TTBK2_MOUSE
ID TTBK2_MOUSE Reviewed; 1243 AA.
AC Q3UVR3; A2AW12; Q3TSR6; Q3UFW0; Q571D1; Q8BKA4; Q924U8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Tau-tubulin kinase 2;
DE EC=2.7.11.1;
DE AltName: Full=Protein bartleby;
GN Name=Ttbk2; Synonyms=Bby, Kiaa0847, Ttbk1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Eye, and Medulla oblongata;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-320, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=11257498; DOI=10.1016/s0014-5793(01)02256-6;
RA Tomizawa K., Omori A., Ohtake A., Sato K., Takahashi M.;
RT "Tau-tubulin kinase phosphorylates tau at Ser-208 and Ser-210, sites found
RT in paired helical filament-tau.";
RL FEBS Lett. 492:221-227(2001).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ASP-163.
RX PubMed=23141541; DOI=10.1016/j.cell.2012.10.010;
RA Goetz S.C., Liem K.F. Jr., Anderson K.V.;
RT "The spinocerebellar ataxia-associated gene tau tubulin kinase 2 controls
RT the initiation of ciliogenesis.";
RL Cell 151:847-858(2012).
CC -!- FUNCTION: Serine/threonine kinase that acts as a key regulator of
CC ciliogenesis: controls the initiation of ciliogenesis by binding to the
CC distal end of the basal body and promoting the removal of CCP110, which
CC caps the mother centriole, leading to the recruitment of IFT proteins,
CC which build the ciliary axoneme. Has some substrate preference for
CC proteins that are already phosphorylated on a Tyr residue at the +2
CC position relative to the phosphorylation site. Able to phosphorylate
CC tau on serines in vitro (PubMed:23141541). Phosphorylates MPHOSPH9
CC which promotes its ubiquitination and proteasomal degradation, loss of
CC MPHOSPH9 facilitates the removal of the CP110-CEP97 complex (a negative
CC regulator of ciliogenesis) from the mother centrioles, promoting the
CC initiation of ciliogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q6IQ55, ECO:0000269|PubMed:11257498,
CC ECO:0000269|PubMed:23141541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with CEP164. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:23141541}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:23141541}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:23141541}. Cytoplasm, cytosol {ECO:0000250}.
CC Nucleus {ECO:0000250}. Note=Localizes to the transition zone in primary
CC cilia in response to cell cycle signals that promote ciliogenesis. May
CC also be present in cytosol and, at lower level in the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UVR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UVR3-2; Sequence=VSP_018276;
CC -!- DISRUPTION PHENOTYPE: Defects in Ttbk2 are the cause of the bartleby
CC (bby) phenotype characterized by defects in sonic hedgehog/SHH
CC signaling and ciliogenesis. Embryos display morphological defects at
CC midgestation similar to those seen in mutants that lack cilia,
CC including holoprosencephaly, twisted body axis, abnormal limb
CC development and randomized laterality of heart looping. Mutants die at
CC midgestation (around 10.5 dpc). {ECO:0000269|PubMed:23141541}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90183.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK053820; BAC35540.1; -; mRNA.
DR EMBL; AK137024; BAE23206.1; -; mRNA.
DR EMBL; AK148269; BAE28449.1; -; mRNA.
DR EMBL; AK161858; BAE36609.1; -; mRNA.
DR EMBL; AK220258; BAD90183.1; ALT_INIT; mRNA.
DR EMBL; AL935168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB046593; BAB62004.2; -; mRNA.
DR CCDS; CCDS16627.1; -. [Q3UVR3-1]
DR RefSeq; NP_001020027.1; NM_001024856.2. [Q3UVR3-1]
DR RefSeq; NP_001020028.1; NM_001024857.2. [Q3UVR3-1]
DR RefSeq; NP_542966.2; NM_080788.3.
DR AlphaFoldDB; Q3UVR3; -.
DR SMR; Q3UVR3; -.
DR STRING; 10090.ENSMUSP00000028740; -.
DR iPTMnet; Q3UVR3; -.
DR PhosphoSitePlus; Q3UVR3; -.
DR MaxQB; Q3UVR3; -.
DR PaxDb; Q3UVR3; -.
DR PRIDE; Q3UVR3; -.
DR ProteomicsDB; 297670; -. [Q3UVR3-1]
DR ProteomicsDB; 297671; -. [Q3UVR3-2]
DR Antibodypedia; 6214; 228 antibodies from 30 providers.
DR DNASU; 140810; -.
DR Ensembl; ENSMUST00000057135; ENSMUSP00000055032; ENSMUSG00000090100. [Q3UVR3-1]
DR Ensembl; ENSMUST00000085840; ENSMUSP00000083001; ENSMUSG00000090100. [Q3UVR3-1]
DR GeneID; 140810; -.
DR KEGG; mmu:140810; -.
DR UCSC; uc008lww.2; mouse. [Q3UVR3-1]
DR CTD; 146057; -.
DR MGI; MGI:2155779; Ttbk2.
DR VEuPathDB; HostDB:ENSMUSG00000090100; -.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000160367; -.
DR InParanoid; Q3UVR3; -.
DR OMA; DPLHQRQ; -.
DR OrthoDB; 75271at2759; -.
DR BRENDA; 2.7.11.26; 3474.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 140810; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Ttbk2; mouse.
DR PRO; PR:Q3UVR3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UVR3; protein.
DR Bgee; ENSMUSG00000090100; Expressed in spermatid and 210 other tissues.
DR ExpressionAtlas; Q3UVR3; baseline and differential.
DR Genevisible; Q3UVR3; MM.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0021681; P:cerebellar granular layer development; IMP:ARUK-UCL.
DR GO; GO:0021935; P:cerebellar granule cell precursor tangential migration; IMP:ARUK-UCL.
DR GO; GO:0021549; P:cerebellum development; IMP:ARUK-UCL.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:1990403; P:embryonic brain development; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:1904527; P:negative regulation of microtubule binding; ISO:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:MGI.
DR GO; GO:1903828; P:negative regulation of protein localization; IMP:MGI.
DR GO; GO:1902817; P:negative regulation of protein localization to microtubule; ISO:MGI.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0033365; P:protein localization to organelle; IMP:MGI.
DR GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1243
FT /note="Tau-tubulin kinase 2"
FT /id="PRO_0000234343"
FT DOMAIN 21..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 674..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ55"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ55"
FT MOD_RES 1102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ55"
FT VAR_SEQ 1091..1243
FT /note="LRRYKVLGSSNSDSDLFSRLAQILQNGSQKSRSTTQCKSPGSPHNPKTPPKS
FT PVVPRRSPSASPRSSSLPRTSSSSPSRAGRPHHDQRSSSPHLGRSKSPPSHSGSSSSRR
FT SCQQEHCKPSKNGPKGSGSLHHHSTSSKTPPGKSKPASKLSR -> PGSPQAVHLITLL
FT QGPGNQRKAPRRPAGLAGWADLPGPPEPHPSRTRPVVQRSIPVAGSAPPGCPWRECACS
FT VASERLHRDGGRFRVAAARRGAGRSRRAVDRAQHPEFGG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018276"
FT MUTAGEN 163
FT /note="D->A: Abolishes serine/threonine-protein kinase
FT activity and ability to initiate ciliogenesis."
FT /evidence="ECO:0000269|PubMed:23141541"
FT CONFLICT 192
FT /note="Y -> C (in Ref. 4; BAB62004)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="N -> D (in Ref. 4; BAB62004)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="K -> E (in Ref. 4; BAB62004)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..320
FT /note="LHTR -> CTPA (in Ref. 4; BAB62004)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="P -> L (in Ref. 2; BAE28449)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="H -> R (in Ref. 2; BAE28449)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="G -> V (in Ref. 2; BAE28449)"
FT /evidence="ECO:0000305"
FT CONFLICT 890
FT /note="R -> G (in Ref. 2; BAE28449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1243 AA; 136770 MW; 978D68D7BC7A535E CRC64;
MSGGGEQPDI LSVGILVKER WKVLRKIGGG GFGEIYDALD MLTRENVALK VESAQQPKQV
LKMEVAVLKK LQGKDHVCRF IGCGRNDRFN YVVMQLQGRN LADLRRSQSR GTFTISTTLR
LGKQILESIE SIHSVGFLHR DIKPSNFAMG RFPSTCRKCF MLDFGLARQF TNSCGDVRPP
RAVAGFRGTV RYASINAHRN REMGRHDDLW SLFYMLVEFV VGQLPWRKIK DKEQVGSIKE
RYDHRLMLKH LPPEFSTFLD HISSLDYFTK PDYQLLTSVF DNSIKTFGVI ESDPFDWEKS
GTDGSLTTTT TSATPQLHTR LTPAAIGIAN ATPIPGDLLR ENTDEVFPDE QLSDGENGIP
VGVSPDKLPG SLGHPRPQEK DVWEEMDINK NKIKLGICKA ATEEENSHGQ VNGILNAPSL
GSPIRVRSEI TQPDRDVPLV RKLRSIHSFE LEKRLTLEPK PDTDKFLETC MEKMQKDSSA
GKEPVPPALP HKPCVPVVTH TDHIWHYDDE YLPDASKPAS ANTPEQADGG GSNGFIAVNL
SSCKQEVDSK EWVIVDKEQD LQDFRTNEVL GHKTTGSPSD EEPEVLQVLE GSPQDEKIQV
GPWTDNHHLK KESSGVVLAL SAECPATAAS ELYTDRLDLQ AGAASQFITV TPTSPMEAQA
EGPLTAITIP RPSVASTQST SGSFHYGPQP EKKDLQPLEP TVELYSPREN FSGLVVTEGE
LASGGSRVDL GLQIDHTGHD MLPNMRDGDT SQDLGPKDPP DHNRLAVKEF EHLPGETEER
SLLLGSENED ERLSKGQHCI EVSSPGELVT AERAQLAATE PLHVSETQNC SVLPNQDKTH
EIMKLLAVGT SEISPQAIDP HAEGQIGQMA AMQKNKLFKD DGIQSESLPR QQGDLSAFLH
QEGKREKVVP RNGELYHCVS ENEHGPPTRK DMLRSSFVTR HSRIPVLAQE IDSTFESSSA
ISAKEKLLQK KAYQPEIVKL LVEKRQFKSF LGDLSSASDK LIEEKLAAVP VPFSEEEVFA
PFSRLAADSH LSRSVEDSFL SPIISQARKS KIPRPVSWVS TDQINGSASP QFLPRPPPGK
PPVRPGVEAR LRRYKVLGSS NSDSDLFSRL AQILQNGSQK SRSTTQCKSP GSPHNPKTPP
KSPVVPRRSP SASPRSSSLP RTSSSSPSRA GRPHHDQRSS SPHLGRSKSP PSHSGSSSSR
RSCQQEHCKP SKNGPKGSGS LHHHSTSSKT PPGKSKPASK LSR
