ID ANK3_HUMAN Reviewed; 4377 AA. AC Q12955; Q5VXD5; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 3. DT 10-AUG-2010, entry version 95. DE RecName: Full=Ankyrin-3; DE Short=ANK-3; DE AltName: Full=Ankyrin-G; GN Name=ANK3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Brain stem; RX MEDLINE=95138209; PubMed=7836469; DOI=10.1074/jbc.270.5.2352; RA Kordeli E., Lambert S., Bennett V.; RT "AnkyrinG. A new ankyrin gene with neural-specific isoforms localized RT at the axonal initial segment and node of Ranvier."; RL J. Biol. Chem. 270:2352-2359(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [3] RP INTERACTION WITH RHBG. RX PubMed=15611082; DOI=10.1074/jbc.M413351200; RA Lopez C., Metral S., Eladari D., Drevensek S., Gane P., Chambrey R., RA Bennett V., Cartron J.-P., Le Van Kim C., Colin Y.; RT "The ammonium transporter RhBG: requirement of a tyrosine-based signal RT and ankyrin-G for basolateral targeting and membrane anchorage in RT polarized kidney epithelial cells."; RL J. Biol. Chem. 280:8221-8228(2005). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-533, AND MASS RP SPECTROMETRY. RC TISSUE=Lung carcinoma; RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4298, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=17287340; DOI=10.1073/pnas.0611217104; RA Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; RT "Global proteomic profiling of phosphopeptides using electron transfer RT dissociation tandem mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). RN [6] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-4338, AND MASS RP SPECTROMETRY. RC TISSUE=Mammary cancer; RX PubMed=17370265; DOI=10.1002/pmic.200600410; RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; RT "Tryptic digestion of ubiquitin standards reveals an improved strategy RT for identifying ubiquitinated proteins by mass spectrometry."; RL Proteomics 7:868-874(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. CC -!- FUNCTION: Membrane-cytoskeleton linker. May participate in the CC maintenance/targeting of ion channels and cell adhesion molecules CC at the nodes of Ranvier and axonal initial segments. CC -!- SUBUNIT: May be a constituent of a neurofascin/NRCAM/ankyrin G CC complex. Interacts with RHBG. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- TISSUE SPECIFICITY: Expressed in brain, neurons and other tissues. CC -!- SIMILARITY: Contains 23 ANK repeats. CC -!- SIMILARITY: Contains 1 death domain. CC -!- SIMILARITY: Contains 1 ZU5 domain. CC -!- SEQUENCE CAUTION: CC Sequence=CAH73232.1; Type=Erroneous gene model prediction; CC Sequence=CAI40518.1; Type=Erroneous gene model prediction; CC Sequence=CAI41373.1; Type=Erroneous gene model prediction; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ankyrin entry; CC URL="http://en.wikipedia.org/wiki/Ankyrin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U13616; AAA64834.1; -; mRNA. DR EMBL; AL359267; CAH73232.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC023904; CAH73232.1; JOINED; Genomic_DNA. DR EMBL; AL359377; CAH73232.1; JOINED; Genomic_DNA. DR EMBL; AL592430; CAH73232.1; JOINED; Genomic_DNA. DR EMBL; AL592430; CAI40518.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC023904; CAI40518.1; JOINED; Genomic_DNA. DR EMBL; AL359267; CAI40518.1; JOINED; Genomic_DNA. DR EMBL; AL359377; CAI40518.1; JOINED; Genomic_DNA. DR EMBL; AL359377; CAI41373.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC023904; CAI41373.1; JOINED; Genomic_DNA. DR EMBL; AL359267; CAI41373.1; JOINED; Genomic_DNA. DR EMBL; AL592430; CAI41373.1; JOINED; Genomic_DNA. DR IPI; IPI00921566; -. DR PIR; A55575; A55575. DR RefSeq; NP_001140.2; -. DR RefSeq; NP_066267.2; -. DR UniGene; Hs.499725; -. DR ProteinModelPortal; Q12955; -. DR IntAct; Q12955; 1. DR STRING; Q12955; -. DR PhosphoSite; Q12955; -. DR PRIDE; Q12955; -. DR Ensembl; ENST00000373827; ENSP00000362933; ENSG00000151150; Homo sapiens. DR GeneID; 288; -. DR KEGG; hsa:288; -. DR CTD; 288; -. DR GeneCards; GC10M061788; -. DR HGNC; HGNC:494; ANK3. DR HPA; CAB015179; -. DR MIM; 600465; gene. DR PharmGKB; PA24800; -. DR eggNOG; prNOG12951; -. DR HOVERGEN; HBG024337; -. DR InParanoid; Q12955; -. DR OMA; SYEFTSK; -. DR OrthoDB; EOG9VHNS3; -. DR PhylomeDB; Q12955; -. DR Reactome; REACT_18266; Axon guidance. DR NextBio; 1175; -. DR ArrayExpress; Q12955; -. DR Bgee; Q12955; -. DR CleanEx; HS_ANK3; -. DR Genevestigator; Q12955; -. DR GermOnline; ENSG00000151150; Homo sapiens. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. DR InterPro; IPR000488; Death. DR InterPro; IPR011029; DEATH-like. DR InterPro; IPR000906; ZU5. DR Gene3D; G3DSA:1.25.40.20; ANK; 4. DR Gene3D; G3DSA:1.10.533.10; DEATH_like; 1. DR Pfam; PF00023; Ank; 20. DR Pfam; PF00531; Death; 1. DR Pfam; PF00791; ZU5; 1. DR SMART; SM00248; ANK; 22. DR SMART; SM00005; DEATH; 1. DR SMART; SM00218; ZU5; 1. DR SUPFAM; SSF48403; ANK; 3. DR SUPFAM; SSF47986; DEATH_like; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 21. DR PROSITE; PS50017; DEATH_DOMAIN; 1. DR PROSITE; PS51145; ZU5; 1. PE 1: Evidence at protein level; KW ANK repeat; Complete proteome; Cytoplasm; Cytoskeleton; KW Isopeptide bond; Phosphoprotein; Polymorphism; Repeat; KW Ubl conjugation. FT CHAIN 1 4377 Ankyrin-3. FT /FTId=PRO_0000066886. FT REPEAT 73 102 ANK 1. FT REPEAT 106 135 ANK 2. FT REPEAT 139 168 ANK 3. FT REPEAT 172 201 ANK 4. FT REPEAT 203 230 ANK 5. FT REPEAT 234 263 ANK 6. FT REPEAT 267 296 ANK 7. FT REPEAT 300 329 ANK 8. FT REPEAT 333 362 ANK 9. FT REPEAT 366 395 ANK 10. FT REPEAT 399 428 ANK 11. FT REPEAT 432 461 ANK 12. FT REPEAT 465 494 ANK 13. FT REPEAT 498 527 ANK 14. FT REPEAT 531 560 ANK 15. FT REPEAT 564 593 ANK 16. FT REPEAT 597 626 ANK 17. FT REPEAT 630 659 ANK 18. FT REPEAT 663 692 ANK 19. FT REPEAT 696 725 ANK 20. FT REPEAT 729 758 ANK 21. FT REPEAT 762 791 ANK 22. FT REPEAT 795 825 ANK 23. FT DOMAIN 982 1089 ZU5. FT DOMAIN 4090 4174 Death. FT COMPBIAS 1519 1898 Ser-rich. FT COMPBIAS 2247 2250 Poly-Thr. FT COMPBIAS 2393 2396 Poly-Glu. FT COMPBIAS 3205 3211 Poly-Glu. FT COMPBIAS 3255 3259 Poly-Pro. FT COMPBIAS 3482 3487 Poly-Ser. FT COMPBIAS 3785 3791 Poly-Asn. FT COMPBIAS 3957 3981 Thr-rich. FT MOD_RES 533 533 Phosphotyrosine. FT MOD_RES 1459 1459 Phosphoserine. FT MOD_RES 4298 4298 Phosphoserine. FT CROSSLNK 4338 4338 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VARIANT 2318 2318 K -> R (in dbSNP:rs59021407). FT /FTId=VAR_061013. FT VARIANT 2885 2885 H -> Q (in dbSNP:rs11599164). FT /FTId=VAR_059115. FT VARIANT 2996 2996 Q -> H (in dbSNP:rs41274672). FT /FTId=VAR_061014. FT VARIANT 3117 3117 I -> V (in dbSNP:rs28932171). FT /FTId=VAR_059116. FT VARIANT 3123 3123 K -> R (in dbSNP:rs10821668). FT /FTId=VAR_059117. FT VARIANT 4257 4257 I -> V (in dbSNP:rs12261793). FT /FTId=VAR_054333. FT CONFLICT 1036 1043 MVEGEGLA -> HGERRGIS (in Ref. 1; FT AAA64834). FT CONFLICT 1418 1418 P -> R (in Ref. 1; AAA64834). FT CONFLICT 1574 1574 F -> L (in Ref. 1; AAA64834). FT CONFLICT 1685 1685 A -> R (in Ref. 1; AAA64834). FT CONFLICT 1726 1726 P -> A (in Ref. 1; AAA64834). FT CONFLICT 2062 2063 ER -> GG (in Ref. 1; AAA64834). FT CONFLICT 2146 2146 S -> T (in Ref. 1; AAA64834). FT CONFLICT 3919 3919 H -> P (in Ref. 1; AAA64834). SQ SEQUENCE 4377 AA; 480410 MW; F6F9FABD09F15C13 CRC64; MAHAASQLKK NRDLEINAEE EPEKKRKHRK RSRDRKKKSD ANASYLRAAR AGHLEKALDY IKNGVDINIC NQNGLNALHL ASKEGHVEVV SELLQREANV DAATKKGNTA LHIASLAGQA EVVKVLVTNG ANVNAQSQNG FTPLYMAAQE NHLEVVKFLL DNGASQSLAT EDGFTPLAVA LQQGHDQVVS LLLENDTKGK VRLPALHIAA RKDDTKAAAL LLQNDNNADV ESKSGFTPLH IAAHYGNINV ATLLLNRAAA VDFTARNDIT PLHVASKRGN ANMVKLLLDR GAKIDAKTRD GLTPLHCGAR SGHEQVVEML LDRAAPILSK TKNGLSPLHM ATQGDHLNCV QLLLQHNVPV DDVTNDYLTA LHVAAHCGHY KVAKVLLDKK ANPNAKALNG FTPLHIACKK NRIKVMELLL KHGASIQAVT ESGLTPIHVA AFMGHVNIVS QLMHHGASPN TTNVRGETAL HMAARSGQAE VVRYLVQDGA QVEAKAKDDQ TPLHISARLG KADIVQQLLQ QGASPNAATT SGYTPLHLSA REGHEDVAAF LLDHGASLSI TTKKGFTPLH VAAKYGKLEV ANLLLQKSAS PDAAGKSGLT PLHVAAHYDN QKVALLLLDQ GASPHAAAKN GYTPLHIAAK KNQMDIATTL LEYGADANAV TRQGIASVHL AAQEGHVDMV SLLLGRNANV NLSNKSGLTP LHLAAQEDRV NVAEVLVNQG AHVDAQTKMG YTPLHVGCHY GNIKIVNFLL QHSAKVNAKT KNGYTPLHQA AQQGHTHIIN VLLQNNASPN ELTVNGNTAL GIARRLGYIS VVDTLKIVTE ETMTTTTVTE KHKMNVPETM NEVLDMSDDE VRKANAPEML SDGEYISDVE EGEDAMTGDT DKYLGPQDLK ELGDDSLPAE GYMGFSLGAR SASLRSFSSD RSYTLNRSSY ARDSMMIEEL LVPSKEQHLT FTREFDSDSL RHYSWAADTL DNVNLVSSPI HSGFLVSFMV DARGGSMRGS RHHGMRIIIP PRKCTAPTRI TCRLVKRHKL ANPPPMVEGE GLASRLVEMG PAGAQFLGPV IVEIPHFGSM RGKERELIVL RSENGETWKE HQFDSKNEDL TELLNGMDEE LDSPEELGKK RICRIITKDF PQYFAVVSRI KQESNQIGPE GGILSSTTVP LVQASFPEGA LTKRIRVGLQ AQPVPDEIVK KILGNKATFS PIVTVEPRRR KFHKPITMTI PVPPPSGEGV SNGYKGDTTP NLRLLCSITG GTSPAQWEDI TGTTPLTFIK DCVSFTTNVS ARFWLADCHQ VLETVGLATQ LYRELICVPY MAKFVVFAKM NDPVESSLRC FCMTDDKVDK TLEQQENFEE VARSKDIEVL EGKPIYVDCY GNLAPLTKGG QQLVFNFYSF KENRLPFSIK IRDTSQEPCG RLSFLKEPKT TKGLPQTAVC NLNITLPAHK KETESDQDDE IEKTDRRQSF ASLALRKRYS YLTEPGMIER STGATRSLPT TYSYKPFFST RPYQSWTTAP ITVPGPAKSG FTSLSSSSSN TPSASPLKSI WSVSTPSPIK STLGASTTSS VKSISDVASP IRSFRTMSSP IKTVVSQSPY NIQVSSGTLA RAPAVTEATP LKGLASNSTF SSRTSPVTTA GSLLERSSIT MTPPASPKSN INMYSSSLPF KSIITSAAPL ISSPLKSVVS PVKSAVDVIS SAKITMASSL SSPVKQMPGH AEVALVNGSI SPLKYPSSST LINGCKATAT LQEKISSATN SVSSVVSAAT DTVEKVFSTT TAMPFSPLRS YVSAAPSAFQ SLRTPSASAL YTSLGSSISA TTSSVTSSII TVPVYSVVNV LPEPALKKLP DSNSFTKSAA ALLSPIKTLT TETHPQPHFS RTSSPVKSSL FLAPSALKLS TPSSLSSSQE ILKDVAEMKE DLMRMTAILQ TDVPEEKPFQ PELPKEGRID DEEPFKIVEK VKEDLVKVSE ILKKDVCVDN KGSPKSPKSD KGHSPEDDWI EFSSEEIREA RQQAAASQSP SLPERVQVKA KAASEKDYNL TKVIDYLTND IGSSSLTNLK YKFEDAKKDG EERQKRVLKP AIALQEHKLK MPPASMRTST SEKELCKMAD SFFGTDTILE SPDDFSQHDQ DKSPLSDSGF ETRSEKTPSA PQSAESTGPK PLFHEVPIPP VITETRTEVV HVIRSYDPSA GDVPQTQPEE PVSPKPSPTF MELEPKPTTS SIKEKVKAFQ MKASSEEDDH NRVLSKGMRV KEETHITTTT RMVYHSPPGG EGASERIEET MSVHDIMKAF QSGRDPSKEL AGLFEHKSAV SPDVHKSAAE TSAQHAEKDN QMKPKLERII EVHIEKGNQA EPTEVIIRET KKHPEKEMYV YQKDLSRGDI NLKDFLPEKH DAFPCSEEQG QQEEEELTAE ESLPSYLESS RVNTPVSQEE DSRPSSAQLI SDDSYKTLKL LSQHSIEYHD DELSELRGES YRFAEKMLLS EKLDVSHSDT EESVTDHAGP PSSELQGSDK RSREKIATAP KKEILSKIYK DVSENGVGKV SKDEHFDKVT VLHYSGNVSS PKHAMWMRFT EDRLDRGREK LIYEDRVDRT VKEAEEKLTE VSQFFRDKTE KLNDELQSPE KKARPKNGKE YSSQSPTSSS PEKVLLTELL ASNDEWVKAR QHGPDGQGFP KAEEKAPSLP SSPEKMVLSQ QTEDSKSTVE AKGSISQSKA PDGPQSGFQL KQSKLSSIRL KFEQGTHAKS KDMSQEDRKS DGQSRIPVKK IQESKLPVYQ VFAREKQQKA IDLPDESVSV QKDFMVLKTK DEHAQSNEIV VNDSGSDNVK KQRTEMSSKA MPDSFSEQQA KDLACHITSD LATRGPWDKK VFRTWESSGA TNNKSQKEKL SHVLVHDVRE NHIGHPESKS VDQKNEFMSV TERERKLLTN GSLSEIKEMT VKSPSKKVLY REYVVKEGDH PGGLLDQPSR RSESSAVSHI PVRVADERRM LSSNIPDGFC EQSAFPKHEL SQKLSQSSMS KETVETQHFN SIEDEKVTYS EISKVSKHQS YVGLCPPLEE TETSPTKSPD SLEFSPGKES PSSDVFDHSP IDGLEKLAPL AQTEGGKEIK TLPVYVSFVQ VGKQYEKEIQ QGGVKKIISQ ECKTVQETRG TFYTTRQQKQ PPSPQGSPED DTLEQVSFLD SSGKSPLTPE TPSSEEVSYE FTSKTPDSLI AYIPGKPSPI PEVSEESEEE EQAKSTSLKQ TTVEETAVER EMPNDVSKDS NQRPKNNRVA YIEFPPPPPL DADQIESDKK HHYLPEKEVD MIEVNLQDEH DKYQLAEPVI RVQPPSPVPP GADVSDSSDD ESIYQPVPVK KYTFKLKEVD DEQKEKPKAS AEKASNQKEL ESNGSGKDNE FGLGLDSPQN EIAQNGNNDQ SITECSIATT AEFSHDTDAT EIDSLDGYDL QDEDDGLTES DSKLPIQAME IKKDIWNTEG ILKPADRSFS QSKLEVIEEE GKVGPDEDKP PSKSSSSEKT PDKTDQKSGA QFFTLEGRHP DRSVFPDTYF SYKVDEEFAT PFKTVATKGL DFDPWSNNRG DDEVFDSKSR EDETKPFGLA VEDRSPATTP DTTPARTPTD ESTPTSEPNP FPFHEGKMFE MTRSGAIDMS KRDFVEERLQ FFQIGEHTSE GKSGDQGEGD KSMVTATPQP QSGDTTVETN LERNVETPTV EPNPSIPTSG ECQEGTSSSG SLEKSAAATN TSKVDPKLRT PIKMGISAST MTMKKEGPGE ITDKIEAVMT SCQGLENETI TMISNTANSQ MGVRPHEKHD FQKDNFNNNN NLDSSTIQTD NIMSNIVLTE HSAPTCTTEK DNPVKVSSGK KTGVLQGHCV RDKQKVLGEQ QKTKELIGIR QKSKLPIKAT SPKDTFPPNH MSNTKASKMK QVSQSEKTKA LTTSSCVDVK SRIPVKNTHR DNIIAVRKAC ATQKQGQPEK GKAKQLPSKL PVKVRSTCVT TTTTTATTTT TTTTTTTTSC TVKVRKSQLK EVCKHSIEYF KGISGETLKL VDRLSEEEKK MQSELSDEEE STSRNTSLSE TSRGGQPSVT TKSARDKKTE AAPLKSKSEK AGSEKRSSRR TGPQSPCERT DIRMAIVADH LGLSWTELAR ELNFSVDEIN QIRVENPNSL ISQSFMLLKK WVTRDGKNAT TDALTSVLTK INRIDIVTLL EGPIFDYGNI SGTRSFADEN NVFHDPVDGW QNETSSGNLE SCAQARRVTG GLLDRLDDSP DQCRDSITSY LKGEAGKFEA NGSHTEITPE AKTKSYFPES QNDVGKQSTK ETLKPKIHGS GHVEEPASPL AAYQKSLEET SKLIIEETKP CVPVSMKKMS RTSPADGKPR LSLHEEEGSS GSEQKQGEGF KVKTKKEIRH VEKKSHS //