TTLL6_HUMAN
ID TTLL6_HUMAN Reviewed; 843 AA.
AC Q8N841; B4DZJ5; C9J233; Q24KB1; Q24KB2; Q24KB6; Q24KF3; Q24KJ5; Q24KN7;
AC Q24KS9; Q24KX1; Q24L13; Q24L55; Q24L76; Q8IYW6; Q8NA62;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tubulin polyglutamylase TTLL6 {ECO:0000303|PubMed:15890843};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:A4Q9E8};
DE AltName: Full=Protein polyglutamylase TTLL6 {ECO:0000250|UniProtKB:A4Q9E8};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 6;
GN Name=TTLL6 {ECO:0000312|HGNC:HGNC:26664};
GN Synonyms=TTL.6 {ECO:0000303|PubMed:16443334};
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 [GENOMIC DNA / MRNA] (ISOFORM 2), AND VARIANT ASP-664.
RX PubMed=16443334; DOI=10.1016/j.gene.2005.11.014;
RA Chen X.-H., Shi H., Liu X.-L., Su B.;
RT "The testis-specific apoptosis related gene TTL.6 underwent adaptive
RT evolution in the lineage leading to humans.";
RL Gene 370:58-63(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-664.
RC TISSUE=Testis {ECO:0000312|EMBL:BAC04066.1};
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 GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis {ECO:0000312|EMBL:AAH33563.1};
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 IDENTIFICATION.
RX PubMed=15890843; DOI=10.1126/science.1113010;
RA Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S.,
RA Gaertig J., Edde B.;
RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT family.";
RL Science 308:1758-1762(2005).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CEP41.
RX PubMed=22246503; DOI=10.1038/ng.1078;
RA Lee J.E., Silhavy J.L., Zaki M.S., Schroth J., Bielas S.L., Marsh S.E.,
RA Olvera J., Brancati F., Iannicelli M., Ikegami K., Schlossman A.M.,
RA Merriman B., Attie-Bitach T., Logan C.V., Glass I.A., Cluckey A.,
RA Louie C.M., Lee J.H., Raynes H.R., Rapin I., Castroviejo I.P., Setou M.,
RA Barbot C., Boltshauser E., Nelson S.F., Hildebrandt F., Johnson C.A.,
RA Doherty D.A., Valente E.M., Gleeson J.G.;
RT "CEP41 is mutated in Joubert syndrome and is required for tubulin
RT glutamylation at the cilium.";
RL Nat. Genet. 44:193-199(2012).
RN [7]
RP DOMAIN, AND MUTAGENESIS OF 396-LYS--LYS-398; ARG-416 AND ARG-419.
RX PubMed=25959773; DOI=10.1016/j.cell.2015.04.003;
RA Garnham C.P., Vemu A., Wilson-Kubalek E.M., Yu I., Szyk A., Lander G.C.,
RA Milligan R.A., Roll-Mecak A.;
RT "Multivalent microtubule recognition by tubulin tyrosine ligase-like family
RT glutamylases.";
RL Cell 161:1112-1123(2015).
CC -!- FUNCTION: Polyglutamylase which modifies both tubulin and non-tubulin
CC proteins, generating alpha-linked polyglutamate side chains on the
CC gamma-carboxyl group of specific glutamate residues of target proteins.
CC Preferentially mediates ATP-dependent long polyglutamate chain
CC elongation over the initiation step of the polyglutamylation reaction.
CC Preferentially modifies the alpha-tubulin tail over a beta-tail.
CC Promotes tubulin polyglutamylation which stimulates spastin/SPAST-
CC mediated microtubule severing, thereby regulating microtubule
CC functions. Mediates microtubule polyglutamylation in primary cilia
CC axoneme, which is important for ciliary structural formation and
CC motility. Mediates microtubule polyglutamylation in motile cilia,
CC necessary for the regulation of ciliary coordinated beating.
CC Polyglutamylates non-tubulin protein nucleotidyltransferase CGAS,
CC leading to CGAS DNA-binding inhibition, thereby preventing antiviral
CC defense response. {ECO:0000250|UniProtKB:A4Q9E8}.
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:0000250|UniProtKB:A4Q9E8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
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:0000250|UniProtKB:A4Q9E8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBUNIT: Found in a complex with CEP41. {ECO:0000269|PubMed:22246503}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A4Q9E8}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A4Q9E8}. Cytoplasm,
CC cytoskeleton, cilium axoneme {ECO:0000269|PubMed:22246503}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:22246503}.
CC Note=CEP41 is required for its transport between the basal body and the
CC cilium axoneme. {ECO:0000269|PubMed:22246503}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:14702039};
CC IsoId=Q8N841-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16443334};
CC IsoId=Q8N841-2; Sequence=VSP_052727, VSP_052728;
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:Q6ZT98, ECO:0000269|PubMed:25959773}.
CC -!- DOMAIN: Gln-181 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 -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04066.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY898275; AAY28091.1; -; Genomic_DNA.
DR EMBL; AY898276; AAY28092.1; -; Genomic_DNA.
DR EMBL; AY898277; AAY28093.1; -; Genomic_DNA.
DR EMBL; AY898278; AAY28094.1; -; Genomic_DNA.
DR EMBL; AY898279; AAY28095.1; -; Genomic_DNA.
DR EMBL; AY898280; AAY28096.1; -; Genomic_DNA.
DR EMBL; AY898281; AAY28097.1; -; Genomic_DNA.
DR EMBL; AY898282; AAY28098.1; -; Genomic_DNA.
DR EMBL; AY898283; AAY28099.1; -; Genomic_DNA.
DR EMBL; AY898284; AAY28100.1; -; Genomic_DNA.
DR EMBL; AY898285; AAY28101.1; -; Genomic_DNA.
DR EMBL; AY898286; AAY28102.1; -; Genomic_DNA.
DR EMBL; AY898287; AAY28103.1; -; Genomic_DNA.
DR EMBL; AY898288; AAY28104.1; -; Genomic_DNA.
DR EMBL; AY898289; AAY28105.1; -; Genomic_DNA.
DR EMBL; AY898290; AAY28106.1; -; Genomic_DNA.
DR EMBL; AY898291; AAY28107.1; -; Genomic_DNA.
DR EMBL; AY898292; AAY28108.1; -; Genomic_DNA.
DR EMBL; AY898293; AAY28109.1; -; Genomic_DNA.
DR EMBL; AY898294; AAY28110.1; -; Genomic_DNA.
DR EMBL; AY898295; AAY28111.1; -; Genomic_DNA.
DR EMBL; AY898296; AAY28112.1; -; Genomic_DNA.
DR EMBL; AY898297; AAY28113.1; -; Genomic_DNA.
DR EMBL; AY898298; AAY28114.1; -; Genomic_DNA.
DR EMBL; AY898299; AAY28115.1; -; Genomic_DNA.
DR EMBL; AY898300; AAY28116.1; -; Genomic_DNA.
DR EMBL; AY898301; AAY28117.1; -; Genomic_DNA.
DR EMBL; AY898302; AAY28118.1; -; Genomic_DNA.
DR EMBL; AY898303; AAY28119.1; -; Genomic_DNA.
DR EMBL; AY898304; AAY28120.1; -; Genomic_DNA.
DR EMBL; AY898305; AAY28121.1; -; Genomic_DNA.
DR EMBL; AY898306; AAY28122.1; -; Genomic_DNA.
DR EMBL; AY898307; AAY28123.1; -; Genomic_DNA.
DR EMBL; AY898308; AAY28124.1; -; Genomic_DNA.
DR EMBL; AY898309; AAY28125.1; -; Genomic_DNA.
DR EMBL; AY898317; AAX86172.1; -; Genomic_DNA.
DR EMBL; AY898318; AAX86173.1; -; Genomic_DNA.
DR EMBL; AY898319; AAX86174.1; -; Genomic_DNA.
DR EMBL; AY898320; AAX86175.1; -; Genomic_DNA.
DR EMBL; AY898321; AAX86176.1; -; Genomic_DNA.
DR EMBL; AY898322; AAX86177.1; -; Genomic_DNA.
DR EMBL; AY898323; AAX86178.1; -; Genomic_DNA.
DR EMBL; AY898324; AAX86179.1; -; Genomic_DNA.
DR EMBL; AY898325; AAX86180.1; -; Genomic_DNA.
DR EMBL; AY898326; AAX86181.1; -; Genomic_DNA.
DR EMBL; AY898327; AAX86182.1; -; Genomic_DNA.
DR EMBL; AY898328; AAX86183.1; -; Genomic_DNA.
DR EMBL; AY898329; AAX86184.1; -; Genomic_DNA.
DR EMBL; AY898330; AAX86185.1; -; Genomic_DNA.
DR EMBL; AY898331; AAX86186.1; -; Genomic_DNA.
DR EMBL; AY898332; AAX86187.1; -; Genomic_DNA.
DR EMBL; AY898333; AAX86188.1; -; Genomic_DNA.
DR EMBL; AY898334; AAX86189.1; -; Genomic_DNA.
DR EMBL; AY898335; AAX86190.1; -; Genomic_DNA.
DR EMBL; AY898336; AAX86191.1; -; Genomic_DNA.
DR EMBL; AY898337; AAX86192.1; -; Genomic_DNA.
DR EMBL; AY898338; AAX86193.1; -; Genomic_DNA.
DR EMBL; AY898339; AAX86194.1; -; Genomic_DNA.
DR EMBL; AY898340; AAX86195.1; -; Genomic_DNA.
DR EMBL; AY898341; AAX86196.1; -; Genomic_DNA.
DR EMBL; AY898342; AAX86197.1; -; Genomic_DNA.
DR EMBL; AY898343; AAX86198.1; -; Genomic_DNA.
DR EMBL; AY898344; AAX86199.1; -; Genomic_DNA.
DR EMBL; AY898345; AAX86200.1; -; Genomic_DNA.
DR EMBL; AY898346; AAX86201.1; -; Genomic_DNA.
DR EMBL; AY898347; AAX86202.1; -; Genomic_DNA.
DR EMBL; AY898348; AAX86203.1; -; Genomic_DNA.
DR EMBL; AY898349; AAX86204.1; -; Genomic_DNA.
DR EMBL; AY898350; AAX86205.1; -; Genomic_DNA.
DR EMBL; AY898351; AAX86206.1; -; Genomic_DNA.
DR EMBL; AY898359; AAX86214.1; -; Genomic_DNA.
DR EMBL; AY898360; AAX86215.1; -; Genomic_DNA.
DR EMBL; AY898361; AAX86216.1; -; Genomic_DNA.
DR EMBL; AY898362; AAX86217.1; -; Genomic_DNA.
DR EMBL; AY898363; AAX86218.1; -; Genomic_DNA.
DR EMBL; AY898364; AAX86219.1; -; Genomic_DNA.
DR EMBL; AY898365; AAX86220.1; -; Genomic_DNA.
DR EMBL; AY898366; AAX86221.1; -; Genomic_DNA.
DR EMBL; AY898367; AAX86222.1; -; Genomic_DNA.
DR EMBL; AY898368; AAX86223.1; -; Genomic_DNA.
DR EMBL; AY898369; AAX86224.1; -; Genomic_DNA.
DR EMBL; AY898370; AAX86225.1; -; Genomic_DNA.
DR EMBL; AY898371; AAX86226.1; -; Genomic_DNA.
DR EMBL; AY898372; AAX86227.1; -; Genomic_DNA.
DR EMBL; AY898373; AAX86228.1; -; Genomic_DNA.
DR EMBL; AY898374; AAX86229.1; -; Genomic_DNA.
DR EMBL; AY898375; AAX86230.1; -; Genomic_DNA.
DR EMBL; AY898376; AAX86231.1; -; Genomic_DNA.
DR EMBL; AY898377; AAX86232.1; -; Genomic_DNA.
DR EMBL; AY898378; AAX86233.1; -; Genomic_DNA.
DR EMBL; AY898379; AAX86234.1; -; Genomic_DNA.
DR EMBL; AY898380; AAX86235.1; -; Genomic_DNA.
DR EMBL; AY898381; AAX86236.1; -; Genomic_DNA.
DR EMBL; AY898382; AAX86237.1; -; Genomic_DNA.
DR EMBL; AY898383; AAX86238.1; -; Genomic_DNA.
DR EMBL; AY898384; AAX86239.1; -; Genomic_DNA.
DR EMBL; AY898385; AAX86240.1; -; Genomic_DNA.
DR EMBL; AY898386; AAX86241.1; -; Genomic_DNA.
DR EMBL; AY898387; AAX86242.1; -; Genomic_DNA.
DR EMBL; AY898388; AAX86243.1; -; Genomic_DNA.
DR EMBL; AY898389; AAX86244.1; -; Genomic_DNA.
DR EMBL; AY898390; AAX86245.1; -; Genomic_DNA.
DR EMBL; AY898391; AAX86246.1; -; Genomic_DNA.
DR EMBL; AY898392; AAX86247.1; -; Genomic_DNA.
DR EMBL; AY898393; AAX86248.1; -; Genomic_DNA.
DR EMBL; AY898401; AAX86256.1; -; Genomic_DNA.
DR EMBL; AY898402; AAX86257.1; -; Genomic_DNA.
DR EMBL; AY898403; AAX86258.1; -; Genomic_DNA.
DR EMBL; AY898404; AAX86259.1; -; Genomic_DNA.
DR EMBL; AY898405; AAX86260.1; -; Genomic_DNA.
DR EMBL; AY898406; AAX86261.1; -; Genomic_DNA.
DR EMBL; AY898407; AAX86262.1; -; Genomic_DNA.
DR EMBL; AY898408; AAX86263.1; -; Genomic_DNA.
DR EMBL; AY898409; AAX86264.1; -; Genomic_DNA.
DR EMBL; AY898410; AAX86265.1; -; Genomic_DNA.
DR EMBL; AY898411; AAX86266.1; -; Genomic_DNA.
DR EMBL; AY898412; AAX86267.1; -; Genomic_DNA.
DR EMBL; AY898413; AAX86268.1; -; Genomic_DNA.
DR EMBL; AY898414; AAX86269.1; -; Genomic_DNA.
DR EMBL; AY898415; AAX86270.1; -; Genomic_DNA.
DR EMBL; AY898416; AAX86271.1; -; Genomic_DNA.
DR EMBL; AY898417; AAX86272.1; -; Genomic_DNA.
DR EMBL; AY898418; AAX86273.1; -; Genomic_DNA.
DR EMBL; AY898419; AAX86274.1; -; Genomic_DNA.
DR EMBL; AY898420; AAX86275.1; -; Genomic_DNA.
DR EMBL; AY898421; AAX86276.1; -; Genomic_DNA.
DR EMBL; AY898422; AAX86277.1; -; Genomic_DNA.
DR EMBL; AY898423; AAX86278.1; -; Genomic_DNA.
DR EMBL; AY898424; AAX86279.1; -; Genomic_DNA.
DR EMBL; AY898425; AAX86280.1; -; Genomic_DNA.
DR EMBL; AY898426; AAX86281.1; -; Genomic_DNA.
DR EMBL; AY898427; AAX86282.1; -; Genomic_DNA.
DR EMBL; AY898428; AAX86283.1; -; Genomic_DNA.
DR EMBL; AY898429; AAX86284.1; -; Genomic_DNA.
DR EMBL; AY898430; AAX86285.1; -; Genomic_DNA.
DR EMBL; AY898431; AAX86286.1; -; Genomic_DNA.
DR EMBL; AY898432; AAX86287.1; -; Genomic_DNA.
DR EMBL; AY898433; AAX86288.1; -; Genomic_DNA.
DR EMBL; AY898434; AAX86289.1; -; Genomic_DNA.
DR EMBL; AY898435; AAX86290.1; -; Genomic_DNA.
DR EMBL; AY898443; AAX86298.1; -; Genomic_DNA.
DR EMBL; AY898444; AAX86299.1; -; Genomic_DNA.
DR EMBL; AY898445; AAX86300.1; -; Genomic_DNA.
DR EMBL; AY898446; AAX86301.1; -; Genomic_DNA.
DR EMBL; AY898447; AAX86302.1; -; Genomic_DNA.
DR EMBL; AY898448; AAX86303.1; -; Genomic_DNA.
DR EMBL; AY898449; AAX86304.1; -; Genomic_DNA.
DR EMBL; AY898450; AAX86305.1; -; Genomic_DNA.
DR EMBL; AY898451; AAX86306.1; -; Genomic_DNA.
DR EMBL; AY898452; AAX86307.1; -; Genomic_DNA.
DR EMBL; AY898453; AAX86308.1; -; Genomic_DNA.
DR EMBL; AY898454; AAX86309.1; -; Genomic_DNA.
DR EMBL; AY898455; AAX86310.1; -; Genomic_DNA.
DR EMBL; AY898456; AAX86311.1; -; Genomic_DNA.
DR EMBL; AY898457; AAX86312.1; -; Genomic_DNA.
DR EMBL; AY898458; AAX86313.1; -; Genomic_DNA.
DR EMBL; AY898459; AAX86314.1; -; Genomic_DNA.
DR EMBL; AY898460; AAX86315.1; -; Genomic_DNA.
DR EMBL; AY898461; AAX86316.1; -; Genomic_DNA.
DR EMBL; AY898462; AAX86317.1; -; Genomic_DNA.
DR EMBL; AY898463; AAX86318.1; -; Genomic_DNA.
DR EMBL; AY898464; AAX86319.1; -; Genomic_DNA.
DR EMBL; AY898465; AAX86320.1; -; Genomic_DNA.
DR EMBL; AY898466; AAX86321.1; -; Genomic_DNA.
DR EMBL; AY898467; AAX86322.1; -; Genomic_DNA.
DR EMBL; AY898468; AAX86323.1; -; Genomic_DNA.
DR EMBL; AY898469; AAX86324.1; -; Genomic_DNA.
DR EMBL; AY898470; AAX86325.1; -; Genomic_DNA.
DR EMBL; AY898471; AAX86326.1; -; Genomic_DNA.
DR EMBL; AY898472; AAX86327.1; -; Genomic_DNA.
DR EMBL; AY898473; AAX86328.1; -; Genomic_DNA.
DR EMBL; AY898474; AAX86329.1; -; Genomic_DNA.
DR EMBL; AY898475; AAX86330.1; -; Genomic_DNA.
DR EMBL; AY898476; AAX86331.1; -; Genomic_DNA.
DR EMBL; AY898477; AAX86332.1; -; Genomic_DNA.
DR EMBL; AY898485; AAX86340.1; -; Genomic_DNA.
DR EMBL; AY898486; AAX86341.1; -; Genomic_DNA.
DR EMBL; AY898487; AAX86342.1; -; Genomic_DNA.
DR EMBL; AY898488; AAX86343.1; -; Genomic_DNA.
DR EMBL; AY898489; AAX86344.1; -; Genomic_DNA.
DR EMBL; AY898490; AAX86345.1; -; Genomic_DNA.
DR EMBL; AY898491; AAX86346.1; -; Genomic_DNA.
DR EMBL; AY898492; AAX86347.1; -; Genomic_DNA.
DR EMBL; AY898493; AAX86348.1; -; Genomic_DNA.
DR EMBL; AY898494; AAX86349.1; -; Genomic_DNA.
DR EMBL; AY898495; AAX86350.1; -; Genomic_DNA.
DR EMBL; AY898496; AAX86351.1; -; Genomic_DNA.
DR EMBL; AY898497; AAX86352.1; -; Genomic_DNA.
DR EMBL; AY898498; AAX86353.1; -; Genomic_DNA.
DR EMBL; AY898499; AAX86354.1; -; Genomic_DNA.
DR EMBL; AY898500; AAX86355.1; -; Genomic_DNA.
DR EMBL; AY898501; AAX86356.1; -; Genomic_DNA.
DR EMBL; AY898502; AAX86357.1; -; Genomic_DNA.
DR EMBL; AY898503; AAX86358.1; -; Genomic_DNA.
DR EMBL; AY898504; AAX86359.1; -; Genomic_DNA.
DR EMBL; AY898505; AAX86360.1; -; Genomic_DNA.
DR EMBL; AY898506; AAX86361.1; -; Genomic_DNA.
DR EMBL; AY898507; AAX86362.1; -; Genomic_DNA.
DR EMBL; AY898508; AAX86363.1; -; Genomic_DNA.
DR EMBL; AY898509; AAX86364.1; -; Genomic_DNA.
DR EMBL; AY898510; AAX86365.1; -; Genomic_DNA.
DR EMBL; AY898511; AAX86366.1; -; Genomic_DNA.
DR EMBL; AY898512; AAX86367.1; -; Genomic_DNA.
DR EMBL; AY898513; AAX86368.1; -; Genomic_DNA.
DR EMBL; AY898514; AAX86369.1; -; Genomic_DNA.
DR EMBL; AY898515; AAX86370.1; -; Genomic_DNA.
DR EMBL; AY898516; AAX86371.1; -; Genomic_DNA.
DR EMBL; AY898517; AAX86372.1; -; Genomic_DNA.
DR EMBL; AY898518; AAX86373.1; -; Genomic_DNA.
DR EMBL; AY898519; AAX86374.1; -; Genomic_DNA.
DR EMBL; AY898527; AAX86382.1; -; Genomic_DNA.
DR EMBL; AY898528; AAX86383.1; -; Genomic_DNA.
DR EMBL; AY898529; AAX86384.1; -; Genomic_DNA.
DR EMBL; AY898530; AAX86385.1; -; Genomic_DNA.
DR EMBL; AY898531; AAX86386.1; -; Genomic_DNA.
DR EMBL; AY898532; AAX86387.1; -; Genomic_DNA.
DR EMBL; AY898533; AAX86388.1; -; Genomic_DNA.
DR EMBL; AY898534; AAX86389.1; -; Genomic_DNA.
DR EMBL; AY898535; AAX86390.1; -; Genomic_DNA.
DR EMBL; AY898536; AAX86391.1; -; Genomic_DNA.
DR EMBL; AY898537; AAX86392.1; -; Genomic_DNA.
DR EMBL; AY898538; AAX86393.1; -; Genomic_DNA.
DR EMBL; AY898539; AAX86394.1; -; Genomic_DNA.
DR EMBL; AY898540; AAX86395.1; -; Genomic_DNA.
DR EMBL; AY898541; AAX86396.1; -; Genomic_DNA.
DR EMBL; AY898542; AAX86397.1; -; Genomic_DNA.
DR EMBL; AY898543; AAX86398.1; -; Genomic_DNA.
DR EMBL; AY898544; AAX86399.1; -; Genomic_DNA.
DR EMBL; AY898545; AAX86400.1; -; Genomic_DNA.
DR EMBL; AY898546; AAX86401.1; -; Genomic_DNA.
DR EMBL; AY898547; AAX86402.1; -; Genomic_DNA.
DR EMBL; AY898548; AAX86403.1; -; Genomic_DNA.
DR EMBL; AY898549; AAX86404.1; -; Genomic_DNA.
DR EMBL; AY898550; AAX86405.1; -; Genomic_DNA.
DR EMBL; AY898551; AAX86406.1; -; Genomic_DNA.
DR EMBL; AY898552; AAX86407.1; -; Genomic_DNA.
DR EMBL; AY898553; AAX86408.1; -; Genomic_DNA.
DR EMBL; AY898554; AAX86409.1; -; Genomic_DNA.
DR EMBL; AY898555; AAX86410.1; -; Genomic_DNA.
DR EMBL; AY898556; AAX86411.1; -; Genomic_DNA.
DR EMBL; AY898557; AAX86412.1; -; Genomic_DNA.
DR EMBL; AY898558; AAX86413.1; -; Genomic_DNA.
DR EMBL; AY898559; AAX86414.1; -; Genomic_DNA.
DR EMBL; AY898560; AAX86415.1; -; Genomic_DNA.
DR EMBL; AY898561; AAX86416.1; -; Genomic_DNA.
DR EMBL; AY898569; AAX86424.1; -; Genomic_DNA.
DR EMBL; AY898570; AAX86425.1; -; Genomic_DNA.
DR EMBL; AY898571; AAX86426.1; -; Genomic_DNA.
DR EMBL; AY898572; AAX86427.1; -; Genomic_DNA.
DR EMBL; AY898573; AAX86428.1; -; Genomic_DNA.
DR EMBL; AY898574; AAX86429.1; -; Genomic_DNA.
DR EMBL; AY898575; AAX86430.1; -; Genomic_DNA.
DR EMBL; AY898576; AAX86431.1; -; Genomic_DNA.
DR EMBL; AY898577; AAX86432.1; -; Genomic_DNA.
DR EMBL; AY898578; AAX86433.1; -; Genomic_DNA.
DR EMBL; AY898579; AAX86434.1; -; Genomic_DNA.
DR EMBL; AY898580; AAX86435.1; -; Genomic_DNA.
DR EMBL; AY898581; AAX86436.1; -; Genomic_DNA.
DR EMBL; AY898582; AAX86437.1; -; Genomic_DNA.
DR EMBL; AY898583; AAX86438.1; -; Genomic_DNA.
DR EMBL; AY898584; AAX86439.1; -; Genomic_DNA.
DR EMBL; AY898585; AAX86440.1; -; Genomic_DNA.
DR EMBL; AY898586; AAX86441.1; -; Genomic_DNA.
DR EMBL; AY898587; AAX86442.1; -; Genomic_DNA.
DR EMBL; AY898588; AAX86443.1; -; Genomic_DNA.
DR EMBL; AY898589; AAX86444.1; -; Genomic_DNA.
DR EMBL; AY898590; AAX86445.1; -; Genomic_DNA.
DR EMBL; AY898591; AAX86446.1; -; Genomic_DNA.
DR EMBL; AY898592; AAX86447.1; -; Genomic_DNA.
DR EMBL; AY898593; AAX86448.1; -; Genomic_DNA.
DR EMBL; AY898594; AAX86449.1; -; Genomic_DNA.
DR EMBL; AY898595; AAX86450.1; -; Genomic_DNA.
DR EMBL; AY898596; AAX86451.1; -; Genomic_DNA.
DR EMBL; AY898597; AAX86452.1; -; Genomic_DNA.
DR EMBL; AY898598; AAX86453.1; -; Genomic_DNA.
DR EMBL; AY898599; AAX86454.1; -; Genomic_DNA.
DR EMBL; AY898600; AAX86455.1; -; Genomic_DNA.
DR EMBL; AY898601; AAX86456.1; -; Genomic_DNA.
DR EMBL; AY898602; AAX86457.1; -; Genomic_DNA.
DR EMBL; AY898603; AAX86458.1; -; Genomic_DNA.
DR EMBL; AK093127; BAC04066.1; ALT_INIT; mRNA.
DR EMBL; AK302952; BAG64107.1; -; mRNA.
DR EMBL; AC068531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033563; AAH33563.1; -; mRNA.
DR RefSeq; NP_001124390.1; NM_001130918.1.
DR RefSeq; NP_775894.2; NM_173623.3.
DR AlphaFoldDB; Q8N841; -.
DR SMR; Q8N841; -.
DR BioGRID; 129751; 12.
DR IntAct; Q8N841; 3.
DR MINT; Q8N841; -.
DR STRING; 9606.ENSP00000377043; -.
DR iPTMnet; Q8N841; -.
DR PhosphoSitePlus; Q8N841; -.
DR BioMuta; TTLL6; -.
DR DMDM; 172045779; -.
DR EPD; Q8N841; -.
DR MassIVE; Q8N841; -.
DR PaxDb; Q8N841; -.
DR PeptideAtlas; Q8N841; -.
DR PRIDE; Q8N841; -.
DR ProteomicsDB; 72370; -. [Q8N841-1]
DR ProteomicsDB; 72371; -. [Q8N841-2]
DR Antibodypedia; 17865; 44 antibodies from 12 providers.
DR DNASU; 284076; -.
DR Ensembl; ENST00000393382.8; ENSP00000377043.3; ENSG00000170703.16.
DR Ensembl; ENST00000433608.6; ENSP00000399211.2; ENSG00000170703.16.
DR GeneID; 284076; -.
DR KEGG; hsa:284076; -.
DR UCSC; uc002iob.4; human. [Q8N841-1]
DR CTD; 284076; -.
DR DisGeNET; 284076; -.
DR GeneCards; TTLL6; -.
DR HGNC; HGNC:26664; TTLL6.
DR HPA; ENSG00000170703; Tissue enriched (testis).
DR MIM; 610849; gene.
DR neXtProt; NX_Q8N841; -.
DR PharmGKB; PA143485662; -.
DR VEuPathDB; HostDB:ENSG00000170703; -.
DR eggNOG; KOG2158; Eukaryota.
DR HOGENOM; CLU_036158_0_0_1; -.
DR InParanoid; Q8N841; -.
DR OrthoDB; 1251554at2759; -.
DR PhylomeDB; Q8N841; -.
DR TreeFam; TF313087; -.
DR PathwayCommons; Q8N841; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; Q8N841; -.
DR BioGRID-ORCS; 284076; 19 hits in 1061 CRISPR screens.
DR ChiTaRS; TTLL6; human.
DR GenomeRNAi; 284076; -.
DR Pharos; Q8N841; Tdark.
DR PRO; PR:Q8N841; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N841; protein.
DR Bgee; ENSG00000170703; Expressed in sperm and 120 other tissues.
DR ExpressionAtlas; Q8N841; baseline and differential.
DR Genevisible; Q8N841; HS.
DR GO; GO:0097731; C:9+0 non-motile cilium; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070739; F:protein-glutamic acid ligase activity; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051013; P:microtubule severing; IEA:Ensembl.
DR GO; GO:0003353; P:positive regulation of cilium movement; IEA:Ensembl.
DR GO; GO:0018095; P:protein polyglutamylation; ISS:UniProtKB.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; ISS:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027754; TTLL6.
DR PANTHER; PTHR12241:SF96; PTHR12241:SF96; 1.
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; Reference proteome.
FT CHAIN 1..843
FT /note="Tubulin polyglutamylase TTLL6"
FT /id="PRO_0000326160"
FT DOMAIN 58..401
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..267
FT /note="L-glutamate"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT REGION 372..451
FT /note="c-MTBD region"
FT /evidence="ECO:0000269|PubMed:25959773"
FT REGION 498..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 181..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 181
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 203..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 216..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 242
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 264..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 284
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 363
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 378
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 181
FT /note="Essential for specifying alpha-elongation versus
FT initiation step of the polyglutamylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 363
FT /note="Important for specifying alpha-elongation versus
FT initiation step of the polyglutamylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT VAR_SEQ 1..274
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16443334"
FT /id="VSP_052727"
FT VAR_SEQ 275..284
FT /note="FSRDAHSGSK -> MEGCLGVAEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16443334"
FT /id="VSP_052728"
FT VARIANT 664
FT /note="E -> D (in dbSNP:rs2032844)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16443334"
FT /id="VAR_039993"
FT MUTAGEN 396..398
FT /note="KKK->EEE: Decreased binding to microtubules and
FT polyglutamylase activity; when associated with E-416 and E-
FT 419."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 416
FT /note="R->E: Decreased binding to microtubules and
FT polyglutamylase activity; when associated with 396-E--E-398
FT and E-419."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 419
FT /note="R->E: Decreased binding to microtubules and
FT polyglutamylase activity; when associated with 396-E--E-398
FT and E-416."
FT /evidence="ECO:0000269|PubMed:25959773"
FT VARIANT Q8N841-2:9
FT /note="E -> V (in dbSNP:rs17853181)"
FT /evidence="ECO:0000269|PubMed:16443334"
FT /id="VAR_082930"
SQ SEQUENCE 843 AA; 96401 MW; D1C24002A551D54D CRC64;
MPQCPTLESQ EGENSEEKGD SSKEDPKETV ALAFVRENPG AQNGLQNAQQ QGKKKRKKKR
LVINLSSCRY ESVRRAAQQY GFREGGEDDD WTLYWTDYSV SLERVMEMKS YQKINHFPGM
SEICRKDLLA RNMSRMLKMF PKDFRFFPRT WCLPADWGDL QTYSRSRKNK TYICKPDSGC
QGKGIFITRT VKEIKPGEDM ICQLYISKPF IIDGFKFDLR IYVLVTSCDP LRIFVYNEGL
ARFATTSYSR PCTDNLDDIC MHLTNYSINK HSSNFSRDAH SGSKRKLSTF SAYLEDHSYN
VEQIWRDIED VIIKTLISAH PIIRHNYHTC FPNHTLNSAC FEILGFDILL DHKLKPWLLE
VNHSPSFSTD SRLDKEVKDG LLYDTLVLIN LESCDKKKVL EEERQRGQFL QQCCSREMRI
EEAKGFRAVQ LKKTETYEKE NCGGFRLIYP SLNSEKYEKF FQDNNSLFQN TVASRAREEY
ARQLIQELRL KREKKPFQMK KKVEMQGESA GEQVRKKGMR GWQQKQQQKD KAATQASKQY
IQPLTLVSYT PDLLLSVRGE RKNETDSSLN QEAPTEEASS VFPKLTSAKP FSSLPDLRNI
NLSSSKLEPS KPNFSIKEAK SASAVNVFTG TVHLTSVETT PESTTQLSIS PKSPPTLAVT
ASSEYSGPET DRVVSFKCKK QQTPPHLTQK KMLKSFLPTK SKSFWESPNT NWTLLKSDMN
KPHLISELLT KLQLSGKLSF FPAHYNPKLG MNNLSQNPSL PGECHSRSDS SGEKRQLDVS
SLLLQSPQSY NVTLRDLLVI ATPAQLDPRP CRSHASAMRD PCMQDQEAYS HCLISGQKGC
ERS
