PKHG6_HUMAN
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 03-AUG-2022, entry version 141.
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.
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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; 44.
DR IntAct; Q3KR16; 32.
DR STRING; 9606.ENSP00000380185; -.
DR iPTMnet; Q3KR16; -.
DR PhosphoSitePlus; Q3KR16; -.
DR BioMuta; PLEKHG6; -.
DR DMDM; 332278231; -.
DR jPOST; Q3KR16; -.
DR MassIVE; Q3KR16; -.
DR PaxDb; Q3KR16; -.
DR PeptideAtlas; Q3KR16; -.
DR PRIDE; Q3KR16; -.
DR ProteomicsDB; 61734; -. [Q3KR16-1]
DR ProteomicsDB; 61735; -. [Q3KR16-2]
DR ProteomicsDB; 61736; -. [Q3KR16-3]
DR Antibodypedia; 49879; 141 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 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; 556467at2759; -.
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; 16 hits in 1072 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 125 other tissues.
DR ExpressionAtlas; Q3KR16; baseline and differential.
DR Genevisible; Q3KR16; HS.
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; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 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; PTHR47671; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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
