FMN1_HUMAN
ID FMN1_HUMAN Reviewed; 1419 AA.
AC Q68DA7; Q3B7I6; Q3ZAR4; Q6ZSY1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Formin-1;
DE AltName: Full=Limb deformity protein homolog;
GN Name=FMN1; Synonyms=FMN, LD;
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 2).
RC TISSUE=Retina;
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 [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., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT PRO-686.
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 [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT
RP PRO-686.
RC TISSUE=Brain;
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 [5]
RP IDENTIFICATION, AND DEVELOPMENTAL STAGE.
RX PubMed=1673046;
RA Maas R.L., Jepeal L.I., Elfering S.L., Holcombe R.F., Morton C.C.,
RA Eddy R.L., Byers M.G., Shows T.B., Leder P.;
RT "A human gene homologous to the formin gene residing at the murine limb
RT deformity locus: chromosomal location and RFLPs.";
RL Am. J. Hum. Genet. 48:687-695(1991).
RN [6]
RP IDENTIFICATION.
RX PubMed=15202026;
RA Katoh M., Katoh M.;
RT "Identification and characterization of the human FMN1 gene in silico.";
RL Int. J. Mol. Med. 14:121-126(2004).
RN [7]
RP IDENTIFICATION BY 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: Plays a role in the formation of adherens junction and the
CC polymerization of linear actin cables. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with alpha-catenin and may interact with tubulin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell junction, adherens junction {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Localization to the adherens junctions is
CC alpha-catenin-dependent. Also localizes to F-actin bundles originating
CC from adherens junctions and to microtubules (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q68DA7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68DA7-2; Sequence=VSP_027209, VSP_027210;
CC Name=3;
CC IsoId=Q68DA7-3; Sequence=VSP_027208, VSP_027211, VSP_027212,
CC VSP_027213;
CC Name=5;
CC IsoId=Q68DA7-5; Sequence=VSP_027208, VSP_027211;
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal kidney and fetal lung.
CC {ECO:0000269|PubMed:1673046}.
CC -!- PTM: Phosphorylated on serine and possibly threonine residues.
CC {ECO:0000250|UniProtKB:Q05860}.
CC -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC subfamily. {ECO:0000305}.
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DR EMBL; CR749487; CAH18313.1; -; mRNA.
DR EMBL; AC090098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC019278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC103692; AAI03693.1; -; mRNA.
DR EMBL; BC107593; AAI07594.1; -; mRNA.
DR EMBL; AK127078; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS45209.1; -. [Q68DA7-5]
DR CCDS; CCDS61581.1; -. [Q68DA7-1]
DR CCDS; CCDS61582.1; -. [Q68DA7-2]
DR RefSeq; NP_001096654.1; NM_001103184.3. [Q68DA7-5]
DR RefSeq; NP_001264242.1; NM_001277313.1. [Q68DA7-1]
DR RefSeq; NP_001264243.1; NM_001277314.1. [Q68DA7-2]
DR RefSeq; XP_011519806.1; XM_011521504.2. [Q68DA7-1]
DR RefSeq; XP_016877619.1; XM_017022130.1. [Q68DA7-1]
DR AlphaFoldDB; Q68DA7; -.
DR SMR; Q68DA7; -.
DR BioGRID; 131167; 11.
DR ELM; Q68DA7; -.
DR IntAct; Q68DA7; 7.
DR MINT; Q68DA7; -.
DR STRING; 9606.ENSP00000479134; -.
DR iPTMnet; Q68DA7; -.
DR PhosphoSitePlus; Q68DA7; -.
DR BioMuta; FMN1; -.
DR DMDM; 327478585; -.
DR EPD; Q68DA7; -.
DR jPOST; Q68DA7; -.
DR MassIVE; Q68DA7; -.
DR MaxQB; Q68DA7; -.
DR PaxDb; Q68DA7; -.
DR PeptideAtlas; Q68DA7; -.
DR PRIDE; Q68DA7; -.
DR ProteomicsDB; 66065; -. [Q68DA7-1]
DR ProteomicsDB; 66066; -. [Q68DA7-2]
DR ProteomicsDB; 66067; -. [Q68DA7-3]
DR ProteomicsDB; 66068; -. [Q68DA7-5]
DR Antibodypedia; 51683; 109 antibodies from 19 providers.
DR DNASU; 342184; -.
DR Ensembl; ENST00000320930.7; ENSP00000325166.7; ENSG00000248905.10. [Q68DA7-2]
DR Ensembl; ENST00000334528.13; ENSP00000333950.9; ENSG00000248905.10. [Q68DA7-5]
DR Ensembl; ENST00000558197.1; ENSP00000452984.1; ENSG00000248905.10. [Q68DA7-3]
DR Ensembl; ENST00000616417.5; ENSP00000479134.1; ENSG00000248905.10. [Q68DA7-1]
DR GeneID; 342184; -.
DR KEGG; hsa:342184; -.
DR MANE-Select; ENST00000616417.5; ENSP00000479134.1; NM_001277313.2; NP_001264242.1.
DR UCSC; uc001zhf.6; human. [Q68DA7-1]
DR CTD; 342184; -.
DR DisGeNET; 342184; -.
DR GeneCards; FMN1; -.
DR HGNC; HGNC:3768; FMN1.
DR HPA; ENSG00000248905; Tissue enhanced (retina).
DR MIM; 136535; gene.
DR neXtProt; NX_Q68DA7; -.
DR OpenTargets; ENSG00000248905; -.
DR VEuPathDB; HostDB:ENSG00000248905; -.
DR eggNOG; KOG1654; Eukaryota.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000154289; -.
DR HOGENOM; CLU_271027_0_0_1; -.
DR InParanoid; Q68DA7; -.
DR OMA; STEHTCR; -.
DR OrthoDB; 509938at2759; -.
DR PhylomeDB; Q68DA7; -.
DR TreeFam; TF326072; -.
DR PathwayCommons; Q68DA7; -.
DR SignaLink; Q68DA7; -.
DR BioGRID-ORCS; 342184; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; FMN1; human.
DR GenomeRNAi; 342184; -.
DR Pharos; Q68DA7; Tbio.
DR PRO; PR:Q68DA7; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q68DA7; protein.
DR Bgee; ENSG00000248905; Expressed in secondary oocyte and 111 other tissues.
DR ExpressionAtlas; Q68DA7; baseline and differential.
DR Genevisible; Q68DA7; HS.
DR GO; GO:0005884; C:actin filament; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0035136; P:forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0035137; P:hindlimb morphogenesis; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0051127; P:positive regulation of actin nucleation; IEA:Ensembl.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0072092; P:ureteric bud invasion; IEA:Ensembl.
DR Gene3D; 1.20.58.2220; -; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR001265; Formin_Cappuccino_subfam.
DR Pfam; PF02181; FH2; 1.
DR PRINTS; PR00828; FORMIN.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cell membrane;
KW Coiled coil; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1419
FT /note="Formin-1"
FT /id="PRO_0000296361"
FT DOMAIN 870..957
FT /note="FH1"
FT DOMAIN 972..1388
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 1..622
FT /note="Microtubule-binding"
FT /evidence="ECO:0000250"
FT REGION 138..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..842
FT /note="Mediates interaction with alpha-catenin"
FT /evidence="ECO:0000250"
FT REGION 685..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 720..774
FT /evidence="ECO:0000255"
FT COMPBIAS 296..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..960
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..680
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027208"
FT VAR_SEQ 623..662
FT /note="GISSEGFPWDGFNEQTPKDLPNRDGGAWVLGYRAGPACPF -> AFHWDLQQ
FT HFQEPVIRTVSISCASNLIKEEAGKGKESRSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_027209"
FT VAR_SEQ 663..1419
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_027210"
FT VAR_SEQ 681
FT /note="H -> MENVDNSLDGSDVSEPAKPEAGLEVAQSILSKFSMKSLFGFTSKLES
FT VNPEEEDAVLKAFHSLDVNPTSQQDDSSNGLDPQEAGSRVSPDLGNDEKIASVETESEG
FT SQRKEAGTSLLAQELLPLSTLKGTKDDVICVRGTLVHTTSDSDSDDGGQEPEEGSSTNG
FT PKSPSGVLSEPSQESKENPGGFRENTVTGEMNGAELCAEDPQRIPPEMSSKLEAGNGGL
FT QTERRPSQDQVGEEGSQDLPAVTNQNSSVGITESASSKKEVSGEKSFQLPAFFSGLRVL
FT KKGATAEGGETITEIKPKDGDLALLKLTQPVQKSLVQAGLQTVKSEKKATDPKATPTLL
FT EQLSLLLNIDMPKTEPKGADPESPRREEMGCNADQESQSGPGVPQTQGGEVKPKSPETA
FT LEAFKALFIRPPRKGTTADTSELEALKRKMRHEKESLRAVFERSNSKPADGPSDSKS
FT (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027211"
FT VAR_SEQ 721..726
FT /note="EYQAAI -> GNVKGS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027212"
FT VAR_SEQ 727..1419
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027213"
FT VARIANT 686
FT /note="L -> P (in dbSNP:rs2306277)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_034630"
FT CONFLICT 57
FT /note="S -> A (in Ref. 1; CAH18313)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="L -> P (in Ref. 1; CAH18313)"
FT /evidence="ECO:0000305"
FT CONFLICT Q68DA7-3:171
FT /note="G -> V (in Ref. 3; AAI03693/AAI07594)"
FT /evidence="ECO:0000305"
FT CONFLICT Q68DA7-3:239
FT /note="G -> E (in Ref. 3; AAI07594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1419 AA; 157578 MW; 6ED2783FC8151A43 CRC64;
MEGTHCTLQL HKPITELCYI SFCLPKGEVR GFSYKGTVTL DRSNKGFHNC YQVREESDII
SLSQEPDEHP GDIFFKQTPT KDILTELYKL TTERERLLTN LLSSDHILGI TMGNQEGKLQ
ELSVSLAPED DCFQSAGDWQ GELPVGPLNK RSTHGNKKPR RSSGRRESFG ALPQKRTKRK
GRGGRESAPL MGKDKICSSH SLPLSRTRPN LWVLEEKGNL LPNGALACSL QRRESCPPDI
PKTPDTDLGF GSFETAFKDT GLGREVLPPD CSSTEAGGDG IRRPPSGLEH QQTGLSESHQ
DPEKHPEAEK DEMEKPAKRT CKQKPVSKVV AKVQDLSSQV QRVVKTHSKG KETIAIRPAA
HAEFVPKADL LTLPGAEAGA HGSRRQGKER QGDRSSQSPA GETASISSVS ASAEGAVNKV
PLKVIESEKL DEAPEGKRLG FPVHTSVPHT RPETRNKRRA GLPLGGHKSL FLDLPHKVGP
DSSQPRGDKK KPSPPAPAAL GKVFNNSASQ SSTHKQTSPV PSPLSPRLPS PQQHHRILRL
PALPGEREAA LNDSPCRKSR VFSGCVSADT LEPPSSAKVT ETKGASPAFL RAGQPRLVPG
ETLEKSLGPG KTTAEPQHQS PPGISSEGFP WDGFNEQTPK DLPNRDGGAW VLGYRAGPAC
PFLLHEEREK SNRSELYLDL HPDHSLTEQD DRTPGRLQAV WPPPKTKDTE EKVGLKYTEA
EYQAAILHLK REHKEEIENL QAQFELRAFH IRGEHAMITA RLEETIENLK HELEHRWRGG
CEERKDVCIS TDDDCPPKTF RNVCVQTDRE TFLKPCESES KTTRSNQLVP KKLNISSLSQ
LSPPNDHKDI HAALQPMEGM ASNQQKALPP PPASIPPPPP LPSGLGSLSP APPMPPVSAG
PPLPPPPPPP PPLPPPSSAG PPPPPPPPPL PNSPAPPNPG GPPPAPPPPG LAPPPPPGLF
FGLGSSSSQC PRKPAIEPSC PMKPLYWTRI QISDRSQNAT PTLWDSLEEP DIRDPSEFEY
LFSKDTTQQK KKPLSETYEK KNKVKKIIKL LDGKRSQTVG ILISSLHLEM KDIQQAIFNV
DDSVVDLETL AALYENRAQE DELVKIRKYY ETSKEEELKL LDKPEQFLHE LAQIPNFAER
AQCIIFRSVF SEGITSLHRK VEIITRASKD LLHVKSVKDI LALILAFGNY MNGGNRTRGQ
ADGYSLEILP KLKDVKSRDN GINLVDYVVK YYLRYYDQEA GTEKSVFPLP EPQDFFLASQ
VKFEDLIKDL RKLKRQLEAS EKQMVVVCKE SPKEYLQPFK DKLEEFFQKA KKEHKMEESH
LENAQKSFET TVRYFGMKPK SGEKEITPSY VFMVWYEFCS DFKTIWKRES KNISKERLKM
AQESVSKLTS EKKVETKKIN PTASLKERLR QKEASVTTN
