ID PKHG6_HUMAN Reviewed; 790 AA. AC Q3KR16; Q3SWR1; Q8N1P1; Q8WYY1; Q9H8F4; Q9NVK9; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 03-MAY-2011, sequence version 3. DT 24-JAN-2024, entry version 149. DE RecName: Full=Pleckstrin homology domain-containing family G member 6; DE Short=PH domain-containing family G member 6; DE AltName: Full=Myosin-interacting guanine nucleotide exchange factor; DE Short=MyoGEF; GN Name=PLEKHG6; 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] (ISOFORMS 1 AND 2), AND VARIANT RP THR-35. RC TISSUE=Tongue; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-35. 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 FUNCTION, INTERACTION WITH MYH10, AND SUBCELLULAR LOCATION. RX PubMed=16721066; DOI=10.4161/cc.5.11.2815; RA Wu D., Asiedu M., Adelstein R.S., Wei Q.; RT "A novel guanine nucleotide exchange factor MyoGEF is required for RT cytokinesis."; RL Cell Cycle 5:1234-1239(2006). RN [7] RP FUNCTION, INTERACTION WITH ELMO1 AND EZR, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF ASN-351. RX PubMed=17881735; DOI=10.1091/mbc.e06-12-1144; RA D'Angelo R., Aresta S., Blangy A., Del Maestro L., Louvard D., Arpin M.; RT "Interaction of ezrin with the novel guanine nucleotide exchange factor RT PLEKHG6 promotes RhoG-dependent apical cytoskeleton rearrangements in RT epithelial cells."; RL Mol. Biol. Cell 18:4780-4793(2007). RN [8] RP INTERACTION WITH CSPP1. RX PubMed=19129481; DOI=10.1091/mbc.e08-01-0001; RA Asiedu M., Wu D., Matsumura F., Wei Q.; RT "Centrosome/spindle pole-associated protein regulates cytokinesis via RT promoting the recruitment of MyoGEF to the central spindle."; RL Mol. Biol. Cell 20:1428-1440(2009). CC -!- FUNCTION: Guanine nucleotide exchange factor activating the small CC GTPase RHOA, which, in turn, induces myosin filament formation. Also CC activates RHOG. Does not activate RAC1, or to a much lower extent than CC RHOA and RHOG. Part of a functional unit, involving PLEKHG6, MYH10 and CC RHOA, at the cleavage furrow to advance furrow ingression during CC cytokinesis. In epithelial cells, required for the formation of CC microvilli and membrane ruffles on the apical pole. Along with EZR, CC required for normal macropinocytosis. {ECO:0000269|PubMed:16721066, CC ECO:0000269|PubMed:17881735}. CC -!- SUBUNIT: Interacts with MYH10. Interacts with ELMO1 and EZR (in an open CC conformation). Interacts with CSPP1. {ECO:0000269|PubMed:16721066, CC ECO:0000269|PubMed:17881735, ECO:0000269|PubMed:19129481}. CC -!- INTERACTION: CC Q3KR16; Q53EZ4: CEP55; NbExp=8; IntAct=EBI-10240979, EBI-747776; CC -!- SUBCELLULAR LOCATION: Cell projection, microvillus CC {ECO:0000269|PubMed:17881735}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:16721066}. Cytoplasm, cytoskeleton, spindle pole CC {ECO:0000269|PubMed:16721066}. Cleavage furrow CC {ECO:0000269|PubMed:16721066}. Note=During mitosis, localizes to the CC spindle pole, central spindle and cleavage furrow (PubMed:16721066). In CC epithelial cells, recruited to the apical membrane by EZR where it CC participates in macropinocytosis (PubMed:17881735). CC {ECO:0000269|PubMed:16721066, ECO:0000269|PubMed:17881735}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q3KR16-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3KR16-2; Sequence=VSP_028857; CC Name=3; CC IsoId=Q3KR16-3; Sequence=VSP_028856, VSP_028858; CC -!- TISSUE SPECIFICITY: Highest expression in the placenta. Low levels in CC small intestine, lung, liver, kidney, thymus and heart. 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; AK001527; BAA91741.1; -; mRNA. DR EMBL; AK095373; BAC04539.1; -; mRNA. DR EMBL; AF289613; AAL55797.1; -; mRNA. DR EMBL; BC104751; AAI04752.1; -; mRNA. DR EMBL; BC105961; AAI05962.1; -; mRNA. DR EMBL; BC109095; AAI09096.1; -; mRNA. DR EMBL; AC006057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471116; EAW88809.1; -; Genomic_DNA. DR CCDS; CCDS8541.1; -. [Q3KR16-1] DR RefSeq; NP_001138328.1; NM_001144856.1. [Q3KR16-1] DR RefSeq; NP_001138329.1; NM_001144857.1. DR RefSeq; NP_060643.2; NM_018173.3. [Q3KR16-1] DR RefSeq; XP_005253761.1; XM_005253704.4. DR AlphaFoldDB; Q3KR16; -. DR SMR; Q3KR16; -. DR BioGRID; 120497; 45. DR IntAct; Q3KR16; 32. DR STRING; 9606.ENSP00000380185; -. DR GlyGen; Q3KR16; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q3KR16; -. DR PhosphoSitePlus; Q3KR16; -. DR BioMuta; PLEKHG6; -. DR DMDM; 332278231; -. DR jPOST; Q3KR16; -. DR MassIVE; Q3KR16; -. DR PaxDb; 9606-ENSP00000380185; -. DR PeptideAtlas; Q3KR16; -. DR ProteomicsDB; 61734; -. [Q3KR16-1] DR ProteomicsDB; 61735; -. [Q3KR16-2] DR ProteomicsDB; 61736; -. [Q3KR16-3] DR Antibodypedia; 49879; 150 antibodies from 21 providers. DR DNASU; 55200; -. DR Ensembl; ENST00000011684.11; ENSP00000011684.7; ENSG00000008323.16. [Q3KR16-1] DR Ensembl; ENST00000304581.8; ENSP00000304640.8; ENSG00000008323.16. [Q3KR16-3] DR Ensembl; ENST00000396988.7; ENSP00000380185.3; ENSG00000008323.16. [Q3KR16-1] DR Ensembl; ENST00000449001.6; ENSP00000393194.2; ENSG00000008323.16. [Q3KR16-2] DR Ensembl; ENST00000684764.1; ENSP00000506982.1; ENSG00000008323.16. [Q3KR16-1] DR GeneID; 55200; -. DR KEGG; hsa:55200; -. DR MANE-Select; ENST00000684764.1; ENSP00000506982.1; NM_001384598.1; NP_001371527.1. DR UCSC; uc001qnr.4; human. [Q3KR16-1] DR AGR; HGNC:25562; -. DR CTD; 55200; -. DR DisGeNET; 55200; -. DR GeneCards; PLEKHG6; -. DR HGNC; HGNC:25562; PLEKHG6. DR HPA; ENSG00000008323; Tissue enhanced (esophagus, intestine). DR MIM; 611743; gene. DR neXtProt; NX_Q3KR16; -. DR OpenTargets; ENSG00000008323; -. DR PharmGKB; PA142671165; -. DR VEuPathDB; HostDB:ENSG00000008323; -. DR eggNOG; KOG3521; Eukaryota. DR GeneTree; ENSGT00940000161250; -. DR HOGENOM; CLU_021968_1_0_1; -. DR InParanoid; Q3KR16; -. DR OMA; SPWESSE; -. DR OrthoDB; 2881273at2759; -. DR PhylomeDB; Q3KR16; -. DR TreeFam; TF316755; -. DR PathwayCommons; Q3KR16; -. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR SignaLink; Q3KR16; -. DR SIGNOR; Q3KR16; -. DR BioGRID-ORCS; 55200; 28 hits in 1151 CRISPR screens. DR ChiTaRS; PLEKHG6; human. DR GenomeRNAi; 55200; -. DR Pharos; Q3KR16; Tbio. DR PRO; PR:Q3KR16; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q3KR16; Protein. DR Bgee; ENSG00000008323; Expressed in mucosa of transverse colon and 126 other cell types or tissues. DR ExpressionAtlas; Q3KR16; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. DR CDD; cd13244; PH_PLEKHG5_G6; 1. DR CDD; cd00160; RhoGEF; 1. DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR035899; DBL_dom_sf. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR042918; PLEKHG6. DR PANTHER; PTHR47671; PLECKSTRIN DOMAIN-CONTAINING FAMILY G MEMBER 6; 1. DR PANTHER; PTHR47671:SF1; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY G MEMBER 6; 1. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00325; RhoGEF; 1. DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR Genevisible; Q3KR16; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell projection; Cytoplasm; Cytoskeleton; KW GTPase activation; Reference proteome. FT CHAIN 1..790 FT /note="Pleckstrin homology domain-containing family G FT member 6" FT /id="PRO_0000307912" FT DOMAIN 161..353 FT /note="DH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" FT DOMAIN 409..509 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 63..91 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 529..677 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 690..730 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 748..790 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 73..87 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 539..559 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 590..606 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 748..766 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..470 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15498874" FT /id="VSP_028856" FT VAR_SEQ 1..46 FT /note="MKAFGPPHEGPLQGLVASRIETYGGRHRASAQSTAGRLYPRGYPVL -> MG FT CRLHAPGEKAAH (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_028857" FT VAR_SEQ 471..508 FT /note="SFLLIHLTEFQCVSSALLVHCPSPTDRAQWLEKTQQAQ -> MCPREGGRAS FT TIHQKTEKAFGQLLCQPLGEPKIQHPLK (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15498874" FT /id="VSP_028858" FT VARIANT 35 FT /note="A -> T (in dbSNP:rs740842)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_036710" FT MUTAGEN 351 FT /note="N->A: Loss of exchange activity." FT /evidence="ECO:0000269|PubMed:17881735" FT CONFLICT 384 FT /note="E -> G (in Ref. 5; AAI04752)" FT /evidence="ECO:0000305" FT CONFLICT 459 FT /note="E -> D (in Ref. 1; BAA91741)" FT /evidence="ECO:0000305" SQ SEQUENCE 790 AA; 88960 MW; 34A2555DEF431EF4 CRC64; MKAFGPPHEG PLQGLVASRI ETYGGRHRAS AQSTAGRLYP RGYPVLDPSR RRLQQYVPFA RGSGQARGLS PMRLRDPEPE KRHGGHVGAG LLHSPKLKEL TKAHELEVRL HTFSMFGMPR LPPEDRRHWE IGEGGDSGLT IEKSWRELVP GHKEMSQELC HQQEALWELL TTELIYVRKL KIMTDLLAAG LLNLQRVGLL MEVSAETLFG NVPSLIRTHR SFWDEVLGPT LEETRASGQP LDPIGLQSGF LTFGQRFHPY VQYCLRVKQT MAYAREQQET NPLFHAFVQW CEKHKRSGRQ MLCDLLIKPH QRITKYPLLL HAVLKRSPEA RAQEALNAMI EAVESFLRHI NGQVRQGEEQ ESLAAAAQRI GPYEVLEPPS DEVEKNLRPF STLDLTSPML GVASEHTRQL LLEGPVRVKE GREGKLDVYL FLFSDVLLVT KPQRKADKAK VIRPPLMLEK LVCQPLRDPN SFLLIHLTEF QCVSSALLVH CPSPTDRAQW LEKTQQAQAA LQKLKAEEYV QQKRELLTLY RDQDRESPST RPSTPSLEGS QSSAEGRTPE FSTIIPHLVV TEDTDEDAPL VPDDTSDSGY GTLIPGTPTG SRSPLSRLRQ RALRRDPRLT FSTLELRDIP LRPHPPDPQA PQRRSAPELP EGILKGGSLP QEDPPTWSEE EDGASERGNV VVETLHRARL RGQLPSSPTH ADSAGESPWE SSGEEEEEGP LFLKAGHTSL RPMRAEDMLR EIREELASQR IEGAEEPRDS RPRKLTRAQL QRMRGPHIIQ LDTPLSASEV //