ID FGD4_HUMAN Reviewed; 766 AA. AC Q96M96; Q6ULS2; Q8TCP6; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 28-JUN-2023, entry version 178. DE RecName: Full=FYVE, RhoGEF and PH domain-containing protein 4; DE AltName: Full=Actin filament-binding protein frabin; DE AltName: Full=FGD1-related F-actin-binding protein; DE AltName: Full=Zinc finger FYVE domain-containing protein 6; GN Name=FGD4; Synonyms=FRABP, ZFYVE6; 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 [MRNA] (ISOFORM 2). RC TISSUE=Testis; RA Lu L., Huang X.Y., Xu M., Yin L.L., Li J.M., Zhou Z.M., Sha J.H.; RT "Cloning a new transcript of actin-filament binding protein frabin in RT testis."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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., 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 [4] RP FUNCTION. RX PubMed=15133042; DOI=10.1074/jbc.m401592200; RA Chen X.M., Splinter P.L., Tietz P.S., Huang B.Q., Billadeau D.D., RA LaRusso N.F.; RT "Phosphatidylinositol 3-kinase and frabin mediate Cryptosporidium parvum RT cellular invasion via activation of Cdc42."; RL J. Biol. Chem. 279:31671-31678(2004). RN [5] RP INVOLVEMENT IN CMT4H, VARIANTS CMT4H ARG-298 AND THR-298, TISSUE RP SPECIFICITY, AND ALTERNATIVE SPLICING. RX PubMed=17564959; DOI=10.1086/518428; RA Delague V., Jacquier A., Hamadouche T., Poitelon Y., Baudot C., RA Boccaccio I., Chouery E., Chaouch M., Kassouri N., Jabbour R., Grid D., RA Megarbane A., Haase G., Levy N.; RT "Mutations in FGD4 encoding the Rho GDP/GTP exchange factor FRABIN cause RT autosomal recessive Charcot-Marie-Tooth type 4H."; RL Am. J. Hum. Genet. 81:1-16(2007). RN [6] RP INVOLVEMENT IN CMT4H, AND VARIANT CMT4H ARG-298. RX PubMed=17564972; DOI=10.1086/518770; RA Stendel C., Roos A., Deconinck T., Pereira J., Castagner F., Niemann A., RA Kirschner J., Korinthenberg R., Ketelsen U.-P., Battaloglu E., Parman Y., RA Nicholson G., Ouvrier R., Seeger J., De Jonghe P., Weis J., Kruettgen A., RA Rudnik-Schoeneborn S., Bergmann C., Suter U., Zerres K., Timmerman V., RA Relvas J.B., Senderek J.; RT "Peripheral nerve demyelination caused by a mutant Rho GTPase guanine RT nucleotide exchange factor, frabin/FGD4."; RL Am. J. Hum. Genet. 81:158-164(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and CC Rac proteins, by exchanging bound GDP for free GTP. Plays a role in CC regulating the actin cytoskeleton and cell shape. Activates MAPK8 (By CC similarity). {ECO:0000250, ECO:0000269|PubMed:15133042}. CC -!- SUBUNIT: Homooligomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell CC projection, filopodium {ECO:0000250}. Note=Concentrated in filopodia CC and poorly detected at lamellipodia. Binds along the sides of actin CC fibers (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q96M96-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96M96-2; Sequence=VSP_013078, VSP_013082; CC Name=3; CC IsoId=Q96M96-3; Sequence=VSP_013079, VSP_013080, VSP_013081; CC -!- TISSUE SPECIFICITY: Expressed in different tissues, including brain, CC cerebellum, peripheral nerve, skeletal muscle, heart, uterus, placenta CC and testis. {ECO:0000269|PubMed:17564959}. CC -!- DOMAIN: The part of the protein spanning the actin filament-binding CC domain together with the DH domain and the first PH domain is necessary CC and sufficient for microspike formation. Activation of MAPK8 requires CC the presence of all domains with the exception of the actin filament- CC binding domain (By similarity). {ECO:0000250}. CC -!- DISEASE: Charcot-Marie-Tooth disease 4H (CMT4H) [MIM:609311]: A CC recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder CC of the peripheral nervous system, characterized by progressive weakness CC and atrophy, initially of the peroneal muscles and later of the distal CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two CC main groups on the basis of electrophysiologic properties and CC histopathology: primary peripheral demyelinating neuropathies CC (designated CMT1 when they are dominantly inherited) and primary CC peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are CC characterized by severely reduced nerve conduction velocities (less CC than 38 m/sec), segmental demyelination and remyelination with onion CC bulb formations on nerve biopsy, slowly progressive distal muscle CC atrophy and weakness, absent deep tendon reflexes, and hollow feet. By CC convention autosomal recessive forms of demyelinating Charcot-Marie- CC Tooth disease are designated CMT4. {ECO:0000269|PubMed:17564959, CC ECO:0000269|PubMed:17564972}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; AY367054; AAQ72372.1; -; mRNA. DR EMBL; AK057294; BAB71413.1; -; mRNA. DR EMBL; AL713762; CAD28532.1; -; mRNA. DR CCDS; CCDS8727.1; -. [Q96M96-1] DR RefSeq; NP_001291409.1; NM_001304480.1. DR RefSeq; NP_001317302.1; NM_001330373.1. DR RefSeq; NP_001317303.1; NM_001330374.1. DR RefSeq; NP_640334.2; NM_139241.3. [Q96M96-1] DR RefSeq; XP_011518857.1; XM_011520555.1. DR RefSeq; XP_011518858.1; XM_011520556.1. DR AlphaFoldDB; Q96M96; -. DR SMR; Q96M96; -. DR BioGRID; 125734; 22. DR IntAct; Q96M96; 6. DR STRING; 9606.ENSP00000394487; -. DR iPTMnet; Q96M96; -. DR PhosphoSitePlus; Q96M96; -. DR BioMuta; FGD4; -. DR DMDM; 116241363; -. DR EPD; Q96M96; -. DR jPOST; Q96M96; -. DR MassIVE; Q96M96; -. DR MaxQB; Q96M96; -. DR PaxDb; Q96M96; -. DR PeptideAtlas; Q96M96; -. DR ProteomicsDB; 77320; -. [Q96M96-1] DR ProteomicsDB; 77321; -. [Q96M96-2] DR ProteomicsDB; 77322; -. [Q96M96-3] DR Antibodypedia; 48934; 123 antibodies from 20 providers. DR DNASU; 121512; -. DR Ensembl; ENST00000427716.7; ENSP00000394487.2; ENSG00000139132.16. [Q96M96-1] DR Ensembl; ENST00000525053.6; ENSP00000433666.2; ENSG00000139132.16. [Q96M96-1] DR Ensembl; ENST00000583694.2; ENSP00000462623.2; ENSG00000139132.16. [Q96M96-1] DR GeneID; 121512; -. DR KEGG; hsa:121512; -. DR UCSC; uc001rkz.5; human. [Q96M96-1] DR AGR; HGNC:19125; -. DR CTD; 121512; -. DR DisGeNET; 121512; -. DR GeneCards; FGD4; -. DR HGNC; HGNC:19125; FGD4. DR HPA; ENSG00000139132; Low tissue specificity. DR MalaCards; FGD4; -. DR MIM; 609311; phenotype. DR MIM; 611104; gene. DR neXtProt; NX_Q96M96; -. DR OpenTargets; ENSG00000139132; -. DR Orphanet; 99954; Charcot-Marie-Tooth disease type 4H. DR PharmGKB; PA134907925; -. DR VEuPathDB; HostDB:ENSG00000139132; -. DR eggNOG; KOG4424; Eukaryota. DR GeneTree; ENSGT00940000155765; -. DR InParanoid; Q96M96; -. DR OMA; EREHSFY; -. DR OrthoDB; 5385125at2759; -. DR PhylomeDB; Q96M96; -. DR TreeFam; TF316247; -. DR PathwayCommons; Q96M96; -. DR Reactome; R-HSA-193648; NRAGE signals death through JNK. DR Reactome; R-HSA-416482; G alpha (12/13) signalling events. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR SignaLink; Q96M96; -. DR SIGNOR; Q96M96; -. DR BioGRID-ORCS; 121512; 6 hits in 1139 CRISPR screens. DR ChiTaRS; FGD4; human. DR GeneWiki; FGD4; -. DR GenomeRNAi; 121512; -. DR Pharos; Q96M96; Tbio. DR PRO; PR:Q96M96; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q96M96; protein. DR Bgee; ENSG00000139132; Expressed in jejunal mucosa and 188 other tissues. DR ExpressionAtlas; Q96M96; baseline and differential. DR Genevisible; Q96M96; HS. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0001726; C:ruffle; ISS:UniProtKB. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB. DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB. DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. DR CDD; cd15741; FYVE_FGD1_2_4; 1. DR CDD; cd15791; PH1_FDG4; 1. DR CDD; cd13236; PH2_FGD1-4; 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); 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR035899; DBL_dom_sf. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR037742; FDG4_N_PH. DR InterPro; IPR035941; FGD1-4_PH2. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR000306; Znf_FYVE. DR InterPro; IPR017455; Znf_FYVE-rel. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1. DR PANTHER; PTHR12673:SF98; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 4; 1. DR Pfam; PF01363; FYVE; 1. DR Pfam; PF00169; PH; 2. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00064; FYVE; 1. DR SMART; SM00233; PH; 2. DR SMART; SM00325; RhoGEF; 1. DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1. DR SUPFAM; SSF50729; PH domain-like; 2. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50003; PH_DOMAIN; 2. DR PROSITE; PS50178; ZF_FYVE; 1. PE 1: Evidence at protein level; KW Actin-binding; Alternative splicing; Cell projection; KW Charcot-Marie-Tooth disease; Cytoplasm; Cytoskeleton; Disease variant; KW Guanine-nucleotide releasing factor; Metal-binding; Neurodegeneration; KW Neuropathy; Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger. FT CHAIN 1..766 FT /note="FYVE, RhoGEF and PH domain-containing protein 4" FT /id="PRO_0000080947" FT DOMAIN 206..393 FT /note="DH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" FT DOMAIN 422..521 FT /note="PH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 643..740 FT /note="PH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT ZN_FING 559..619 FT /note="FYVE-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT REGION 1..150 FT /note="Actin filament-binding" FT /evidence="ECO:0000250" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 46..83 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 134..188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 742..766 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 53..83 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 136..157 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 170..188 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 752..766 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 565 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 568 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 582 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 585 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 590 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 593 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 611 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 614 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT MOD_RES 702 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 716 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91ZT5" FT VAR_SEQ 1..248 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_013078" FT VAR_SEQ 1..30 FT /note="MEEIKPASASCVSKEKPSKVSDLISRFEGG -> MFSCFLCILSF (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_013079" FT VAR_SEQ 201..207 FT /note="ETNEQKL -> VEHETSS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_013080" FT VAR_SEQ 208..766 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_013081" FT VAR_SEQ 515..766 FT /note="ALQETIDAFHQRHETFRNAIAKDNDIHSEVSTAELGKRAPRWIRDNEVTMCM FT KCKEPFNALTRRRHHCRACGYVVCWKCSDYKAQLEYDGGKLSKVCKDCYQIISGFTDSE FT EKKRKGILEIESAEVSGNSVVCSFLQYMEKSKPWQKAWCVIPKQDPLVLYMYGAPQDVR FT AQATIPLLGYVVDEMPRSADLPHSFKLTQSKSVHSFAADSEELKQKWLKVILLAVTGET FT PGGPNEHPATLDDHPEPKKKSEC -> RRGFAMLPRLISNS (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_013082" FT VARIANT 298 FT /note="M -> R (in CMT4H; found in patient's fibroblasts but FT absent from peripheral nerve where splicing defects and FT aberrant transcripts are detected; dbSNP:rs63749871)" FT /evidence="ECO:0000269|PubMed:17564959, FT ECO:0000269|PubMed:17564972" FT /id="VAR_034957" FT VARIANT 298 FT /note="M -> T (in CMT4H; dbSNP:rs63749871)" FT /evidence="ECO:0000269|PubMed:17564959" FT /id="VAR_044321" FT CONFLICT 79 FT /note="T -> A (in Ref. 2; BAB71413)" FT /evidence="ECO:0000305" FT CONFLICT 303 FT /note="V -> A (in Ref. 1; AAQ72372)" FT /evidence="ECO:0000305" SQ SEQUENCE 766 AA; 86626 MW; B919A7C1D164B05D CRC64; MEEIKPASAS CVSKEKPSKV SDLISRFEGG SSLSNYSDLK KESAVNLNAP RTPGRHGLTT TPQQKLLSQH LPQRQGNDTD KTQGAQTCVA NGVMAAQNQM ECEEEKAATL SSDTSIQASE PLLDTHIVNG ERDETATAPA SPTTDSCDGN ASDSSYRTPG IGPVLPLEER GAETETKVQE RENGESPLEL EQLDQHHEMK ETNEQKLHKI ANELLLTERA YVNRLDLLDQ VFYCKLLEEA NRGSFPAEMV NKIFSNISSI NAFHSKFLLP ELEKRMQEWE TTPRIGDILQ KLAPFLKMYG EYVKGFDNAM ELVKNMTERI PQFKSVVEEI QKQKICGSLT LQHHMLEPVQ RIPRYEMLLK DYLRKLPPDS LDWNDAKKSL EIISTAASHS NSAIRKMENL KKLLEIYEML GEEEDIVNPS NELIKEGQIL KLAARNTSAQ ERYLFLFNNM LLYCVPKFSL VGSKFTVRTR VGIDGMKIVE TQNEEYPHTF QVSGKERTLE LQASSAQDKE EWIKALQETI DAFHQRHETF RNAIAKDNDI HSEVSTAELG KRAPRWIRDN EVTMCMKCKE PFNALTRRRH HCRACGYVVC WKCSDYKAQL EYDGGKLSKV CKDCYQIISG FTDSEEKKRK GILEIESAEV SGNSVVCSFL QYMEKSKPWQ KAWCVIPKQD PLVLYMYGAP QDVRAQATIP LLGYVVDEMP RSADLPHSFK LTQSKSVHSF AADSEELKQK WLKVILLAVT GETPGGPNEH PATLDDHPEP KKKSEC //