ID ANR26_HUMAN Reviewed; 1710 AA. AC Q9UPS8; A6NH29; Q2TAZ3; Q6ZR14; Q9H1Q1; Q9NSK9; Q9NTD5; Q9NW69; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 12-SEP-2018, sequence version 4. DT 27-MAR-2024, entry version 171. DE RecName: Full=Ankyrin repeat domain-containing protein 26 {ECO:0000305}; GN Name=ANKRD26 {ECO:0000312|HGNC:HGNC:29186}; Synonyms=KIAA1074; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-20. RC TISSUE=Brain; RX PubMed=10470851; DOI=10.1093/dnares/6.3.197; RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:197-205(1999). 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., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1522 (ISOFORM 2), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-546 (ISOFORM 1), AND VARIANTS ARG-20; RP SER-606 DEL; ILE-1305 AND LEU-1514. RC TISSUE=Embryo, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1338-1710. RC TISSUE=Melanoma, and Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1546-1710. RC TISSUE=Lymph; 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). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [7] RP IDENTIFICATION. RX PubMed=16364570; DOI=10.1016/j.gene.2005.07.045; RA Hahn Y., Bera T.K., Pastan I.H., Lee B.; RT "Duplication and extensive remodeling shaped POTE family genes encoding RT proteins containing ankyrin repeat and coiled coil domains."; RL Gene 366:238-245(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP INVOLVEMENT IN THC2. RX PubMed=21211618; DOI=10.1016/j.ajhg.2010.12.006; RA Pippucci T., Savoia A., Perrotta S., Pujol-Moix N., Noris P., RA Castegnaro G., Pecci A., Gnan C., Punzo F., Marconi C., Gherardi S., RA Loffredo G., De Rocco D., Scianguetta S., Barozzi S., Magini P., Bozzi V., RA Dezzani L., Di Stazio M., Ferraro M., Perini G., Seri M., Balduini C.L.; RT "Mutations in the 5' UTR of ANKRD26, the ankirin repeat domain 26 gene, RT cause an autosomal-dominant form of inherited thrombocytopenia, THC2."; RL Am. J. Hum. Genet. 88:115-120(2011). RN [11] RP INTERACTION WITH TRIO; CCDC85B; GPS2 AND HMMR. RX PubMed=22666460; DOI=10.1371/journal.pone.0038130; RA Liu X.F., Bera T.K., Kahue C., Escobar T., Fei Z., Raciti G.A., Pastan I.; RT "ANKRD26 and its interacting partners TRIO, GPS2, HMMR and DIPA regulate RT adipogenesis in 3T3-L1 cells."; RL PLoS ONE 7:E38130-E38130(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15; SER-261; SER-489; RP SER-530 AND SER-631, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Acts as a regulator of adipogenesis. Involved in the CC regulation of the feeding behavior. {ECO:0000250|UniProtKB:Q811D2}. CC -!- SUBUNIT: Interacts with TRIO (PubMed:22666460). Interacts with GPS2 CC (PubMed:22666460). Interacts with CCDC85B (PubMed:22666460). Interacts CC with HMMR (PubMed:22666460). {ECO:0000269|PubMed:22666460}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UPS8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UPS8-2; Sequence=VSP_019434, VSP_019435; CC -!- DISEASE: Thrombocytopenia 2 (THC2) [MIM:188000]: A form of CC thrombocytopenia, a hematologic disorder defined by a decrease in the CC number of platelets in circulating blood, resulting in the potential CC for increased bleeding and decreased ability for clotting. CC {ECO:0000269|PubMed:21211618}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=BAA83026.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AB028997; BAA83026.2; ALT_INIT; mRNA. DR EMBL; AL162272; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK001137; BAA91516.1; -; mRNA. DR EMBL; AK128577; BAC87508.1; -; mRNA. DR EMBL; AL137351; CAB70706.1; -; mRNA. DR EMBL; AL162063; CAB82401.1; -; mRNA. DR EMBL; BC110646; AAI10647.1; -; mRNA. DR CCDS; CCDS41499.1; -. [Q9UPS8-1] DR PIR; T46425; T46425. DR PIR; T47167; T47167. DR RefSeq; NP_001242982.1; NM_001256053.1. DR RefSeq; NP_055730.2; NM_014915.2. [Q9UPS8-1] DR AlphaFoldDB; Q9UPS8; -. DR SMR; Q9UPS8; -. DR BioGRID; 116523; 120. DR IntAct; Q9UPS8; 38. DR MINT; Q9UPS8; -. DR STRING; 9606.ENSP00000365255; -. DR GlyGen; Q9UPS8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UPS8; -. DR PhosphoSitePlus; Q9UPS8; -. DR BioMuta; ANKRD26; -. DR DMDM; 109940217; -. DR EPD; Q9UPS8; -. DR jPOST; Q9UPS8; -. DR MassIVE; Q9UPS8; -. DR MaxQB; Q9UPS8; -. DR PaxDb; 9606-ENSP00000365255; -. DR PeptideAtlas; Q9UPS8; -. DR ProteomicsDB; 85431; -. [Q9UPS8-1] DR ProteomicsDB; 85432; -. [Q9UPS8-2] DR Pumba; Q9UPS8; -. DR Antibodypedia; 25959; 146 antibodies from 25 providers. DR DNASU; 22852; -. DR Ensembl; ENST00000376087.5; ENSP00000365255.4; ENSG00000107890.17. [Q9UPS8-1] DR GeneID; 22852; -. DR KEGG; hsa:22852; -. DR MANE-Select; ENST00000376087.5; ENSP00000365255.4; NM_014915.3; NP_055730.2. DR UCSC; uc009xku.2; human. [Q9UPS8-1] DR AGR; HGNC:29186; -. DR CTD; 22852; -. DR DisGeNET; 22852; -. DR GeneCards; ANKRD26; -. DR GeneReviews; ANKRD26; -. DR HGNC; HGNC:29186; ANKRD26. DR HPA; ENSG00000107890; Low tissue specificity. DR MalaCards; ANKRD26; -. DR MIM; 188000; phenotype. DR MIM; 610855; gene. DR neXtProt; NX_Q9UPS8; -. DR OpenTargets; ENSG00000107890; -. DR Orphanet; 168629; Autosomal thrombocytopenia with normal platelets. DR Orphanet; 71290; Familial platelet disorder with associated myeloid malignancy. DR PharmGKB; PA134926710; -. DR VEuPathDB; HostDB:ENSG00000107890; -. DR eggNOG; ENOG502QR0R; Eukaryota. DR GeneTree; ENSGT00940000162459; -. DR HOGENOM; CLU_001111_0_0_1; -. DR InParanoid; Q9UPS8; -. DR OMA; QCQMKEV; -. DR OrthoDB; 2385613at2759; -. DR PhylomeDB; Q9UPS8; -. DR TreeFam; TF333496; -. DR PathwayCommons; Q9UPS8; -. DR Reactome; R-HSA-9696264; RND3 GTPase cycle. DR Reactome; R-HSA-9696270; RND2 GTPase cycle. DR Reactome; R-HSA-9696273; RND1 GTPase cycle. DR SignaLink; Q9UPS8; -. DR SIGNOR; Q9UPS8; -. DR BioGRID-ORCS; 22852; 8 hits in 1160 CRISPR screens. DR ChiTaRS; ANKRD26; human. DR GeneWiki; ANKRD26; -. DR GenomeRNAi; 22852; -. DR Pharos; Q9UPS8; Tbio. DR PRO; PR:Q9UPS8; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9UPS8; Protein. DR Bgee; ENSG00000107890; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 126 other cell types or tissues. DR ExpressionAtlas; Q9UPS8; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR039497; CC144C-like_CC_dom. DR InterPro; IPR021885; DUF3496. DR PANTHER; PTHR24147; ANKYRIN REPEAT DOMAIN 36-RELATED; 1. DR PANTHER; PTHR24147:SF60; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 26-RELATED; 1. DR Pfam; PF00023; Ank; 2. DR Pfam; PF12796; Ank_2; 1. DR Pfam; PF14915; CCDC144C; 1. DR Pfam; PF12001; DUF3496; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 4. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR SUPFAM; SSF57997; Tropomyosin; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 4. DR Genevisible; Q9UPS8; HS. PE 1: Evidence at protein level; KW Alternative splicing; ANK repeat; Coiled coil; Phosphoprotein; KW Reference proteome; Repeat. FT CHAIN 1..1710 FT /note="Ankyrin repeat domain-containing protein 26" FT /id="PRO_0000240843" FT REPEAT 45..75 FT /note="ANK 1" FT REPEAT 79..108 FT /note="ANK 2" FT REPEAT 112..141 FT /note="ANK 3" FT REPEAT 145..174 FT /note="ANK 4" FT REPEAT 178..207 FT /note="ANK 5" FT REGION 1..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 222..274 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 504..630 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 650..698 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 892..912 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 529..566 FT /evidence="ECO:0000255" FT COILED 743..873 FT /evidence="ECO:0000255" FT COILED 905..1472 FT /evidence="ECO:0000255" FT COILED 1517..1587 FT /evidence="ECO:0000255" FT COILED 1649..1674 FT /evidence="ECO:0000255" FT COMPBIAS 230..247 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 518..568 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 579..599 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 657..680 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 681..698 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q811D2" FT MOD_RES 261 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 489 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 530 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 631 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..443 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_019434" FT VAR_SEQ 444..545 FT /note="KEKNIGNEQAEDVFYIPSCMSGSRNFKMAKLEDTRNVGMPVAHMESPERYLH FT LKPTIEMKDSVPNKAGGMKDVQTSKAAEHDLEVASEEEQEREGSENNQPQ -> MNHMF FT HIKRHSISAGTDAYKKTKPIQNLFQKPLYDHCSANNYKSMEPELENVRSSPPRGDRTSK FT VSLKEELQQDMQRFKNEIGMLKVEFQALEKEKVQLQKE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_019435" FT VARIANT 20 FT /note="Q -> R (in dbSNP:rs7897309)" FT /evidence="ECO:0000269|PubMed:10470851, FT ECO:0000269|PubMed:14702039" FT /id="VAR_026833" FT VARIANT 425 FT /note="I -> V (in dbSNP:rs12359281)" FT /id="VAR_055513" FT VARIANT 606 FT /note="Missing (in dbSNP:rs564681878)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_080646" FT VARIANT 1220 FT /note="V -> L (in dbSNP:rs12572862)" FT /id="VAR_055514" FT VARIANT 1305 FT /note="V -> I (in dbSNP:rs10829163)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_026834" FT VARIANT 1514 FT /note="F -> L (in dbSNP:rs2274741)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_026835" FT CONFLICT 1347 FT /note="D -> G (in Ref. 3; BAC87508)" FT /evidence="ECO:0000305" FT CONFLICT 1517..1523 FT /note="NNFASMK -> KQDLPDS (in Ref. 3; BAC87508)" FT /evidence="ECO:0000305" SQ SEQUENCE 1710 AA; 196411 MW; 01CBF9BADB894872 CRC64; MKKIFSKKGE SPLGSFARRQ RSSAGGGGEP GEGAYSQPGY HVRDRDLGKI HKAASAGNVA KVQQILLLRK NGLNDRDKMN RTALHLACAN GHPEVVTLLV DRKCQLNVCD NENRTALMKA VQCQEEKCAT ILLEHGADPN LADVHGNTAL HYAVYNEDIS VATKLLLYDA NIEAKNKDDL TPLLLAVSGK KQQMVEFLIK KKANVNAVDK LESSHQLISE YKEERIPKHS SQNSNSVDES SEDSLSRLSG KPGVDDSWPT SDDEDLNFDT KNVPKPSLAK LMTASQQSRK NLEATYGTVR TGNRTLFEDR DSDSQDEVVV ESLPTTSIKV QCFSHPTYQS PDLLPKPSHK SLANPGLMKE EPTKPGIAKK ENGIDIIESA PLEQTNNDNL TYVDEVHKNN RSDMMSALGL GQEEDIESPW DSESISENFP QKYVDPLAGA ADGKEKNIGN EQAEDVFYIP SCMSGSRNFK MAKLEDTRNV GMPVAHMESP ERYLHLKPTI EMKDSVPNKA GGMKDVQTSK AAEHDLEVAS EEEQEREGSE NNQPQVEEER KKHRNNEMEV SANIHDGATD DAEDDDDDDG LIQKRKSGET DHQQFPRKEN KEYASSGPAL QMKEVKSTEK EKRTSKESVN SPVFGKASLL TGGLLQVDDD SSLSEIDEDE GRPTKKTSNE KNKVKNQIQS MDDVDDLTQS SETASEDCEL PHSSYKNFML LIEQLGMECK DSVSLLKIQD AALSCERLLE LKKNHCELLT VKIKKMEDKV NVLQRELSET KEIKSQLEHQ KVEWERELCS LRFSLNQEEE KRRNADTLYE KIREQLRRKE EQYRKEVEVK QQLELSLQTL EMELRTVKSN LNQVVQERND AQRQLSREQN ARMLQDGILT NHLSKQKEIE MAQKKMNSEN SHSHEEEKDL SHKNSMLQEE IAMLRLEIDT IKNQNQEKEK KCFEDLKIVK EKNEDLQKTI KQNEETLTQT ISQYNGRLSV LTAENAMLNS KLENEKQSKE RLEAEVESYH SRLAAAIHDR DQSETSKREL ELAFQRARDE CSRLQDKMNF DVSNLKDNNE ILSQQLFKTE SKLNSLEIEF HHTRDALREK TLGLERVQKD LSQTQCQMKE MEQKYQNEQV KVNKYIGKQE SVEERLSQLQ SENMLLRQQL DDAHNKADNK EKTVINIQDQ FHAIVQKLQA ESEKQSLLLE ERNKELISEC NHLKERQYQY ENEKAEREVV VRQLQQELAD TLKKQSMSEA SLEVTSRYRI NLEDETQDLK KKLGQIRNQL QEAQDRHTEA VRCAEKMQDH KQKLEKDNAK LKVTVKKQMD KIEELQKNLL NANLSEDEKE QLKKLMELKQ SLECNLDQEM KKNVELEREI TGFKNLLKMT RKKLNEYENG EFSFHGDLKT SQFEMDIQIN KLKHKIDDLT AELETAGSKC LHLDTKNQIL QEELLSMKTV QKKCEKLQKN KKKLEQEVIN LRSHIERNMV ELGQVKQYKQ EIEERARQEI AEKLKEVNLF LQAQAASQEN LEQFRENNFA SMKSQMELRI KDLESELSKI KTSQEDFNKT ELEKYKQLYL EELKVRKSLS SKLTKTNERL AEVNTKLLVE KQQSRSLFTT LTTRPVMEPP CVGNLNNSLD LNRKLIPREN LVISTSNPRA SNNSMENYLS KMQQELEKNI TRELKEAAAE LESGSIASPL GSTDESNLNQ DLVWKASREY VQVLKKNYMI //