TTLL7_MOUSE
ID TTLL7_MOUSE Reviewed; 912 AA.
AC A4Q9F0; A4Q9E9; Q8C417; Q9D5V3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Tubulin polyglutamylase TTLL7 {ECO:0000305|PubMed:17499049};
DE EC=6.3.2.- {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:19152315};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 7 {ECO:0000305|PubMed:16901895};
DE Short=mTTLL7 {ECO:0000303|PubMed:19152315};
GN Name=Ttll7 {ECO:0000312|MGI:MGI:1918142};
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] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:CAM84328.1};
RC TISSUE=Testis {ECO:0000312|EMBL:CAM84328.1};
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 636-912 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB29613.1};
RC TISSUE=Hippocampus {ECO:0000312|EMBL:BAC38821.1}, and
RC Testis {ECO:0000312|EMBL:BAB29613.1};
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF GLU-349.
RX PubMed=16901895; DOI=10.1074/jbc.m603984200;
RA Ikegami K., Mukai M., Tsuchida J., Heier R.L., Macgregor G.R., Setou M.;
RT "TTLL7 is a mammalian beta-tubulin polyglutamylase required for growth of
RT MAP2-positive neurites.";
RL J. Biol. Chem. 281:30707-30716(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19152315; DOI=10.1021/bi802047y;
RA Mukai M., Ikegami K., Sugiura Y., Takeshita K., Nakagawa A., Setou M.;
RT "Recombinant mammalian tubulin polyglutamylase TTLL7 performs both
RT initiation and elongation of polyglutamylation on beta-tubulin through a
RT random sequential pathway.";
RL Biochemistry 48:1084-1093(2009).
CC -!- FUNCTION: Polyglutamylase which modifies tubulin, generating
CC polyglutamate side chains of variable lengths on the gamma-carboxyl
CC group of specific glutamate residues within the C-terminal tail of
CC tubulin (PubMed:17499049, PubMed:16901895, PubMed:19152315). Mediates
CC both ATP-dependent initiation and elongation steps of the
CC polyglutamylation reaction (PubMed:17499049, PubMed:16901895,
CC PubMed:19152315). Preferentially modifies the beta-tubulin tail over an
CC alpha-tail (PubMed:17499049, PubMed:16901895, PubMed:19152315).
CC Competes with monoglycylase TTLL3 for modification site on beta-tubulin
CC substrate, thereby creating an anticorrelation between glycylation and
CC glutamylation reactions (By similarity). Required for neurite growth;
CC responsible for the strong increase in tubulin polyglutamylation during
CC postnatal neuronal maturation (PubMed:16901895).
CC {ECO:0000250|UniProtKB:F7E540, ECO:0000269|PubMed:16901895,
CC ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:19152315}.
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:16901895,
CC ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:19152315};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000305|PubMed:16901895, ECO:0000305|PubMed:17499049,
CC ECO:0000305|PubMed:19152315};
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:16901895,
CC ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:19152315};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC Evidence={ECO:0000305|PubMed:16901895, ECO:0000305|PubMed:17499049,
CC ECO:0000305|PubMed:19152315};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.2 uM for Glu (with 17 uM of tubulin for adult mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=19.1 uM for ATP (with 17 uM of tubulin for adult mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=19.6 uM for Glu (with 17 uM of tubulin for newborn mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=26.5 uM for ATP (with 17 uM of tubulin for newborn mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=5.4 uM for Glu (with 50 uM of ATP for adult mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=21.8 uM for tubulin (with 50 uM of ATP for adult mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=4.4 uM for Glu (with 50 uM of ATP for newborn mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=15.8 uM for tubulin (with 50 uM of ATP for newborn mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=7.5 uM for ATP (with 6 uM of Glu for adult mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=3.1 uM for tubulin (with 6 uM of Glu for adult mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=16 uM for ATP (with 6 uM of Glu for newborn mouse)
CC {ECO:0000269|PubMed:19152315};
CC KM=6.7 uM for tubulin (with 6 uM of Glu for newborn mouse)
CC {ECO:0000269|PubMed:19152315};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:19152315};
CC -!- SUBUNIT: Interacts with both alpha- and beta-tubulin (via C-terminal
CC tubulin tails). {ECO:0000250|UniProtKB:Q6ZT98}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:16901895,
CC ECO:0000269|PubMed:17499049}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Perikaryon
CC {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Note=In
CC cells with primary cilia, found in both cilia and basal bodies. In
CC neuronal cells, found in dendrites and perikaryon.
CC {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000303|PubMed:17499049};
CC IsoId=A4Q9F0-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:17499049}; Synonyms=TTLL7S
CC {ECO:0000303|PubMed:17499049};
CC IsoId=A4Q9F0-2; Sequence=VSP_052730, VSP_052731;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, testis and trachea
CC (PubMed:17499049). Expressed in brain, heart, kidney, liver, lung,
CC muscle and trachea (PubMed:17499049). In the brain, highly expressed in
CC hippocampus, thalamus, olfactory bulb and cerebellum cortex, corpus
CC callosum and striatum (PubMed:16901895, PubMed:17499049).
CC {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}.
CC -!- DOMAIN: The enzyme uses its core to engage the disordered anionic tails
CC of alpha- and beta-tubulin and the flexible c-MTBD (cationic
CC microtubule binding domain) region to bind the microtubule and position
CC itself for beta-tail modification. The c-MTBD region is positively
CC charged and becomes ordered when bound to microtubules: it interacts
CC with a negatively charged patch on alpha-tubulin. The presence of
CC positive charges in the c-MTBD region is essential for proper binding.
CC {ECO:0000250|UniProtKB:Q6ZT98}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000255}.
CC -!- CAUTION: Was initially though to be involved in the side-chain
CC initiation step of the polyglutamylation reaction rather than in the
CC elongation step (PubMed:17499049). However, it was later shown to be
CC involved in both steps (PubMed:19152315). {ECO:0000269|PubMed:17499049,
CC ECO:0000269|PubMed:19152315}.
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DR EMBL; AM690750; CAM84327.1; -; mRNA.
DR EMBL; AM690751; CAM84328.1; -; mRNA.
DR EMBL; AK014905; BAB29613.1; -; mRNA.
DR EMBL; AK083236; BAC38821.1; -; mRNA.
DR CCDS; CCDS51094.2; -. [A4Q9F0-1]
DR RefSeq; NP_001289887.1; NM_001302958.1. [A4Q9F0-2]
DR AlphaFoldDB; A4Q9F0; -.
DR SMR; A4Q9F0; -.
DR IntAct; A4Q9F0; 10.
DR STRING; 10090.ENSMUSP00000129369; -.
DR BindingDB; A4Q9F0; -.
DR ChEMBL; CHEMBL2401604; -.
DR iPTMnet; A4Q9F0; -.
DR PhosphoSitePlus; A4Q9F0; -.
DR PaxDb; A4Q9F0; -.
DR PRIDE; A4Q9F0; -.
DR ProteomicsDB; 298020; -. [A4Q9F0-1]
DR ProteomicsDB; 298021; -. [A4Q9F0-2]
DR GeneID; 70892; -.
DR KEGG; mmu:70892; -.
DR UCSC; uc008rrw.2; mouse. [A4Q9F0-2]
DR UCSC; uc008rrx.2; mouse. [A4Q9F0-1]
DR CTD; 79739; -.
DR MGI; MGI:1918142; Ttll7.
DR eggNOG; KOG2158; Eukaryota.
DR InParanoid; A4Q9F0; -.
DR BRENDA; 6.3.2.B24; 3474.
DR Reactome; R-MMU-8955332; Carboxyterminal post-translational modifications of tubulin.
DR BioGRID-ORCS; 70892; 1 hit in 40 CRISPR screens.
DR PRO; PR:A4Q9F0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A4Q9F0; protein.
DR GO; GO:0097731; C:9+0 non-motile cilium; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0018095; P:protein polyglutamylation; 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 Alternative splicing; ATP-binding; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Ligase; Magnesium;
KW Metal-binding; Microtubule; Neurogenesis; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..912
FT /note="Tubulin polyglutamylase TTLL7"
FT /id="PRO_0000326163"
FT DOMAIN 38..390
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 251..252
FT /note="L-glutamate"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT REGION 388..450
FT /note="c-MTBD region"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT REGION 547..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 166..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 188..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 201..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 227
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 249..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 271
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 367
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 106
FT /note="Binds negatively charged residues of beta-tubulin C-
FT terminal tails"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT SITE 352
FT /note="Binds negatively charged residues of beta-tubulin C-
FT terminal tails"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT VAR_SEQ 596..609
FT /note="PSGSHNLIYSESPV -> SSKSISPTSLEEEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17499049"
FT /id="VSP_052730"
FT VAR_SEQ 610..912
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17499049"
FT /id="VSP_052731"
FT MUTAGEN 349
FT /note="E->V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16901895"
FT CONFLICT 98
FT /note="F -> Y (in Ref. 2; BAB29613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 912 AA; 105501 MW; ABCDD119BFF29336 CRC64;
MPSLPQDGVI QGSSPVDLGT ELPYQCTMKR KVRKKKKKGI ITANVAGTKF EIVRLVIDEM
GFMKTPDEDE TSNLIWCDAA VQQEKITDLQ NYQRINHFPG MGEICRKDFL ARNMTKMIKS
RPMDYTFVPR TWIFPSEYTQ FQNYVKELKK KRKQKTFIVK PANGAMGHGI SLIRNGDKVP
SQDHLIVQEY IEKPFLMEGY KFDLRIYILV TSCDPLKIFL YHDGLVRMGT EKYIPPNESN
LTQLYMHLTN YSVNKHNERF ERNETEDKGS KRSIKWFTEF LQANQHDVTK FWSDISELVV
KTLIVAEPHV LHAYRMCRPG QPPGSESVCF EVLGFDILLD RKLKPWLLEI NRAPSFGTDQ
KIDYDVKRGV LLNALKLLNI RTSDKRKNLA KQKAEAQRRL YGQNPVRRLS PGSSDWEQQR
HQLERRKEEL KERLLQVRKQ VSQEEHENRH MGNYRRIYPP EDKALLEKYE GLLAVAFQTF
LSGRAASFQR EMNNPLKKMR EEDLLDLLEQ CEIDDEKLMG KTGRVRGPKP LCCMPECAEV
TKKQKYYGSS DSSYDSSSSS SNSELDENEK ELCQKRLDQV PYSLKHTSHC KIIQQPSGSH
NLIYSESPVY LTTLVFLSEF PDSMRRSVSC PRSISAHLPS RGDVRPFSSQ QVIPLARPTS
ASRSHSLNRA SSYARHLPHG SDTGSTNTLN ESLRQLKTKE QEDDLTSQTL FVLKDMRIRF
PGKSDAESEL LIEDIMDNWK HYKTKVASYW LIKLDSVKQR KVLDIVKSSI RTVLPRIWRV
PDAEELSLYR IFNRVFNRLL WSHGQGLWSC FCDSGSSWES IFSKSPEVVT PLQLQCCQRL
VELCKQCLLV VYKYTTETRG PISGIGPDWG NSRYLLPGST QFLMRSPLYN MKYNSPGMTR
SNVLFTSRYG RL
