ID MYO9A_HUMAN Reviewed; 2548 AA. AC B2RTY4; B0I1T5; Q14787; Q3YLD7; Q3YLD8; Q6P986; Q9H8T5; Q9NTG2; AC Q9NUY2; Q9UEP3; Q9UNJ2; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 05-OCT-2010, entry version 30. DE RecName: Full=Myosin-IXa; DE AltName: Full=Unconventional myosin-9a; GN Name=MYO9A; Synonyms=MYR7; 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] (ISOFORMS 1 AND 5), TISSUE SPECIFICITY, AND RP VARIANTS GLN-85; ASP-168; PRO-211; GLN-946; GLU-1193; PRO-1362 AND RP CYS-1834. RX MEDLINE=99339979; PubMed=10409426; DOI=10.1006/geno.1999.5867; RA Gorman S.W., Haider N.B., Grieshammer U., Swiderski R.E., Kim E., RA Welch J.W., Searby C., Leng S., Carmi R., Sheffield V.C., Duhl D.M.; RT "The cloning and developmental expression of unconventional myosin IXA RT (MYO9A) a gene in the Bardet-Biedl syndrome (BBS4) region at RT chromosome 15q22-q23."; RL Genomics 59:150-160(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., RA Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human RT chromosome 15."; RL Nature 440:671-675(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-1193. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND RP VARIANTS LYS-37 AND GLU-1193. RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-774 (ISOFORMS 1/4). RX PubMed=9819351; RA Chieregatti E., Gaertner A., Stoeffler H.-E., Baehler M.; RT "Myr 7 is a novel myosin IX-RhoGAP expressed in rat brain."; RL J. Cell Sci. 111:3597-3608(1998). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-2548 (ISOFORM 1), AND RP VARIANT GLU-1193. RC TISSUE=Brain; RA Yamakawa H., Kikuno R.F., Nagase T., Ohara O.; RT "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free RT recombination: preparation of full-length cDNA clones encoding motor RT proteins."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 234-322 (ISOFORMS 1/2/3/4). RX MEDLINE=94294418; PubMed=8022818; DOI=10.1073/pnas.91.14.6549; RA Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.; RT "Identification and overlapping expression of multiple unconventional RT myosin genes in vertebrate cell types."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6549-6553(1994). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 292-445 (ISOFORMS 1/2/3/4/5). RX PubMed=16204458; DOI=10.1093/nar/gki870; RA Hiller M., Huse K., Platzer M., Backofen R.; RT "Non-EST based prediction of exon skipping and intron retention events RT using Pfam information."; RL Nucleic Acids Res. 33:5611-5621(2005). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1223-2548 (ISOFORM 4). RC TISSUE=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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1457-1981 (ISOFORM 4), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1984-2548 (ISOFORMS RP 1/2/4/5). RC TISSUE=Ovary, and Placenta; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase CC activity. Unconventional myosins serve in intracellular movements. CC Regulates Rho activity in neurons, has a role in the regulation of CC neuronal morphology and function (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein CC (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=B2RTY4-1; Sequence=Displayed; CC Name=2; CC IsoId=B2RTY4-2; Sequence=VSP_035157; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=B2RTY4-3; Sequence=VSP_035158, VSP_035159; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=B2RTY4-4; Sequence=VSP_035160; CC Name=5; CC IsoId=B2RTY4-5; Sequence=VSP_035156; CC Note=Lacks the ATP-binding domain which suggests that it cannot CC interact with actin; CC -!- TISSUE SPECIFICITY: Found to be expressed in testis and placenta, CC and at lower levels in all the examined tissues with the exception CC of liver. Isoform 5 was found in leukocytes but not in brain, CC retina or testis. CC -!- SIMILARITY: Contains 5 IQ domains. CC -!- SIMILARITY: Contains 2 myosin head-like domains. CC -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers. CC -!- SIMILARITY: Contains 1 Ras-associating domain. CC -!- SIMILARITY: Contains 1 Rho-GAP domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91979.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAB14517.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF117888; AAD49195.1; -; mRNA. DR EMBL; AC020779; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC022872; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090454; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104938; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471082; EAW77880.1; -; Genomic_DNA. DR EMBL; BC060886; AAH60886.1; -; mRNA. DR EMBL; BC140869; AAI40870.1; -; mRNA. DR EMBL; AJ001714; CAA04947.1; -; mRNA. DR EMBL; AB290183; BAG06737.1; -; mRNA. DR EMBL; L29148; AAA20911.1; -; mRNA. DR EMBL; DQ088983; AAZ85978.1; -; mRNA. DR EMBL; DQ088984; AAZ85979.1; -; mRNA. DR EMBL; AL137287; CAB70679.1; -; mRNA. DR EMBL; AK001923; BAA91979.1; ALT_INIT; mRNA. DR EMBL; AK023306; BAB14517.1; ALT_INIT; mRNA. DR IPI; IPI00018057; -. DR IPI; IPI00160131; -. DR IPI; IPI00902852; -. DR IPI; IPI00902943; -. DR IPI; IPI00953559; -. DR PIR; E59435; E59435. DR PIR; I61699; I61699. DR PIR; T46354; T46354. DR RefSeq; NP_008832.2; -. DR UniGene; Hs.546268; -. DR ProteinModelPortal; B2RTY4; -. DR SMR; B2RTY4; 4-112, 143-1045, 1996-2246. DR PeptideAtlas; Q14787; -. DR Ensembl; ENST00000356056; ENSP00000348349; ENSG00000066933. DR GeneID; 4649; -. DR KEGG; hsa:4649; -. DR CTD; 4649; -. DR GeneCards; GC15M072114; -. DR H-InvDB; HIX0012401; -. DR HGNC; HGNC:7608; MYO9A. DR MIM; 604875; gene. DR PharmGKB; PA31413; -. DR HOVERGEN; HBG108165; -. DR InParanoid; B2RTY4; -. DR Reactome; REACT_11044; Signaling by Rho GTPases. DR Bgee; B2RTY4; -. DR Genevestigator; B2RTY4; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0016461; C:unconventional myosin complex; NAS:UniProtKB. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd. DR InterPro; IPR000159; Ras-assoc. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP. DR Gene3D; G3DSA:1.10.555.10; RhoGAP; 1. DR Pfam; PF00612; IQ; 4. DR Pfam; PF00063; Myosin_head; 2. DR Pfam; PF00788; RA; 1. DR Pfam; PF00620; RhoGAP; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR SMART; SM00109; C1; 1. DR SMART; SM00015; IQ; 5. DR SMART; SM00242; MYSc; 1. DR SMART; SM00314; RA; 1. DR SMART; SM00324; RhoGAP; 1. DR SUPFAM; SSF48350; Rho_GAP; 1. DR PROSITE; PS50096; IQ; 4. DR PROSITE; PS50200; RA; 1. DR PROSITE; PS50238; RHOGAP; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 1. PE 1: Evidence at protein level; KW Actin-binding; Alternative splicing; ATP-binding; Coiled coil; KW Complete proteome; GTPase activation; Membrane; Metal-binding; KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; KW Polymorphism; Repeat; Transmembrane; Transmembrane helix; Zinc; KW Zinc-finger. FT CHAIN 1 2548 Myosin-IXa. FT /FTId=PRO_0000348440. FT TRANSMEM 175 195 Helical; (Potential). FT DOMAIN 14 112 Ras-associating. FT DOMAIN 148 690 Myosin head-like 1. FT DOMAIN 884 1005 Myosin head-like 2. FT DOMAIN 1021 1041 IQ 1. FT DOMAIN 1042 1071 IQ 2. FT DOMAIN 1074 1103 IQ 3. FT DOMAIN 1115 1144 IQ 4. FT DOMAIN 1138 1167 IQ 5. FT DOMAIN 2063 2251 Rho-GAP. FT NP_BIND 239 246 ATP (Potential). FT ZN_FING 1999 2048 Phorbol-ester/DAG-type 1. FT ZN_FING 2068 2119 Phorbol-ester/DAG-type 2. FT REGION 907 918 Actin-binding (By similarity). FT REGION 1021 1162 Neck or regulatory domain. FT REGION 1163 2511 Tail. FT COILED 1264 1291 Potential. FT COILED 1486 1532 Potential. FT COILED 2315 2358 Potential. FT MOD_RES 770 770 Phosphothreonine (By similarity). FT MOD_RES 1258 1258 Phosphoserine (By similarity). FT MOD_RES 1829 1829 Phosphoserine (By similarity). FT VAR_SEQ 45 280 Missing (in isoform 5). FT /FTId=VSP_035156. FT VAR_SEQ 367 385 Missing (in isoform 2). FT /FTId=VSP_035157. FT VAR_SEQ 729 729 H -> K (in isoform 3). FT /FTId=VSP_035158. FT VAR_SEQ 730 2548 Missing (in isoform 3). FT /FTId=VSP_035159. FT VAR_SEQ 1714 1714 E -> EVARPAHKKKARMARTRSDFLTRGTFADGEGDTEED FT DYDDIIEPLLSLDQASHCELGPAPSLGQASHSDSEM (in FT isoform 4). FT /FTId=VSP_035160. FT VARIANT 37 37 R -> K (in dbSNP:rs17855105). FT /FTId=VAR_046165. FT VARIANT 85 85 R -> Q. FT /FTId=VAR_046166. FT VARIANT 161 161 T -> I (in dbSNP:rs2929516). FT /FTId=VAR_046167. FT VARIANT 168 168 N -> D. FT /FTId=VAR_046168. FT VARIANT 211 211 L -> P. FT /FTId=VAR_046169. FT VARIANT 825 825 A -> V (in dbSNP:rs11637562). FT /FTId=VAR_056189. FT VARIANT 946 946 R -> Q. FT /FTId=VAR_046170. FT VARIANT 1193 1193 G -> E (in dbSNP:rs2415129). FT /FTId=VAR_046171. FT VARIANT 1362 1362 S -> P (in dbSNP:rs55738821). FT /FTId=VAR_046172. FT VARIANT 1476 1476 P -> R (in dbSNP:rs16956375). FT /FTId=VAR_046173. FT VARIANT 1795 1795 H -> Y (in dbSNP:rs16956367). FT /FTId=VAR_046174. FT VARIANT 1805 1805 H -> Q (in dbSNP:rs2306575). FT /FTId=VAR_046175. FT VARIANT 1834 1834 R -> C. FT /FTId=VAR_046176. FT VARIANT 2390 2390 I -> V (in dbSNP:rs2291280). FT /FTId=VAR_046177. FT CONFLICT 88 88 L -> R (in Ref. 5; CAA04947). FT CONFLICT 94 94 L -> Q (in Ref. 5; CAA04947). FT CONFLICT 104 104 R -> H (in Ref. 5; CAA04947). FT CONFLICT 206 206 H -> R (in Ref. 5; CAA04947). FT CONFLICT 394 394 D -> N (in Ref. 5; CAA04947). FT CONFLICT 424 424 S -> P (in Ref. 5; CAA04947). FT CONFLICT 504 504 S -> C (in Ref. 5; CAA04947). FT CONFLICT 573 573 E -> D (in Ref. 5; CAA04947). FT CONFLICT 595 595 C -> Y (in Ref. 5; CAA04947). FT CONFLICT 694 694 I -> M (in Ref. 5; CAA04947). FT CONFLICT 705 705 L -> I (in Ref. 5; CAA04947). FT CONFLICT 1591 1591 S -> P (in Ref. 10; BAB14517). SQ SEQUENCE 2548 AA; 292706 MW; 867835BD2B841C84 CRC64; MNINDGGRRR FEDNEHTLRI YPGAISEGTI YCPIPARKNS TAAEVIESLI NKLHLDKTKC YVLAEVKEFG GEEWILNPTD CPVQRMMLWP RMALENRLSG EDYRFLLREK NLDGSIHYGS LQSWLRVTEE RRRMMERGFL PQPQQKDFDD LCSLPDLNEK TLLENLRNRF KHEKIYTYVG SILIVINPFK FLPIYNPKYV KMYDNHQLGK LEPHIYAVAD VAYHAMLQRK KNQCIVISGE SGSGKTQSTN FLIHHLTALS QKGFASGVEQ IILGAGPVLE AFGNAKTAHN NNSSRFGKFI QVNYQETGTV LGAYVEKYLL EKSRLVYQEH NERNYHVFYY LLAGASEDER SAFHLKQPEE YHYLNQITKK PLRQSWDDYC YDSEPDCFTV EGEDLRHDFE RLQLAMEMVG FLPKTRRQIF SLLSAILHLG NICYKKKTYR DDSIDICNPE VLPIVSELLE VKEEMLFEAL VTRKTVTVGE KLILPYKLAE AVTVRNSMAK SLYSALFDWI VFRINHALLN SKDLEHNTKT LSIGVLDIFG FEDYENNSFE QFCINFANER LQHYFNQHIF KLEQEEYRTE GISWHNIDYI DNTCCINLIS KKPTGLLHLL DEESNFPQAT NQTLLDKFKH QHEDNSYIEF PAVMEPAFII KHYAGKVKYG VKDFREKNTD HMRPDIVALL RSSKNAFISG MIGIDPVAVF RWAILRAFFR AMVAFREAGK RNIHRKTGHD DTAPCAILKS MDSFSFLQHP VHQRSLEILQ RCKEEKYSIT RKNPRTPLSD LQGMNALNEK NQHDTFDIAW NGRTGIRQSR LSSGTSLLDK DGIFANSTSS KLLERAHGIL TRNKNFKSKP ALPKHLLEVN SLKHLTRLTL QDRITKSLLH LHKKKKPPSI SAQFQASLSK LMETLGQAEP YFVKCIRSNA EKLPLRFSDV LVLRQLRYTG MLETVRIRQS GYSSKYSFQD FVSHFHVLLP RNIIPSKFNI QDFFRKINLN PDNYQVGKTM VFLKEQERQH LQDLLHQEVL RRIILLQRWF RVLLCRQHFL HLRQASVIIQ RFWRNYLNQK QVRDAAVQKD AFVMASAAAL LQASWRAHLE RQRYLELRAA AIVIQQKWRD YYRRRHMAAI CIQARWKAYR ESKRYQEQRK KIILLQSTCR GFRARQRFKA LKEQRLRETK PEVGLVNIKG YGSLEIQGSD PSGWEDCSFD NRIKAIEECK SVIESNRISR ESSVDCLKES PNKQQERAQS QSGVDLQEDV LVRERPRSLE DLHQKKVGRA KRESRRMREL EQAIFSLELL KVRSLGGISP SEDRRWSTEL VPEGLQSPRG TPDSESSQGS LELLSYEESQ KSKLESVISD EGDLQFPSPK ISSSPKFDSR DNALSASNET SSAEHLKDGT MKEMVVCSSE SITCKPQLKD SFISNSLPTF FYIPQQDPLK TNSQLDTSIQ RNKLLENEDT AGEALTLDIN RETRRYHCSG KDQIVPSLNT ESSNPVLKKL EKLNTEKEER QKQLQQQNEK EMMEQIRQQT DILEKERKAF KTIEKPRIGE CLVAPSSYQS KQRVERPSSL LSLNTSNKGE LNVLGSLSLK DAALAQKDSS SAHLPPKDRP VTVFFERKGS PCQSSTVKEL SKTDRMGTQL NVACKLSNNR ISKREHFRPT QSYSHNSDDL SREGNARPIF FTPKDNMSIP LVSKEALNSK NPQLHKEDEP AWKPVKLAGP GQRETSQRFS SVDEQAKLHK TMSQGEITKL AVRQKASDSD IRPQRAKMRF WAKGKQGEKK TTRVKPTTQS EVSPLFAGTD VIPAHQFPDE LAAYHPTPPL SPELPGSCRK EFKENKEPSP KAKRKRSVKI SNVALDSMHW QNDSVQIIAS VSDLKSMDEF LLKKVNDLDN EDSKKDTLVD VVFKKALKEF RQNIFSFYSS ALAMDDGKSI RYKDLYALFE QILEKTMRLE QRDSLGESPV RVWVNTFKVF LDEYMNEFKT SDCTATKVPK TERKKRRKKE TDLVEEHNGH IFKATQYSIP TYCEYCSSLI WIMDRASVCK LCKYACHKKC CLKTTAKCSK KYDPELSSRQ FGVELSRLTS EDRTVPLVVE KLINYIEMHG LYTEGIYRKS GSTNKIKELR QGLDTDAESV NLDDYNIHVI ASVFKQWLRD LPNPLMTFEL YEEFLRAMGL QERKETIRGV YSVIDQLSRT HLNTLERLIF HLVRIALQED TNRMSANALA IVFAPCILRC PDTTDPLQSV QDISKTTTCV ELIVVEQMNK YKARLKDISS LEFAENKAKT RLSLIRRSMG KGRIRRGNYP GPSSPVVVRL PSVSDVSEET LTSEAAMETD ITEQQQAAMQ QEERVLTEQI ENLQKEKEEL TFEMLVLEPR ASDDETLESE ASIGTADSSE NLNMESEYAI SEKSERSLAL SSLKTAGKSE PSSKLRKQLK KQQDSLDVVD SSVSSLCLSN TASSHGTRKL FQIYSKSPFY RAASGNEALG MEGPLGQTKF LEDKPQFISR GTFNPEKGKQ KLKNVKNSPQ KTKETPEGTV MSGRRKTVDP DCTSNQQLAL FGNNEFMV //