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   02-SEP-2026, entry version 153.
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; DOI=10.3892/ijmm.14.1.121;
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_001103184.4. [Q68DA7-5]
DR   RefSeq; NP_001264242.1; NM_001277313.2. [Q68DA7-1]
DR   RefSeq; NP_001264243.1; NM_001277314.2. [Q68DA7-2]
DR   RefSeq; XP_011519806.1; XM_011521504.4. [Q68DA7-1]
DR   AlphaFoldDB; Q68DA7; -.
DR   SMR; Q68DA7; -.
DR   BioGRID; 131167; 15.
DR   ELM; Q68DA7; -.
DR   FunCoup; Q68DA7; 1184.
DR   IntAct; Q68DA7; 8.
DR   MINT; Q68DA7; -.
DR   NDEx; IQUERY-CP-FMN1; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000479134; -.
DR   GlyGen; Q68DA7; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q68DA7; -.
DR   PhosphoSitePlus; Q68DA7; -.
DR   BioMuta; FMN1; -.
DR   DMDM; 327478585; -.
DR   jPOST; Q68DA7; -.
DR   MassIVE; Q68DA7; -.
DR   PaxDb; 9606-ENSP00000479134; -.
DR   PeptideAtlas; Q68DA7; -.
DR   ProteomicsDB; 66065; -. [Q68DA7-1]
DR   ProteomicsDB; 66066; -. [Q68DA7-2]
DR   ProteomicsDB; 66067; -. [Q68DA7-3]
DR   ProteomicsDB; 66068; -. [Q68DA7-5]
DR   Antibodypedia; 51683; 100 antibodies from 20 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   AGR; HGNC:3768; -.
DR   CTD; 342184; -.
DR   DisGeNET; 342184; -.
DR   GeneCards; FMN1; -.
DR   HGNC; HGNC:3768; FMN1.
DR   HPA; ENSG00000248905; Tissue enhanced (retina).
DR   MalaCards; FMN1; -.
DR   MIM; 136535; gene.
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; 427644at2759; -.
DR   PAN-GO; Q68DA7; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; Q68DA7; -.
DR   PathwayCommons; Q68DA7; -.
DR   SignaLink; Q68DA7; -.
DR   Agora; ENSG00000248905; -.
DR   BioGRID-ORCS; 342184; 12 hits in 1150 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 male germ line stem cell (sensu Vertebrata) in testis and 112 other cell types or tissues.
DR   ExpressionAtlas; Q68DA7; 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:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IBA:GO_Central.
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:0070649; P:formin-nucleated actin cable assembly; IBA:GO_Central.
DR   FunFam; 1.20.58.2220:FF:000005; Formin 1; 1.
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; PTHR45920; FORMIN HOMOLOGY 2 DOMAIN CONTAINING, ISOFORM I; 1.
DR   PANTHER; PTHR45920:SF7; FORMIN-G; 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.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cell junction; Cell membrane;
KW   Coiled coil; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW   Proteomics identification; 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        151..163
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..529
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..882
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..958
FT                   /note="Pro 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
//