tongue;
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).
CC -!- FUNCTION: Polyglutamylase which modifies tubulin, generating
CC polyglutamate side chains on the gamma-carboxyl group of specific
CC glutamate residues within the C-terminal tail of tubulin
CC (PubMed:17499049). Preferentially mediates ATP-dependent initiation
CC step of the polyglutamylation reaction over the elongation step
CC (PubMed:17499049). Preferentially modifies the alpha-tubulin tail over
CC a beta-tail (PubMed:17499049). Required for CCSAP localization to both
CC polyglutamylated spindle and cilia microtubules (By similarity).
CC Increases the effects of transcriptional coactivator NCOA2/TIF2 in
CC glucocorticoid receptor-mediated repression and induction and in
CC androgen receptor-mediated induction (By similarity).
CC {ECO:0000250|UniProtKB:Q6EMB2, ECO:0000269|PubMed:17499049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17499049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000305|PubMed:17499049};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP +
CC L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein]
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519,
CC Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17499049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC Evidence={ECO:0000305|PubMed:17499049};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBUNIT: Interacts with the transcriptional coactivators NCOA1/SRC-1
CC and NCOA2/TIF2. {ECO:0000250|UniProtKB:Q6EMB2}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:17499049}. Nucleus
CC {ECO:0000250|UniProtKB:Q6EMB2}. Cytoplasm {ECO:0000250,
CC ECO:0000250|UniProtKB:Q6EMB2}. Note=In osteosarcoma cells, found in
CC both cytoplasm and nucleus in the absence of steroid but located
CC exclusively in the nucleus in the presence of steroid (By similarity).
CC Localized to the base of the connecting cilium between the basal body
CC and the adjacent daughter centriole of the cilium.
CC {ECO:0000250|UniProtKB:Q6EMB2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CHB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CHB8-2; Sequence=VSP_041931;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, kidney, liver, spleen
CC and testis (PubMed:17499049). Expressed in heart, lung, muscle and
CC trachea (PubMed:17499049). {ECO:0000269|PubMed:17499049}.
CC -!- DOMAIN: The flexible c-MTBD (cationic microtubule binding domain)
CC region mediates binding to microtubules. It is positively charged and
CC becomes ordered when bound to microtubules: it interacts with a
CC negatively charged patch on tubulin. The presence of positive charges
CC in the c-MTBD region is essential for proper binding.
CC {ECO:0000250|UniProtKB:Q6EMB2, ECO:0000250|UniProtKB:Q6ZT98}.
CC -!- DOMAIN: Arg-186 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 -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35276.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC41462.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE43213.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AM690748; CAM84325.1; -; mRNA.
DR EMBL; AB093278; BAC41462.1; ALT_INIT; mRNA.
DR EMBL; BC035276; AAH35276.1; ALT_INIT; mRNA.
DR EMBL; AK006726; BAB24715.1; -; mRNA.
DR EMBL; AK009255; BAE43213.1; ALT_FRAME; mRNA.
DR EMBL; AK028083; BAC25741.1; -; mRNA.
DR CCDS; CCDS36499.2; -. [Q8CHB8-1]
DR RefSeq; NP_001074892.2; NM_001081423.2. [Q8CHB8-1]
DR RefSeq; NP_001334324.1; NM_001347395.1.
DR RefSeq; XP_017170604.1; XM_017315115.1.
DR AlphaFoldDB; Q8CHB8; -.
DR SMR; Q8CHB8; -.
DR STRING; 10090.ENSMUSP00000048809; -.
DR iPTMnet; Q8CHB8; -.
DR PhosphoSitePlus; Q8CHB8; -.
DR EPD; Q8CHB8; -.
DR MaxQB; Q8CHB8; -.
DR PaxDb; Q8CHB8; -.
DR PRIDE; Q8CHB8; -.
DR ProteomicsDB; 297753; -. [Q8CHB8-1]
DR ProteomicsDB; 297754; -. [Q8CHB8-2]
DR DNASU; 320244; -.
DR Ensembl; ENSMUST00000040179; ENSMUSP00000048809; ENSMUSG00000012609. [Q8CHB8-1]
DR Ensembl; ENSMUST00000155448; ENSMUSP00000134971; ENSMUSG00000012609. [Q8CHB8-2]
DR GeneID; 320244; -.
DR KEGG; mmu:320244; -.
DR UCSC; uc007ohj.2; mouse. [Q8CHB8-1]
DR CTD; 23093; -.
DR MGI; MGI:2443657; Ttll5.
DR VEuPathDB; HostDB:ENSMUSG00000012609; -.
DR eggNOG; KOG2156; Eukaryota.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000162910; -.
DR InParanoid; Q8CHB8; -.
DR OMA; TRLFQDX; -.
DR OrthoDB; 219807at2759; -.
DR PhylomeDB; Q8CHB8; -.
DR TreeFam; TF313087; -.
DR BRENDA; 6.3.2.B3; 3474.
DR Reactome; R-MMU-8955332; Carboxyterminal post-translational modifications of tubulin.
DR BioGRID-ORCS; 320244; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Ttll5; mouse.
DR PRO; PR:Q8CHB8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8CHB8; protein.
DR Bgee; ENSMUSG00000012609; Expressed in spermatocyte and 204 other tissues.
DR ExpressionAtlas; Q8CHB8; baseline and differential.
DR Genevisible; Q8CHB8; MM.
DR GO; GO:0097731; C:9+0 non-motile cilium; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IDA:UniProtKB.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0018095; P:protein polyglutamylation; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:MGI.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Ligase; Magnesium; Metal-binding; Microtubule;
KW Nucleotide-binding; Nucleus; Reference proteome; Transcription.
FT CHAIN 1..1328
FT /note="Tubulin polyglutamylase TTLL5"
FT /id="PRO_0000223342"
FT DOMAIN 62..407
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..271
FT /note="L-glutamate"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT REGION 378..488
FT /note="c-MTBD region"
FT /evidence="ECO:0000250|UniProtKB:Q6EMB2"
FT REGION 411..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..617
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 186..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 186
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 208..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 221..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 247
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 268..269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 293
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 384
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 186
FT /note="Essential for specifying initiation versus
FT elongation step of the polyglutamylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT VAR_SEQ 564..1328
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041931"
FT CONFLICT 663..664
FT /note="IE -> NQ (in Ref. 4; BAE43213)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="A -> G (in Ref. 2; BAC41462)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="I -> M (in Ref. 4; BAE43213)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="E -> D (in Ref. 4; BAE43213)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222
FT /note="K -> N (in Ref. 4; BAE43213)"
FT /evidence="ECO:0000305"
FT CONFLICT 1252
FT /note="R -> K (in Ref. 4; BAB24715)"
FT /evidence="ECO:0000305"
FT CONFLICT 1266
FT /note="E -> K (in Ref. 4; BAB24715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1328 AA; 147715 MW; AA8D8E25F21C55C5 CRC64;
MPVVMARDLE ETASSSEDED LANQEDHPCI MWTGGCRRIP VLVFHAEAIL TKDNNIRVIG
ERYHLSYKIV RTDSRLVRSI LTAHGFHEVH PSSTDYNLMW TGSHLKPFLL RTLSEAQKVN
HFPRSYELTR KDRLYKNIIR MQHTHGFKAF HILPQTFLLP AEYAEFCNSY SKDRGPWIVK
PVASSRGRGV YLINNPNQIS LEENILVSRY INNPLLIDDF KFDVRLYVLV TSYDPLVIYL
YEEGLARFAT VRYDQGSKNI RNQFMHLTNY SVNKKSGDYV SCDDPEVEDY GNKWSMSAML
RYLKQEGKDT TALMAHVEDL IIKTIISAEL AIATACKTFV PHRSSCFELY GFDVLIDNTL
KPWLLEVNLS PSLACDAPLD LKIKASMISD MFTVVGFVCQ DPAQRTSNRS IYPSFESSRR
NPFQKPQRTR PLSASDAEMK NLVASAREKV PGKLGGSVLG LSMEEIKVLR RVKEENDRRG
GFIRIFPTSE TWEIYGSYLE HKTSMNYMLA TRLFQDRGNP RRSLLTGRAR VSTEGAPELK
VESMNSKAKL HAALYERKLL SLEVRKRRRR SGRLRAMRPK YPVIAQPAEM NIKTETESEE
EEEVGLDNDD EEQEASQEES AGSLGENQAK YTPSLTVIVE NSPRDNAMKV AEWTNKGEPC
CKIEAQEPES KFNLMQILQD NGNLSKVQAR LAFSAYLQHV QIRLTKDSGG QTLSPSWAAK
EDEQMELVVR FLKRASSNLQ HSLRMVLPSR RLALLERRRI LAHQLGDFIG VYNKETEQMA
EKKSKKKLEE EEEDGVNAES FQEFIRQASE AELEEVLTFY TQKNKSASVF LGTHSKSSKN
SSSYSDSGAK GDHPETIQEV KIKQPKQQQA TEIHADKLSR FTTSSGKEAK LVYTNCSSFC
SPAAVLLQRL PSSHLSSVIT TSALSAGPGH HASLSQIPPA VPSLPHQPAL LLSPVPDNAP
PSIHSGTQNV SPAGLPRCRS GSYTIGPFSS FQSAAHIYSQ KLSRPSSAKA AGSCHPHKHH
SGIAKTQKEG EDVSLNRRYN QSLVTAELQR LAEKQAARQY SPASHISLLT QQVTNLNLAS
SVINRSSAST PPTLRPVISP SGPTWSIQPD LHASETHSSP PGSRSLQTGG FAWEGEVENN
AYSKTTGVVP QHKYHPTAGS YQLHFALQQL EQQKLQSRQL LDQSRARHQA IFGSQTLPNS
SLWTMNNGPG CRISSATTGG QKPNTLPQKV VAPPNSSTLV SKPASNHKQV LRKPASQRAS
KGSSAEGQLN GLQSSLNPAA FMPITNSTGS LEAPQVIFAR SKPLPTQSGA LATVIGQRKS
KSVKSGTI
