FMN2_MOUSE
ID FMN2_MOUSE Reviewed; 1578 AA.
AC Q9JL04; Q505D3;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Formin-2;
GN Name=Fmn2;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=10781961; DOI=10.1016/s0925-4773(00)00276-8;
RA Leader B., Leder P.;
RT "Formin-2, a novel formin homology protein of the cappuccino subfamily, is
RT highly expressed in the developing and adult central nervous system.";
RL Mech. Dev. 93:221-231(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12447394; DOI=10.1038/ncb880;
RA Leader B., Lim H., Carabatsos M.J., Harrington A., Ecsedy J., Pellman D.,
RA Maas R., Leder P.;
RT "Formin-2, polyploidy, hypofertility and positioning of the meiotic spindle
RT in mouse oocytes.";
RL Nat. Cell Biol. 4:921-928(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP FUNCTION.
RX PubMed=18848445; DOI=10.1016/j.cub.2008.08.044;
RA Azoury J., Lee K.W., Georget V., Rassinier P., Leader B., Verlhac M.H.;
RT "Spindle positioning in mouse oocytes relies on a dynamic meshwork of actin
RT filaments.";
RL Curr. Biol. 18:1514-1519(2008).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19062278; DOI=10.1016/j.cub.2008.11.022;
RA Schuh M., Ellenberg J.;
RT "A new model for asymmetric spindle positioning in mouse oocytes.";
RL Curr. Biol. 18:1986-1992(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-459; SER-489 AND
RP SER-493, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21620703; DOI=10.1016/j.cub.2011.04.029;
RA Pfender S., Kuznetsov V., Pleiser S., Kerkhoff E., Schuh M.;
RT "Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric
RT oocyte division.";
RL Curr. Biol. 21:955-960(2011).
RN [9]
RP INTERACTION WITH SPIRE1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-1571.
RX PubMed=21705804; DOI=10.1074/jbc.m111.257782;
RA Zeth K., Pechlivanis M., Samol A., Pleiser S., Vonrhein C., Kerkhoff E.;
RT "Molecular basis of actin nucleation factor cooperativity: crystal
RT structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)*formin-2
RT formin SPIR interaction motif (FSI) complex.";
RL J. Biol. Chem. 286:30732-30739(2011).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21983562; DOI=10.1038/ncb2353;
RA Schuh M.;
RT "An actin-dependent mechanism for long-range vesicle transport.";
RL Nat. Cell Biol. 13:1431-1436(2011).
CC -!- FUNCTION: Actin-binding protein that is involved in actin cytoskeleton
CC assembly and reorganization (PubMed:18848445, PubMed:21620703). Acts as
CC an actin nucleation factor and promotes assembly of actin filaments
CC together with SPIRE1 and SPIRE2 (PubMed:18848445, PubMed:21620703).
CC Involved in intracellular vesicle transport along actin fibers,
CC providing a novel link between actin cytoskeleton dynamics and
CC intracellular transport (PubMed:21983562). Required for asymmetric
CC spindle positioning, asymmetric oocyte division and polar body
CC extrusion during female germ cell meiosis (PubMed:12447394,
CC PubMed:18848445, PubMed:19062278, PubMed:21620703). Plays a role in
CC responses to DNA damage, cellular stress and hypoxia by protecting
CC CDKN1A against degradation, and thereby plays a role in stress-induced
CC cell cycle arrest (By similarity). Also acts in the nucleus: together
CC with SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in
CC response to DNA damage in order to facilitate movement of chromatin and
CC repair factors after DNA damage (By similarity). Protects cells against
CC apoptosis by protecting CDKN1A against degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZ56, ECO:0000269|PubMed:12447394,
CC ECO:0000269|PubMed:18848445, ECO:0000269|PubMed:19062278,
CC ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}.
CC -!- SUBUNIT: Interacts with SPIRE1 (PubMed:21705804). Binds actin
CC (PubMed:21705804). Interacts with CDKN1A (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZ56, ECO:0000269|PubMed:21705804}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19062278, ECO:0000269|PubMed:21620703}. Cytoplasm,
CC cytosol {ECO:0000250|UniProtKB:Q9NZ56}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:21620703}. Nucleus {ECO:0000250|UniProtKB:Q9NZ56}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NZ56}. Cell membrane
CC {ECO:0000269|PubMed:21705804}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21705804}; Cytoplasmic side
CC {ECO:0000269|PubMed:21705804}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:21983562}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:21983562}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21983562}; Cytoplasmic side
CC {ECO:0000269|PubMed:21983562}. Note=Colocalizes with the actin
CC cytoskeleton (PubMed:21705804). Recruited to the membranes via its
CC interaction with SPIRE1 (PubMed:21705804). Detected at the cleavage
CC furrow during asymmetric oocyte division and polar body extrusion
CC (PubMed:21620703). Accumulates in the nucleus following DNA damage (By
CC similarity). {ECO:0000250|UniProtKB:Q9NZ56,
CC ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21705804}.
CC -!- TISSUE SPECIFICITY: Detected in brain and in oocytes (at protein level)
CC (PubMed:12447394, PubMed:19062278). Expressed almost exclusively in the
CC developing and mature central nervous system (PubMed:10781961).
CC Detected in oocytes (PubMed:12447394, PubMed:19062278).
CC {ECO:0000269|PubMed:10781961, ECO:0000269|PubMed:12447394,
CC ECO:0000269|PubMed:19062278}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at embryonic day 9.5 in the
CC developing spinal cord and brain structures and continues in neonatal
CC and adult brain structures including the olfactory bulb, cortex,
CC thalamus, hypothalamus, hippocampus and cerebellum.
CC {ECO:0000269|PubMed:10781961}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in male mice, but female
CC mice show reduced fertility and produce at most one to three pups per
CC litter (PubMed:12447394). Female mice display defects in asymmetric
CC spindle positioning, asymmetric cell division and polar body extrusion
CC during oocyte meiosis (PubMed:12447394). During early pregnancy,
CC females present normal numbers of implantation sites, but only very few
CC normal-looking embryos (PubMed:12447394). Most of the embryos show
CC developmental delays and gross morphological defects, leading to
CC embryonic death (PubMed:12447394). {ECO:0000269|PubMed:12447394}.
CC -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC subfamily. {ECO:0000305}.
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DR EMBL; AF218940; AAF72883.1; -; mRNA.
DR EMBL; BC094606; AAH94606.1; -; mRNA.
DR CCDS; CCDS48459.1; -.
DR RefSeq; NP_062318.2; NM_019445.2.
DR AlphaFoldDB; Q9JL04; -.
DR SMR; Q9JL04; -.
DR BioGRID; 207654; 3.
DR DIP; DIP-60685N; -.
DR IntAct; Q9JL04; 2.
DR MINT; Q9JL04; -.
DR STRING; 10090.ENSMUSP00000030039; -.
DR iPTMnet; Q9JL04; -.
DR PhosphoSitePlus; Q9JL04; -.
DR MaxQB; Q9JL04; -.
DR PaxDb; Q9JL04; -.
DR PeptideAtlas; Q9JL04; -.
DR PRIDE; Q9JL04; -.
DR ProteomicsDB; 267605; -.
DR Antibodypedia; 20819; 136 antibodies from 28 providers.
DR DNASU; 54418; -.
DR Ensembl; ENSMUST00000030039; ENSMUSP00000030039; ENSMUSG00000028354.
DR GeneID; 54418; -.
DR KEGG; mmu:54418; -.
DR UCSC; uc007dtd.2; mouse.
DR CTD; 56776; -.
DR MGI; MGI:1859252; Fmn2.
DR VEuPathDB; HostDB:ENSMUSG00000028354; -.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000161899; -.
DR HOGENOM; CLU_002670_2_0_1; -.
DR InParanoid; Q9JL04; -.
DR OMA; DTLQRVC; -.
DR OrthoDB; 249504at2759; -.
DR PhylomeDB; Q9JL04; -.
DR TreeFam; TF326072; -.
DR BioGRID-ORCS; 54418; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Fmn2; mouse.
DR PRO; PR:Q9JL04; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9JL04; protein.
DR Bgee; ENSMUSG00000028354; Expressed in secondary oocyte and 178 other tissues.
DR ExpressionAtlas; Q9JL04; baseline and differential.
DR Genevisible; Q9JL04; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005884; C:actin filament; IEA:InterPro.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:MGI.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; IMP:UniProtKB.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IMP:UniProtKB.
DR GO; GO:0051758; P:homologous chromosome movement towards spindle pole in meiosis I anaphase; IMP:BHF-UCL.
DR GO; GO:0046907; P:intracellular transport; IMP:UniProtKB.
DR GO; GO:0016344; P:meiotic chromosome movement towards spindle pole; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:BHF-UCL.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:BHF-UCL.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
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; Cell membrane; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Developmental protein; DNA damage; Membrane; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Stress response; Transport.
FT CHAIN 1..1578
FT /note="Formin-2"
FT /id="PRO_0000194889"
FT DOMAIN 735..1124
FT /note="FH1"
FT REPEAT 919..929
FT /note="1"
FT REPEAT 930..940
FT /note="2"
FT REPEAT 941..951
FT /note="3"
FT REPEAT 952..962
FT /note="4"
FT REPEAT 963..973
FT /note="5"
FT REPEAT 974..984
FT /note="6"
FT REPEAT 985..995
FT /note="7"
FT REPEAT 996..1006
FT /note="8"
FT REPEAT 1007..1017
FT /note="9"
FT REPEAT 1018..1028
FT /note="10"
FT REPEAT 1029..1039
FT /note="11"
FT REPEAT 1040..1050
FT /note="12"
FT DOMAIN 1139..1554
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..1039
FT /note="12 X 11 AA tandem repeats of [MV]-G-I-P-P-P-P-P-L-P-
FT G"
FT REGION 1037..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1578
FT /note="Important for interaction with SPIRE1"
FT /evidence="ECO:0000269|PubMed:21705804"
FT COILED 643..683
FT /evidence="ECO:0000255"
FT COILED 1419..1455
FT /evidence="ECO:0000255"
FT COMPBIAS 10..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1097
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 1571
FT /note="K->A,E: Strongly reduced interaction with SPIRE1."
FT /evidence="ECO:0000269|PubMed:21705804"
FT CONFLICT 33
FT /note="I -> T (in Ref. 2; AAH94606)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="V -> M (in Ref. 2; AAH94606)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="V -> A (in Ref. 2; AAH94606)"
FT /evidence="ECO:0000305"
FT CONFLICT 430..432
FT /note="RSS -> PSP (in Ref. 2; AAH94606)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="L -> P (in Ref. 2; AAH94606)"
FT /evidence="ECO:0000305"
FT CONFLICT 936..946
FT /note="Missing (in Ref. 2; AAH94606)"
FT /evidence="ECO:0000305"
FT CONFLICT 1040
FT /note="V -> M (in Ref. 2; AAH94606)"
FT /evidence="ECO:0000305"
FT CONFLICT 1142
FT /note="L -> P (in Ref. 2; AAH94606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1578 AA; 167387 MW; DD0FDC8FC25C47DB CRC64;
MGNQDGKLKR SAGDASHEGG GAEDAAGPRD AEITKKASGS KKALGKHGKG GGGSGETSKK
KSKSDSRASV FSNLRIRKNL TKGKGACDSR EDVLDSQALP IGELDSAHSI VTKTPDLSLS
AEETGLSDTE CADPFEVIHP GASRPAEAGV GIQATAEDLE TAAGAQDGQR TSSGSDTDIY
SFHSATEQED LLSDIQQAIR LQQQQQQKLL LQDSEEPAAP PTAISPQPGA FLGLDQFLLG
PRSEAEKDTV QALPVRPDLP ETTKSLVPEH PPSSGSHLTS ETPGYATAPS AVTDSLSSPA
FTFPEAGPGE GAAGVPVAGT GDTDEECEED AFEDAPRGSP GEEWVPEVEE ASQRLEKEPE
EGMRESITSA VVSLPGSPAP SPRCFKPYPL ITPCYIKTTT RQLSSPNHSP SQSPNQSPRI
KKRPDPSVSR SSRTALASAA APAKKHRLEG GLTGGLSRSA DWTEELGVRT PGAGGSVHLL
GRGATADDSG GGSPVLAAKA PGAPATADGF QNVFTGRTLL EKLFSQQENG PPEEAEKFCS
RIIAMGLLLP FSDCFREPCN QNAGSSSAPF DQDQLYTWAA VSQPTHSMDY SEGQFPRREP
SMWPSSKLPE EEPSPKDVDT EPKSSILESP KKCSNGVQQE VFDVKSEGQA TVIQQLEQTI
EDLRTKIAEL EKQYPALDLE GPRGLSGLEN GLTASADVSL DALVLHGKVA QPPRTLEAKS
IQTSPTEEGR ILTLPPPKAP PEGLLGSPAA ASGESALLTS PSGPQTKFCS EISLIVSPRR
ISVQLDAQQI QSASQLPPPP PLLGSDSQGQ PSQPSLHTES ETSHEHSVSS SFGNNCNVPP
APPLPCTESS SFMPGLGMAI PPPPCLSDIT VPALPSPTAP ALQFSNLQGP EMLPAPPQPP
PLPGLGVPPP PPAPPLPGMG IPPPPPLPGM GIPPPPPLPG MGISPLPPLP GMGIPPPPPL
PGVGIPPPPP LPGVGIPPPP PLPGVGIPPP PPLPGVGIPP PPPLPGVGIP PPPPLPGVGI
PPPPPLPGVG IPPPPPLPGV GIPPPPPLPG SGIPPPPALP GVAIPPPPPL PGMGVPPPAP
PPPGAGIPPP PLLPGSGPPH SSQVGSSTLP AAPQGCGFLF PPLPTGLFGL GMNQDRVARK
QLIEPCRPMK PLYWTRIQLH SKRDSSPSLI WEKIEEPSID CHEFEELFSK TAVKERKKPI
SDTISKTKAK QVVKLLSNKR SQAVGILMSS LHLDMKDIQH AVVNLDNSVV DLETLQALYE
NRAQSDELEK IEKHSRSSKD KENAKSLDKP EQFLYELSLI PNFSERVFCI LFQSTFSESI
CSIRRKLELL QKLCETLKNG PGVMQVLGLV LAFGNYMNAG NKTRGQADGF GLDILPKLKD
VKSSDNSRSL LSYIVSYYLR NFDEDAGKEQ CVFPLAEPQE LFQASQMKFE DFQKDLRKLK
KDLKACEAEA GKVYQVSSAE HMQPFKENME QFISQAKIDQ ESQEAALTET HKCFLETTAY
YFMKPKLGEK EVSPNVFFSV WHEFSSDFKD AWKKENKLIL QERVKEAEEV CRQKKGKSLY
KVKPRHDSGI KAKISMKT
