TNKS2_MOUSE
ID TNKS2_MOUSE Reviewed; 1166 AA.
AC Q3UES3; Q6P537; Q8BXH7;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Poly [ADP-ribose] polymerase tankyrase-2 {ECO:0000305};
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:Q9H2K2};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 6;
DE Short=ARTD6;
DE AltName: Full=Protein poly-ADP-ribosyltransferase tankyrase-2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9H2K2};
DE AltName: Full=TNKS-2;
DE AltName: Full=TRF1-interacting ankyrin-related ADP-ribose polymerase 2;
DE AltName: Full=Tankyrase II;
DE AltName: Full=Tankyrase-2;
DE Short=TANK2;
GN Name=Tnks2 {ECO:0000312|MGI:MGI:1921743}; Synonyms=Tank2;
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=Cerebellum, and Liver;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 759-1166.
RC TISSUE=Embryo;
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).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase involved in various processes
CC such as Wnt signaling pathway, telomere length and vesicle trafficking.
CC Acts as an activator of the Wnt signaling pathway by mediating poly-
CC ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-
CC catenin destruction complex: poly-ADP-ribosylated target proteins are
CC recognized by RNF146, which mediates their ubiquitination and
CC subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1
CC and CASC3, followed by recruitment of RNF146 and subsequent
CC ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby
CC contributing to the regulation of telomere length. Stimulates 26S
CC proteasome activity. {ECO:0000250|UniProtKB:Q9H2K2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000250|UniProtKB:Q9H2K2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Oligomerizes and associates with TNKS. Interacts with the
CC cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to
CC the N-terminus of Grb14 and TRF1 with its ankyrin repeat region.
CC Interacts with HIF1AN. Interacts with RNF146; this interaction leads to
CC ubiquitination and proteasomal degradation. Interacts with NUMA1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9H2K2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H2K2}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q9H2K2}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9H2K2}. Nucleus
CC {ECO:0000250|UniProtKB:Q9H2K2}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q9H2K2}. Note=Associated with the Golgi and with
CC juxtanuclear SLC2A4/GLUT4-vesicles (By similarity). Also found around
CC the pericentriolar matrix of mitotic centromeres (By similarity).
CC During interphase, a small fraction of TNKS2 is found in the nucleus,
CC associated with TRF1 (By similarity). {ECO:0000250|UniProtKB:Q9H2K2}.
CC -!- PTM: Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to
CC its degradation. {ECO:0000250|UniProtKB:Q9H2K2}.
CC -!- PTM: ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is
CC recognized by RNF146, followed by ubiquitination.
CC {ECO:0000250|UniProtKB:Q9H2K2}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AK047094; BAC32960.2; -; mRNA.
DR EMBL; AK149368; BAE28838.1; -; mRNA.
DR EMBL; AC116128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063101; AAH63101.1; -; mRNA.
DR CCDS; CCDS50426.1; -.
DR RefSeq; NP_001157107.1; NM_001163635.1.
DR AlphaFoldDB; Q3UES3; -.
DR SMR; Q3UES3; -.
DR BioGRID; 216798; 18.
DR CORUM; Q3UES3; -.
DR IntAct; Q3UES3; 19.
DR STRING; 10090.ENSMUSP00000025729; -.
DR BindingDB; Q3UES3; -.
DR ChEMBL; CHEMBL3232703; -.
DR iPTMnet; Q3UES3; -.
DR PhosphoSitePlus; Q3UES3; -.
DR SwissPalm; Q3UES3; -.
DR EPD; Q3UES3; -.
DR MaxQB; Q3UES3; -.
DR PaxDb; Q3UES3; -.
DR PRIDE; Q3UES3; -.
DR ProteomicsDB; 258938; -.
DR Antibodypedia; 30362; 223 antibodies from 30 providers.
DR Ensembl; ENSMUST00000025729; ENSMUSP00000025729; ENSMUSG00000024811.
DR GeneID; 74493; -.
DR KEGG; mmu:74493; -.
DR UCSC; uc008hhu.2; mouse.
DR CTD; 80351; -.
DR MGI; MGI:1921743; Tnks2.
DR VEuPathDB; HostDB:ENSMUSG00000024811; -.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000159911; -.
DR HOGENOM; CLU_004303_0_0_1; -.
DR InParanoid; Q3UES3; -.
DR OMA; YQIIKPE; -.
DR OrthoDB; 111565at2759; -.
DR PhylomeDB; Q3UES3; -.
DR TreeFam; TF326036; -.
DR Reactome; R-MMU-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR BioGRID-ORCS; 74493; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Tnks2; mouse.
DR PRO; PR:Q3UES3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3UES3; protein.
DR Bgee; ENSMUSG00000024811; Expressed in primitive streak and 255 other tissues.
DR ExpressionAtlas; Q3UES3; baseline and differential.
DR Genevisible; Q3UES3; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000242; C:pericentriolar material; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:MGI.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0000723; P:telomere maintenance; ISS:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 5.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 5.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 15.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 15.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; ANK repeat; Chromosome; Cytoplasm; Glycosyltransferase;
KW Golgi apparatus; Hydroxylation; Membrane; Metal-binding; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Telomere;
KW Transferase; Ubl conjugation; Wnt signaling pathway; Zinc.
FT CHAIN 1..1166
FT /note="Poly [ADP-ribose] polymerase tankyrase-2"
FT /id="PRO_0000409512"
FT REPEAT 23..52
FT /note="ANK 1"
FT REPEAT 57..86
FT /note="ANK 2"
FT REPEAT 90..119
FT /note="ANK 3"
FT REPEAT 123..152
FT /note="ANK 4"
FT REPEAT 210..239
FT /note="ANK 5"
FT REPEAT 243..272
FT /note="ANK 6"
FT REPEAT 276..305
FT /note="ANK 7"
FT REPEAT 363..395
FT /note="ANK 8"
FT REPEAT 399..428
FT /note="ANK 9"
FT REPEAT 432..461
FT /note="ANK 10"
FT REPEAT 463..489
FT /note="ANK 11"
FT REPEAT 525..554
FT /note="ANK 12"
FT REPEAT 558..587
FT /note="ANK 13"
FT REPEAT 591..620
FT /note="ANK 14"
FT REPEAT 624..652
FT /note="ANK 15"
FT REPEAT 678..707
FT /note="ANK 16"
FT REPEAT 711..740
FT /note="ANK 17"
FT REPEAT 744..773
FT /note="ANK 18"
FT DOMAIN 873..936
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 959..1164
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 545..553
FT /note="HIF1AN-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9H2K2"
FT BINDING 1081
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1084
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1089
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1092
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT MOD_RES 203
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 238
FT /note="(3S)-3-hydroxyhistidine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 271
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 427
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 518
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 553
FT /note="(3S)-3-hydroxyhistidine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 586
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 671
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 706
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 739
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT CONFLICT 116
FT /note="D -> H (in Ref. 1; BAC32960)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="K -> E (in Ref. 1; BAC32960)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="G -> E (in Ref. 1; BAC32960)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="P -> T (in Ref. 1; BAE28838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1166 AA; 126744 MW; 5C1E11B74BB11FC9 CRC64;
MSGRRCAGGG AACASAGAEA VEPSARELFE ACRNGDVERV KRLVTPEKVN SRDTAGRKST
PLHFAAGFGR KDVVEYLLQN GANVQARDDG GLIPLHNACS FGHAEVVNLL LQHGADPNAR
DNWNYTPLHE AAIKGKIDVC IVLLQHGAEP TIRNTDGRTA LDLADPSAKA VLTGDYKKDE
LLESARSGNE EKMMALLTPL NVNCHASDGR KSTPLHLAAG YNRVKIVQLL LHHGADVHAK
DKGDLVPLHN ACSYGHYEVT ELLVKHGACV NAMDLWQFTP LHEAASKNRI EVCSLLLSYG
ADPTLLNCHN KSAIDLAPTA QLKERLSYEF KGHSLLQAAR EADVTRIKKH LSLEMVNFKH
PQTHETALHC AAASPYPKRK QICELLLRKG ANTNEKTKEF LTPLHVASEN AHNDVVEVVV
KHEAKVNALD SLGQTSLHRA AHCGHLQTCR LLLSYGCDPN IISLQGFTAL QMGNENVQQL
LQEGASLGHS EADRQLLEAA KAGDVETVKK LCTVQSVNCR DIEGRQSTPL HFAAGYNRVS
VVEYLLQHGA DVHAKDKGGL VPLHNACSYG HYEVAELLVK HGAVVNVADL WKFTPLHEAA
AKGKYEICKL LLQHGADPTK KNRDGNTPLD LVKDGDTDIQ DLLRGDAALL DAAKKGCLAR
VKKLSSPDNV NCRDTQGRHS TPLHLAAGYN NLEVAEYLLQ HGADVNAQDK GGLIPLHNAA
SYGHVDVAAL LIKYNACVNA TDKWAFTPLH EAAQKGRTQL CALLLAHGAD PTLKNQEGQT
PLDLVSADDV SALLTAAMPP SALPTCYKPQ VLSGVRGPGA TADALSSGPS SPSSLSAASS
LDNLSGSFSE LSAVVSSSAA EGATGLQRKE DSGIDFSITQ FIRNLGLEHL MDIFEREQIT
LDVLVEMGHK ELKEIGINAY GHRHKLIKGV ERLISGQQGL NPYLTLNNSG SGTILIDLSP
DDKEFQSVEE EMQSTVREHR DGGHAGGVFN RYNILKIQKV CNKKLWERYT HRRKEVSEEN
HNHANERMLF HGSPFVNAII HKGFDERHAY IGGMFGAGIY FAENSSKSNQ YVYGIGGGTG
CPIHKDRSCY ICHRQLLFCR VTLGKSFLQF SAMKMAHSPP GHHSVTGRPS VNGLALAEYV
IYRGEQAYPE YLITYQIVRP EGMVDG
