TWF2_HUMAN
ID TWF2_HUMAN Reviewed; 349 AA.
AC Q6IBS0; Q9Y3F5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Twinfilin-2;
DE AltName: Full=A6-related protein;
DE Short=hA6RP;
DE AltName: Full=Protein tyrosine kinase 9-like;
DE AltName: Full=Twinfilin-1-like protein;
GN Name=TWF2; Synonyms=PTK9L; ORFNames=MSTP011;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RC TISSUE=Keratinocyte;
RX PubMed=10406962; DOI=10.1046/j.1432-1327.1999.00537.x;
RA Rohwer A., Kittstein W., Marks F., Gschwendt M.;
RT "Cloning, expression and characterization of an A6 related protein.";
RL Eur. J. Biochem. 263:518-525(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Aorta;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W., Liu S.,
RA Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y.,
RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Lung, and Placenta;
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 PROTEIN SEQUENCE OF 2-19 AND 279-293, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309 AND SER-349, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 6-313.
RG Structural genomics consortium (SGC);
RT "Crystal structure of N-Terminal and C-Terminal actin depolymerizing factor
RT homology (Adf-H) domain of human twinfilin-2.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-72; ARG-76 AND THR-103.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Actin-binding protein involved in motile and morphological
CC processes. Inhibits actin polymerization, likely by sequestering G-
CC actin. By capping the barbed ends of filaments, it also regulates
CC motility. Seems to play an important role in clathrin-mediated
CC endocytosis and distribution of endocytic organelles. May play a role
CC in regulating the mature length of the middle and short rows of
CC stereocilia (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with G-actin; ADP-actin form and capping protein
CC (CP). May also be able to interact with TWF1 and phosphoinositides,
CC PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated. Interacts
CC with MYO7A (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q6IBS0; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-722204, EBI-750109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10406962}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10406962}. Cell projection, stereocilium
CC {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin
CC structure sublocalization.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC {ECO:0000269|PubMed:10406962}.
CC -!- PTM: In vitro, phosphorylated by PRKCZ, CK2 and SRC.
CC {ECO:0000269|PubMed:10406962}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. Twinfilin
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular embrace - Issue 73
CC of August 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/073";
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DR EMBL; Y17169; CAB38055.1; -; mRNA.
DR EMBL; AL136773; CAB66707.1; -; mRNA.
DR EMBL; AF109365; AAQ13513.1; -; mRNA.
DR EMBL; CR456732; CAG33013.1; -; mRNA.
DR EMBL; CR533520; CAG38551.1; -; mRNA.
DR EMBL; BC000327; AAH00327.1; -; mRNA.
DR EMBL; BC003161; AAH03161.1; -; mRNA.
DR EMBL; BC016452; AAH16452.1; -; mRNA.
DR CCDS; CCDS2849.1; -.
DR PIR; T46362; T46362.
DR RefSeq; NP_009215.1; NM_007284.3.
DR PDB; 2VAC; X-ray; 1.70 A; A=6-137.
DR PDB; 2W0I; X-ray; 1.80 A; A=181-313.
DR PDBsum; 2VAC; -.
DR PDBsum; 2W0I; -.
DR AlphaFoldDB; Q6IBS0; -.
DR SMR; Q6IBS0; -.
DR BioGRID; 116472; 80.
DR IntAct; Q6IBS0; 32.
DR MINT; Q6IBS0; -.
DR STRING; 9606.ENSP00000303908; -.
DR GlyGen; Q6IBS0; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q6IBS0; -.
DR PhosphoSitePlus; Q6IBS0; -.
DR SwissPalm; Q6IBS0; -.
DR BioMuta; TWF2; -.
DR DMDM; 94730596; -.
DR OGP; Q9Y3F5; -.
DR EPD; Q6IBS0; -.
DR jPOST; Q6IBS0; -.
DR MassIVE; Q6IBS0; -.
DR MaxQB; Q6IBS0; -.
DR PaxDb; Q6IBS0; -.
DR PeptideAtlas; Q6IBS0; -.
DR PRIDE; Q6IBS0; -.
DR ProteomicsDB; 66370; -.
DR Antibodypedia; 46152; 243 antibodies from 28 providers.
DR DNASU; 11344; -.
DR Ensembl; ENST00000305533.10; ENSP00000303908.4; ENSG00000247596.10.
DR GeneID; 11344; -.
DR KEGG; hsa:11344; -.
DR MANE-Select; ENST00000305533.10; ENSP00000303908.4; NM_007284.4; NP_009215.1.
DR UCSC; uc003ddd.4; human.
DR CTD; 11344; -.
DR DisGeNET; 11344; -.
DR GeneCards; TWF2; -.
DR HGNC; HGNC:9621; TWF2.
DR HPA; ENSG00000247596; Tissue enhanced (skeletal).
DR MIM; 607433; gene.
DR neXtProt; NX_Q6IBS0; -.
DR OpenTargets; ENSG00000247596; -.
DR PharmGKB; PA162407429; -.
DR VEuPathDB; HostDB:ENSG00000247596; -.
DR eggNOG; KOG1747; Eukaryota.
DR GeneTree; ENSGT00530000063868; -.
DR HOGENOM; CLU_031995_1_0_1; -.
DR InParanoid; Q6IBS0; -.
DR OMA; RWDTDYD; -.
DR OrthoDB; 1578109at2759; -.
DR PhylomeDB; Q6IBS0; -.
DR TreeFam; TF352598; -.
DR PathwayCommons; Q6IBS0; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q6IBS0; -.
DR BioGRID-ORCS; 11344; 16 hits in 1079 CRISPR screens.
DR ChiTaRS; TWF2; human.
DR EvolutionaryTrace; Q6IBS0; -.
DR GeneWiki; TWF2; -.
DR GenomeRNAi; 11344; -.
DR Pharos; Q6IBS0; Tbio.
DR PRO; PR:Q6IBS0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q6IBS0; protein.
DR Bgee; ENSG00000247596; Expressed in apex of heart and 192 other tissues.
DR ExpressionAtlas; Q6IBS0; baseline and differential.
DR Genevisible; Q6IBS0; HS.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISS:BHF-UCL.
DR GO; GO:0030426; C:growth cone; IDA:BHF-UCL.
DR GO; GO:0030027; C:lamellipodium; ISS:BHF-UCL.
DR GO; GO:0030016; C:myofibril; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0032420; C:stereocilium; ISS:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:BHF-UCL.
DR GO; GO:0005080; F:protein kinase C binding; IPI:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; ISS:BHF-UCL.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISS:BHF-UCL.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:BHF-UCL.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:BHF-UCL.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IBA:GO_Central.
DR GO; GO:0032532; P:regulation of microvillus length; IC:BHF-UCL.
DR GO; GO:0042989; P:sequestering of actin monomers; ISS:BHF-UCL.
DR Gene3D; 3.40.20.10; -; 2.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR028458; Twinfilin.
DR PANTHER; PTHR13759; PTHR13759; 1.
DR Pfam; PF00241; Cofilin_ADF; 2.
DR SMART; SM00102; ADF; 2.
DR PROSITE; PS51263; ADF_H; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell projection;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330"
FT CHAIN 2..349
FT /note="Twinfilin-2"
FT /id="PRO_0000233136"
FT DOMAIN 4..139
FT /note="ADF-H 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 177..313
FT /note="ADF-H 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 322..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330"
FT MOD_RES 14
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 309
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT VARIANT 72
FT /note="R -> C (in dbSNP:rs35114109)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042407"
FT VARIANT 76
FT /note="Q -> R (in dbSNP:rs35711542)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042408"
FT VARIANT 103
FT /note="A -> T (in a lung neuroendocrine carcinoma sample;
FT somatic mutation; dbSNP:rs867679383)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042409"
FT CONFLICT 110
FT /note="K -> R (in Ref. 4; CAG33013)"
FT /evidence="ECO:0000305"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:2VAC"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2VAC"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:2VAC"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:2VAC"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2VAC"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:2VAC"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:2VAC"
FT HELIX 95..112
FT /evidence="ECO:0007829|PDB:2VAC"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2VAC"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:2VAC"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2VAC"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:2VAC"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:2W0I"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:2W0I"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:2W0I"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:2W0I"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:2W0I"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2W0I"
FT STRAND 235..245
FT /evidence="ECO:0007829|PDB:2W0I"
FT STRAND 248..258
FT /evidence="ECO:0007829|PDB:2W0I"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:2W0I"
FT HELIX 266..285
FT /evidence="ECO:0007829|PDB:2W0I"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:2W0I"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:2W0I"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:2W0I"
SQ SEQUENCE 349 AA; 39548 MW; 635EF8C04EFCE92B CRC64;
MAHQTGIHAT EELKEFFAKA RAGSVRLIKV VIEDEQLVLG ASQEPVGRWD QDYDRAVLPL
LDAQQPCYLL YRLDSQNAQG FEWLFLAWSP DNSPVRLKML YAATRATVKK EFGGGHIKDE
LFGTVKDDLS FAGYQKHLSS CAAPAPLTSA ERELQQIRIN EVKTEISVES KHQTLQGLAF
PLQPEAQRAL QQLKQKMVNY IQMKLDLERE TIELVHTEPT DVAQLPSRVP RDAARYHFFL
YKHTHEGDPL ESVVFIYSMP GYKCSIKERM LYSSCKSRLL DSVEQDFHLE IAKKIEIGDG
AELTAEFLYD EVHPKQHAFK QAFAKPKGPG GKRGHKRLIR GPGENGDDS
