ID ANK3_HUMAN Reviewed; 4372 AA. AC Q12955; Q5VXD5; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 2. DT 28-JUL-2009, entry version 83. 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] (ISOFORM 2). 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. 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-4293, AND MASS RP SPECTROMETRY. 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-4333, AND MASS RP SPECTROMETRY. 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-1454, AND MASS RP SPECTROMETRY. 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 [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. CC -!- FUNCTION: Membrane-cytoskeleton linker. The neural-specific CC isoforms may participate in the maintenance/targeting of ion CC channels and cell adhesion molecules at the nodes of Ranvier and CC axonal initial segments. CC -!- SUBUNIT: Neural-specific isoforms may be a constituent of a CC neurofascin/NRCAM/ankyrin G complex. Interacts with RHBG. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=A number of isoforms are produced; CC Name=1; Synonyms=480-kDa isoform; CC IsoId=Q12955-1; Sequence=Displayed; CC Name=2; CC IsoId=Q12955-2; Sequence=VSP_036243; CC -!- TISSUE SPECIFICITY: Expressed in brain and other tissues. Isoform CC 1 is neural-specific. CC -!- SIMILARITY: Contains 23 ANK repeats. CC -!- SIMILARITY: Contains 1 death domain. CC -!- SIMILARITY: Contains 1 ZU5 domain. 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; -; 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; -; 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; -; 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; IPI00472779; -. DR IPI; IPI00921566; -. DR PIR; A55575; A55575. DR RefSeq; NP_066267.2; -. DR UniGene; Hs.499725; -. DR HSSP; P16157; 1N11. DR PhosphoSite; Q12955; -. DR Ensembl; ENST00000280772; ENSP00000280772; ENSG00000151150; Homo sapiens. DR Ensembl; ENST00000373827; ENSP00000362933; ENSG00000151150; Homo sapiens. DR GeneID; 288; -. DR UCSC; uc001jky.1; human. DR GeneCards; GC10M061458; -. DR H-InvDB; HIX0008849; -. DR HGNC; HGNC:494; ANK3. DR HPA; CAB015179; -. DR MIM; 600465; gene. DR PharmGKB; PA24800; -. DR HOGENOM; Q12955; -. DR HOVERGEN; Q12955; -. DR OMA; Q12955; SPATTPD. DR NextBio; 1175; -. DR ArrayExpress; Q12955; -. DR Bgee; Q12955; -. DR CleanEx; HS_ANK3; -. DR GermOnline; ENSG00000151150; Homo sapiens. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; ANK. 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; 23. DR Pfam; PF00531; Death; 1. DR Pfam; PF00791; ZU5; 1. DR SMART; SM00248; ANK; 21. DR SMART; SM00005; DEATH; 1. DR SMART; SM00218; ZU5; 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 Alternative splicing; ANK repeat; Complete proteome; Cytoplasm; KW Cytoskeleton; Isopeptide bond; Phosphoprotein; Polymorphism; Repeat; KW Ubl conjugation. FT CHAIN 1 4372 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 663 690 ANK 19. FT REPEAT 691 720 ANK 20. FT REPEAT 724 753 ANK 21. FT REPEAT 757 786 ANK 22. FT REPEAT 790 820 ANK 23. FT DOMAIN 977 1084 ZU5. FT DOMAIN 4085 4169 Death. FT COMPBIAS 1514 1893 Ser-rich. FT COMPBIAS 2242 2245 Poly-Thr. FT COMPBIAS 2388 2391 Poly-Glu. FT COMPBIAS 3200 3206 Poly-Glu. FT COMPBIAS 3250 3254 Poly-Pro. FT COMPBIAS 3477 3482 Poly-Ser. FT COMPBIAS 3780 3786 Poly-Asn. FT COMPBIAS 3952 3976 Thr-rich. FT MOD_RES 533 533 Phosphotyrosine. FT MOD_RES 1454 1454 Phosphoserine. FT MOD_RES 4293 4293 Phosphoserine. FT CROSSLNK 4333 4333 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VAR_SEQ 690 690 V -> VNLSNK (in isoform 2). FT /FTId=VSP_036243. FT VARIANT 4252 4252 I -> V (in dbSNP:rs12261793). FT /FTId=VAR_054333. FT CONFLICT 1031 1038 MVEGEGLA -> HGERRGIS (in Ref. 1; FT AAA64834). FT CONFLICT 1413 1413 P -> R (in Ref. 1; AAA64834). FT CONFLICT 1569 1569 F -> L (in Ref. 1; AAA64834). FT CONFLICT 1680 1680 A -> R (in Ref. 1; AAA64834). FT CONFLICT 1721 1721 P -> A (in Ref. 1; AAA64834). FT CONFLICT 2057 2058 ER -> GG (in Ref. 1; AAA64834). FT CONFLICT 2141 2141 S -> T (in Ref. 1; AAA64834). FT CONFLICT 3914 3914 H -> P (in Ref. 1; AAA64834). SQ SEQUENCE 4372 AA; 479853 MW; 86E4A747C402562F 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 SGLTPLHLAA QEDRVNVAEV LVNQGAHVDA QTKMGYTPLH VGCHYGNIKI VNFLLQHSAK VNAKTKNGYT PLHQAAQQGH THIINVLLQN NASPNELTVN GNTALGIARR LGYISVVDTL KIVTEETMTT TTVTEKHKMN VPETMNEVLD MSDDEVRKAN APEMLSDGEY ISDVEEGEDA MTGDTDKYLG PQDLKELGDD SLPAEGYMGF SLGARSASLR SFSSDRSYTL NRSSYARDSM MIEELLVPSK EQHLTFTREF DSDSLRHYSW AADTLDNVNL VSSPIHSGFL VSFMVDARGG SMRGSRHHGM RIIIPPRKCT APTRITCRLV KRHKLANPPP MVEGEGLASR LVEMGPAGAQ FLGPVIVEIP HFGSMRGKER ELIVLRSENG ETWKEHQFDS KNEDLTELLN GMDEELDSPE ELGKKRICRI ITKDFPQYFA VVSRIKQESN QIGPEGGILS STTVPLVQAS FPEGALTKRI RVGLQAQPVP DEIVKKILGN KATFSPIVTV EPRRRKFHKP ITMTIPVPPP SGEGVSNGYK GDTTPNLRLL CSITGGTSPA QWEDITGTTP LTFIKDCVSF TTNVSARFWL ADCHQVLETV GLATQLYREL ICVPYMAKFV VFAKMNDPVE SSLRCFCMTD DKVDKTLEQQ ENFEEVARSK DIEVLEGKPI YVDCYGNLAP LTKGGQQLVF NFYSFKENRL PFSIKIRDTS QEPCGRLSFL KEPKTTKGLP QTAVCNLNIT LPAHKKETES DQDDEIEKTD RRQSFASLAL RKRYSYLTEP GMIERSTGAT RSLPTTYSYK PFFSTRPYQS WTTAPITVPG PAKSGFTSLS SSSSNTPSAS PLKSIWSVST PSPIKSTLGA STTSSVKSIS DVASPIRSFR TMSSPIKTVV SQSPYNIQVS SGTLARAPAV TEATPLKGLA SNSTFSSRTS PVTTAGSLLE RSSITMTPPA SPKSNINMYS SSLPFKSIIT SAAPLISSPL KSVVSPVKSA VDVISSAKIT MASSLSSPVK QMPGHAEVAL VNGSISPLKY PSSSTLINGC KATATLQEKI SSATNSVSSV VSAATDTVEK VFSTTTAMPF SPLRSYVSAA PSAFQSLRTP SASALYTSLG SSISATTSSV TSSIITVPVY SVVNVLPEPA LKKLPDSNSF TKSAAALLSP IKTLTTETHP QPHFSRTSSP VKSSLFLAPS ALKLSTPSSL SSSQEILKDV AEMKEDLMRM TAILQTDVPE EKPFQPELPK EGRIDDEEPF KIVEKVKEDL VKVSEILKKD VCVDNKGSPK SPKSDKGHSP EDDWIEFSSE EIREARQQAA ASQSPSLPER VQVKAKAASE KDYNLTKVID YLTNDIGSSS LTNLKYKFED AKKDGEERQK RVLKPAIALQ EHKLKMPPAS MRTSTSEKEL CKMADSFFGT DTILESPDDF SQHDQDKSPL SDSGFETRSE KTPSAPQSAE STGPKPLFHE VPIPPVITET RTEVVHVIRS YDPSAGDVPQ TQPEEPVSPK PSPTFMELEP KPTTSSIKEK VKAFQMKASS EEDDHNRVLS KGMRVKEETH ITTTTRMVYH SPPGGEGASE RIEETMSVHD IMKAFQSGRD PSKELAGLFE HKSAVSPDVH KSAAETSAQH AEKDNQMKPK LERIIEVHIE KGNQAEPTEV IIRETKKHPE KEMYVYQKDL SRGDINLKDF LPEKHDAFPC SEEQGQQEEE ELTAEESLPS YLESSRVNTP VSQEEDSRPS SAQLISDDSY KTLKLLSQHS IEYHDDELSE LRGESYRFAE KMLLSEKLDV SHSDTEESVT DHAGPPSSEL QGSDKRSREK IATAPKKEIL SKIYKDVSEN GVGKVSKDEH FDKVTVLHYS GNVSSPKHAM WMRFTEDRLD RGREKLIYED RVDRTVKEAE EKLTEVSQFF RDKTEKLNDE LQSPEKKARP KNGKEYSSQS PTSSSPEKVL LTELLASNDE WVKARQHGPD GQGFPKAEEK APSLPSSPEK MVLSQQTEDS KSTVEAKGSI SQSKAPDGPQ SGFQLKQSKL SSIRLKFEQG THAKSKDMSQ EDRKSDGQSR IPVKKIQESK LPVYQVFARE KQQKAIDLPD ESVSVQKDFM VLKTKDEHAQ SNEIVVNDSG SDNVKKQRTE MSSKAMPDSF SEQQAKDLAC HITSDLATRG PWDKKVFRTW ESSGATNNKS QKEKLSHVLV HDVRENHIGH PESKSVDQKN EFMSVTERER KLLTNGSLSE IKEMTVKSPS KKVLYREYVV KEGDHPGGLL DQPSRRSESS AVSHIPVRVA DERRMLSSNI PDGFCEQSAF PKHELSQKLS QSSMSKETVE TQHFNSIEDE KVTYSEISKV SKHQSYVGLC PPLEETETSP TKSPDSLEFS PGKESPSSDV FDHSPIDGLE KLAPLAQTEG GKEIKTLPVY VSFVQVGKQY EKEIQQGGVK KIISQECKTV QETRGTFYTT RQQKQPPSPQ GSPEDDTLEQ VSFLDSSGKS PLTPETPSSE EVSYEFTSKT PDSLIAYIPG KPSPIPEVSE ESEEEEQAKS TSLKQTTVEE TAVEREMPND VSKDSNQRPK NNRVAYIEFP PPPPLDADQI ESDKKHHYLP EKEVDMIEVN LQDEHDKYQL AEPVIRVQPP SPVPPGADVS DSSDDESIYQ PVPVKKYTFK LKEVDDEQKE KPKASAEKAS NQKELESNGS GKDNEFGLGL DSPQNEIAQN GNNDQSITEC SIATTAEFSH DTDATEIDSL DGYDLQDEDD GLTESDSKLP IQAMEIKKDI WNTEGILKPA DRSFSQSKLE VIEEEGKVGP DEDKPPSKSS SSEKTPDKTD QKSGAQFFTL EGRHPDRSVF PDTYFSYKVD EEFATPFKTV ATKGLDFDPW SNNRGDDEVF DSKSREDETK PFGLAVEDRS PATTPDTTPA RTPTDESTPT SEPNPFPFHE GKMFEMTRSG AIDMSKRDFV EERLQFFQIG EHTSEGKSGD QGEGDKSMVT ATPQPQSGDT TVETNLERNV ETPTVEPNPS IPTSGECQEG TSSSGSLEKS AAATNTSKVD PKLRTPIKMG ISASTMTMKK EGPGEITDKI EAVMTSCQGL ENETITMISN TANSQMGVRP HEKHDFQKDN FNNNNNLDSS TIQTDNIMSN IVLTEHSAPT CTTEKDNPVK VSSGKKTGVL QGHCVRDKQK VLGEQQKTKE LIGIRQKSKL PIKATSPKDT FPPNHMSNTK ASKMKQVSQS EKTKALTTSS CVDVKSRIPV KNTHRDNIIA VRKACATQKQ GQPEKGKAKQ LPSKLPVKVR STCVTTTTTT ATTTTTTTTT TTTSCTVKVR KSQLKEVCKH SIEYFKGISG ETLKLVDRLS EEEKKMQSEL SDEEESTSRN TSLSETSRGG QPSVTTKSAR DKKTEAAPLK SKSEKAGSEK RSSRRTGPQS PCERTDIRMA IVADHLGLSW TELARELNFS VDEINQIRVE NPNSLISQSF MLLKKWVTRD GKNATTDALT SVLTKINRID IVTLLEGPIF DYGNISGTRS FADENNVFHD PVDGWQNETS SGNLESCAQA RRVTGGLLDR LDDSPDQCRD SITSYLKGEA GKFEANGSHT EITPEAKTKS YFPESQNDVG KQSTKETLKP KIHGSGHVEE PASPLAAYQK SLEETSKLII EETKPCVPVS MKKMSRTSPA DGKPRLSLHE EEGSSGSEQK QGEGFKVKTK KEIRHVEKKS HS //