ID   FMN1_MOUSE              Reviewed;        1466 AA.
AC   Q05860; A2AFY9; A2AFZ0; Q05859;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 170.
DE   RecName: Full=Formin-1;
DE   AltName: Full=Limb deformity protein;
GN   Name=Fmn1; Synonyms=Fmn, Ld;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Kidney, and Testis;
RX   PubMed=2392150; DOI=10.1038/346850a0;
RA   Woychik R.P., Maas R.L., Zeller R., Vogt T.F., Leder P.;
RT   "'Formins': proteins deduced from the alternative transcripts of the limb
RT   deformity gene.";
RL   Nature 346:850-853(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND ALTERNATIVE SPLICING.
RC   TISSUE=Embryo;
RX   PubMed=1339380; DOI=10.1101/gad.6.1.29;
RA   Grusby-Jackson L., Kuo A., Leder P.;
RT   "A variant limb deformity transcript expressed in the embryonic mouse limb
RT   defines a novel formin.";
RL   Genes Dev. 6:29-37(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   PHOSPHORYLATION, AND ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
RX   PubMed=8516300; DOI=10.1073/pnas.90.12.5554;
RA   Vogt T.F., Jackson-Grusby L., Rush J., Leder P.;
RT   "Formins: phosphoprotein isoforms encoded by the mouse limb deformity
RT   locus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5554-5558(1993).
RN   [5]
RP   ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
RX   PubMed=9119367; DOI=10.1006/geno.1996.4519;
RA   Wang C.C., Chan D.C., Leder P.;
RT   "The mouse formin (Fmn) gene: genomic structure, novel exons, and genetic
RT   mapping.";
RL   Genomics 39:303-311(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=15198975; DOI=10.1101/gad.299904;
RA   Zuniga A., Michos O., Spitz F., Haramis A.-P.G., Panman L., Galli A.,
RA   Vintersten K., Klasen C., Mansfield W., Kuc S., Duboule D., Dono R.,
RA   Zeller R.;
RT   "Mouse limb deformity mutations disrupt a global control region within the
RT   large regulatory landscape required for Gremlin expression.";
RL   Genes Dev. 18:1553-1564(2004).
RN   [7]
RP   ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), FUNCTION, SUBCELLULAR LOCATION,
RP   INTERACTION WITH ALPHA-CATENIN, AND TISSUE SPECIFICITY.
RX   PubMed=14647292; DOI=10.1038/ncb1075;
RA   Kobielak A., Pasolli H.A., Fuchs E.;
RT   "Mammalian formin-1 participates in adherens junctions and polymerization
RT   of linear actin cables.";
RL   Nat. Cell Biol. 6:21-30(2004).
RN   [8]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH TUBULIN.
RX   PubMed=16480715; DOI=10.1016/j.yexcr.2005.12.035;
RA   Zhou F., Leder P., Martin S.S.;
RT   "Formin-1 protein associates with microtubules through a peptide domain
RT   encoded by exon-2.";
RL   Exp. Cell Res. 312:1119-1126(2006).
CC   -!- FUNCTION: Plays a role in the formation of adherens junction and the
CC       polymerization of linear actin cables. {ECO:0000269|PubMed:14647292,
CC       ECO:0000269|PubMed:15198975}.
CC   -!- SUBUNIT: Interacts with alpha-catenin and may interact with tubulin.
CC       {ECO:0000269|PubMed:14647292, ECO:0000269|PubMed:16480715}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell junction, adherens
CC       junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
CC       Note=Localization to the adherens junctions is alpha-catenin-dependent.
CC       Also localizes to F-actin bundles originating from adherens junctions.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.
CC       Note=Isoform 2 localizes to microtubules.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=IA;
CC         IsoId=Q05860-1; Sequence=Displayed;
CC       Name=2; Synonyms=IB;
CC         IsoId=Q05860-2; Sequence=VSP_027216;
CC       Name=3; Synonyms=II;
CC         IsoId=Q05860-3; Sequence=VSP_001570;
CC       Name=4; Synonyms=III;
CC         IsoId=Q05860-4; Sequence=VSP_001571, VSP_001572;
CC       Name=5; Synonyms=IV;
CC         IsoId=Q05860-5; Sequence=VSP_027214, VSP_027215, VSP_027216;
CC       Name=6; Synonyms=V;
CC         IsoId=Q05860-6; Sequence=VSP_029424, VSP_029425, VSP_027216;
CC   -!- TISSUE SPECIFICITY: It is present in the adult kidney, testis, limb,
CC       ovary, brain, small intestine, salivary gland and harderian gland.
CC       Isoforms 1, 2 and 5 are detected in skin and keratinocytes. Isoform 5
CC       is found throughout the embryo. {ECO:0000269|PubMed:14647292,
CC       ECO:0000269|PubMed:2392150}.
CC   -!- DEVELOPMENTAL STAGE: It is present throughout the embryo. In the
CC       developing limb bud, the protein is expressed in the apical ectodermal
CC       ridge and the mesenchymal compartment, predominantly in the posterior
CC       region. During kidney morphogenesis, expression is initially restricted
CC       to the epithelial compartment of the pronephros and mesonephros.
CC       Isoform 5 is found in the apical ectodermal ridge and the mesenchymal
CC       compartment of the developing limb bud.
CC   -!- PTM: Phosphorylated on serine and possibly threonine residues.
CC       {ECO:0000269|PubMed:8516300}.
CC   -!- MISCELLANEOUS: Was originally thought to play a role in limb bud
CC       development based on the fact that limb deformity (ld) mutants are
CC       associated with Fmn1 gene disruption. However, PubMed:15198975 shows
CC       that limb deformity mutations rather affects Grem1 cis-regulatory
CC       regions localized in Fmn1 gene and that loss of Grem1 (gremlin-1)
CC       expression is the cause of limb malformations.
CC   -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X53599; CAA37668.1; -; mRNA.
DR   EMBL; X62379; CAA44244.1; -; mRNA.
DR   EMBL; AL672253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL691437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL691466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS16559.1; -. [Q05860-1]
DR   CCDS; CCDS71113.1; -. [Q05860-5]
DR   PIR; S11515; S11515.
DR   PIR; S24407; S24407.
DR   RefSeq; NP_001272388.1; NM_001285459.1. [Q05860-5]
DR   RefSeq; NP_034360.2; NM_010230.2. [Q05860-1]
DR   RefSeq; XP_011237596.1; XM_011239294.1. [Q05860-2]
DR   RefSeq; XP_011237597.1; XM_011239295.1. [Q05860-2]
DR   PDB; 2JUP; NMR; -; P=881-888.
DR   PDB; 2RLY; NMR; -; P=874-881.
DR   PDB; 2RM0; NMR; -; P=880-888.
DR   PDBsum; 2JUP; -.
DR   PDBsum; 2RLY; -.
DR   PDBsum; 2RM0; -.
DR   AlphaFoldDB; Q05860; -.
DR   SMR; Q05860; -.
DR   BioGRID; 199711; 14.
DR   DIP; DIP-646N; -.
DR   ELM; Q05860; -.
DR   IntAct; Q05860; 2.
DR   MINT; Q05860; -.
DR   STRING; 10090.ENSMUSP00000099606; -.
DR   iPTMnet; Q05860; -.
DR   PhosphoSitePlus; Q05860; -.
DR   MaxQB; Q05860; -.
DR   PaxDb; 10090-ENSMUSP00000099606; -.
DR   PeptideAtlas; Q05860; -.
DR   ProteomicsDB; 267599; -. [Q05860-1]
DR   ProteomicsDB; 267600; -. [Q05860-2]
DR   ProteomicsDB; 267601; -. [Q05860-3]
DR   ProteomicsDB; 267602; -. [Q05860-4]
DR   ProteomicsDB; 267603; -. [Q05860-5]
DR   ProteomicsDB; 267604; -. [Q05860-6]
DR   Pumba; Q05860; -.
DR   Antibodypedia; 51683; 129 antibodies from 19 providers.
DR   DNASU; 14260; -.
DR   Ensembl; ENSMUST00000081349.9; ENSMUSP00000080093.7; ENSMUSG00000044042.20. [Q05860-5]
DR   Ensembl; ENSMUST00000099576.9; ENSMUSP00000097171.3; ENSMUSG00000044042.20. [Q05860-2]
DR   Ensembl; ENSMUST00000102547.10; ENSMUSP00000099606.4; ENSMUSG00000044042.20. [Q05860-1]
DR   GeneID; 14260; -.
DR   KEGG; mmu:14260; -.
DR   UCSC; uc008lpk.1; mouse. [Q05860-4]
DR   UCSC; uc008lpl.1; mouse. [Q05860-1]
DR   UCSC; uc008lpn.2; mouse. [Q05860-5]
DR   AGR; MGI:101815; -.
DR   CTD; 342184; -.
DR   MGI; MGI:101815; Fmn1.
DR   VEuPathDB; HostDB:ENSMUSG00000044042; -.
DR   eggNOG; KOG1922; Eukaryota.
DR   GeneTree; ENSGT00940000154289; -.
DR   HOGENOM; CLU_271027_0_0_1; -.
DR   InParanoid; Q05860; -.
DR   OMA; WHERNDN; -.
DR   OrthoDB; 53873at2759; -.
DR   PhylomeDB; Q05860; -.
DR   TreeFam; TF351317; -.
DR   BioGRID-ORCS; 14260; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Fmn1; mouse.
DR   EvolutionaryTrace; Q05860; -.
DR   PRO; PR:Q05860; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q05860; Protein.
DR   Bgee; ENSMUSG00000044042; Expressed in lumbar dorsal root ganglion and 180 other cell types or tissues.
DR   ExpressionAtlas; Q05860; baseline and differential.
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; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
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; IPI:MGI.
DR   GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR   GO; GO:0035136; P:forelimb morphogenesis; IMP:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0035137; P:hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0060173; P:limb development; IMP:MGI.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:MGI.
DR   GO; GO:0051127; P:positive regulation of actin nucleation; IDA:MGI.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:MGI.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0072092; P:ureteric bud invasion; IMP:MGI.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR001265; Formin_Cappuccino_subfam.
DR   PANTHER; PTHR13037; FORMIN; 1.
DR   PANTHER; PTHR13037:SF11; FORMIN-1; 1.
DR   Pfam; PF02181; FH2; 1.
DR   PRINTS; PR00828; FORMIN.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51444; FH2; 1.
DR   Genevisible; Q05860; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Cell junction;
KW   Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..1466
FT                   /note="Formin-1"
FT                   /id="PRO_0000194886"
FT   DOMAIN          870..970
FT                   /note="FH1"
FT   DOMAIN          983..1435
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   REGION          1..624
FT                   /note="Microtubule-binding"
FT   REGION          150..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..842
FT                   /note="Mediates interaction with alpha-catenin"
FT   REGION          507..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          913..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1446..1466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          722..786
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        153..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..868
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..897
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..971
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1446..1460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..682
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:1339380"
FT                   /id="VSP_027214"
FT   VAR_SEQ         1..623
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_029424"
FT   VAR_SEQ         624
FT                   /note="P -> MVTTGSPPFNTMGACYRYNPRYGQPISVPKVWKCRHRRSVTPDE
FT                   (in isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_029425"
FT   VAR_SEQ         625..722
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001570"
FT   VAR_SEQ         626..627
FT                   /note="IA -> SV (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001571"
FT   VAR_SEQ         628..1466
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001572"
FT   VAR_SEQ         683
FT                   /note="N -> MEEVGNSLSSRDVLEPDKSEAGLEMAQSILSKFSMKSLFGFTNKLDS
FT                   LEPEEEDAVLKAFRSLEGDPAPERGDPSKGSDQPQAEAPVPPDLKNDGKSARAETGSEG
FT                   SQGKGRSNTSSPGYELSPATVSVDNEEVIWVRGTLVHTTSDSDSEDGDQEAEEESSLDT
FT                   QKPTTVVLCEPSQEPKDRAGDSEENTDTGNTDDTELCAEESQRTLPETSSKLELGGDGS
FT                   HPAEHSPRQDQAAEEGSQIPPAATDQTVGALASTVSKREAPEEKPFQLPAFFSGLRVLK
FT                   KGATAEAGETITEIKPKDGDLALLKLTQRVQKSLGQGGPQTVKSPGRATDPKATPTLLE
FT                   QLSQLLNIDMPRTEQKEADPEFHGADEMGYSTDQESHKSPRDAHVQGGQVKARTPETAL
FT                   EAFKALFIRPPKKGSTADTSELEALKRKMKHEKESLRAVFERSKSRPADSPSDPKS
FT                   (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:1339380"
FT                   /id="VSP_027215"
FT   VAR_SEQ         1250..1285
FT                   /note="Missing (in isoform 2, isoform 5 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:1339380"
FT                   /id="VSP_027216"
FT   CONFLICT        220
FT                   /note="V -> A (in Ref. 1; CAA37668)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        776
FT                   /note="G -> E (in Ref. 1; CAA37668 and 2; CAA44244)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        866
FT                   /note="H -> Q (in Ref. 1; CAA37668 and 2; CAA44244)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        950
FT                   /note="G -> GPP (in Ref. 1; CAA37668 and 2; CAA44244)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1466 AA;  163581 MW;  5482F8AAB66CBF32 CRC64;
     MEGTHCTLQL HNPIAELCYI SFYLPKGEVR GFSYKGTVTL DRSNNAFHNC YQVREGPDIT
     SLSQQPNEHP GDIFFKQTPT KNILTELYKL TAEKERLLDS LLRSDNILGV SMGSQEGKLQ
     ELSVILATGD EYFQSAGNWR RELPVSSLIR RSTQENKKPR RSGRRRESPE ELRQKRTRRK
     GRGCQESAFQ MGKDQVCSSS SLSFRARPNL RLLEERGNLV PRGTLTSSLR RRESCPANIL
     RTPDADLAFG NSGRTSEDTD LEGPLSPDSS PTEVGDADVG GQLKSSHQQE PPQPNVSESH
     GKHAGAERWS SRTRKSKSLE RTCSKKPVSK VVAKIQEPSA PVKRIVRAHH DGKGRVAYGP
     ETQTEFIPKA DFLTLPGGET ETHSSGRLEE EQPGIKSLRS SAPERASITK EPASTEAAVN
     KVLRKVIESE KLDEATEGKR LGFSLNTRAT HTFPETRSQR KAGLPQSGHK FLLLDLPHTV
     GPDSPQPKCD EKKPTPQVPT ALGMVFNNSS PQSSAHKRLS PVPSPLSPRC PSPQQHHRIL
     LLPPLPSEGE VVFNEYPSRK NDVSSGFPSA DTLEPSSTTK VTETKGASPT SLRASQTWLV
     SEEASEKGLG PEKITAPPQH QLPPGIASEG FPCDNFKEQT AKDLPNKDGG VWVPGYRAGP
     PCPFLLHEEK EKTSRSELYL DLNPDQSPTE QDDRTPGRLQ AVWPPPKTKD TEEKVGLKYT
     EAEYQAAILH LKREHKEEIE TLQAQFELKT FHIRGEHALV TARLEEAIEN LKQQLGKRRE
     GCEEMRDVCI STDDDCSPKA FRNVCIQTDR ETFLKPCDAE SKATRSSQIV PKKLTISLTQ
     LSPSKDSKDI HAPFQTREGT SSSSQHKISP PAPPTPPPLP PPLIPPPPPL PPGLGPLPPA
     PPIPPVCPVS PPPPPPPPPP TPVPPSDGPP PPPPPPPPLP NVLALPNSGG PPPPPPPPPP
     GLAPPPPPGL SFGLSSSSSQ YPRKPAIEPS CPMKPLYWTR IQINDKSQDA APTLWDSLEE
     PHIRDTSEFE YLFSKDTTQQ KKKPLSEAYE KKNKVKKIIK LLDGKRSQTV GILISSLHLE
     MKDIQQAIFT VDDSVVDLET LAALYENRAQ EDELTKIRKY YETSKEEDLK LLDKPEQFLH
     ELAQIPNFAE RAQCIIFRAV FSEGITSLHR KVEIVTRASK GLLHMKSVKD ILALILAFGN
     YMNGGNRTRG QADGYSLEIL PKLKDVKSRD NGMNLVDYVV KYYLRYYDQC KHHDQEASCR
     GKDLFSLYFH IAVHPQRKSG LELKQEAGTD KSVFPLPEPQ DFFLASQVKF EDLLKDLRKL
     KRQLEASEQQ MKLVCKESPR EYLQPFKDKL EEFFKKAKKE HKMEESHLEN AQKSFETTVG
     YFGMKPKTGE KEVTPSYVFM VWFEFCSDFK TIWKRESKNI SKERLKMAQA SVSKLTSEKK
     VETKKINPTA SLKERLRQKE ASVATN
//