IQGA1_MOUSE
ID IQGA1_MOUSE Reviewed; 1657 AA.
AC Q9JKF1; G3UW45;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Ras GTPase-activating-like protein IQGAP1;
GN Name=Iqgap1;
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].
RC TISSUE=Pre-B cell;
RA Bernards A.;
RT "Sequence of Mus musculus Cdc42 effector protein IQGAP1.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-172, 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 [5]
RP INTERACTION WITH CDC42.
RX PubMed=16968698; DOI=10.1074/jbc.m606248200;
RA Lin Q., Yang W., Baird D., Feng Q., Cerione R.A.;
RT "Identification of a DOCK180-related guanine nucleotide exchange factor
RT that is capable of mediating a positive feedback activation of Cdc42.";
RL J. Biol. Chem. 281:35253-35262(2006).
RN [6]
RP INTERACTION WITH S.TYPHIMURIUM SSEI (MICROBIAL INFECTION).
RX PubMed=19956712; DOI=10.1371/journal.ppat.1000671;
RA McLaughlin L.M., Govoni G.R., Gerke C., Gopinath S., Peng K., Laidlaw G.,
RA Chien Y.H., Jeong H.W., Li Z., Brown M.D., Sacks D.B., Monack D.;
RT "The Salmonella SPI2 effector SseI mediates long-term systemic infection by
RT modulating host cell migration.";
RL PLoS Pathog. 5:E1000671-E1000671(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=20883816; DOI=10.1016/j.biocel.2010.09.014;
RA Johnson M., Sharma M., Brocardo M.G., Henderson B.R.;
RT "IQGAP1 translocates to the nucleus in early S-phase and contributes to
RT cell cycle progression after DNA replication arrest.";
RL Int. J. Biochem. Cell Biol. 43:65-73(2011).
RN [9]
RP INTERACTION WITH PJVK.
RX PubMed=28089576; DOI=10.1016/j.neuroscience.2016.12.055;
RA Harris S.L., Kazmierczak M., Pangrsic T., Shah P., Chuchvara N.,
RA Barrantes-Freer A., Moser T., Schwander M.;
RT "Conditional deletion of pejvakin in adult outer hair cells causes
RT progressive hearing loss in mice.";
RL Neuroscience 344:380-393(2017).
CC -!- FUNCTION: Plays a crucial role in regulating the dynamics and assembly
CC of the actin cytoskeleton. Binds to activated CDC42 but does not
CC stimulate its GTPase activity (PubMed:16968698). It associates with
CC calmodulin. Could serve as an assembly scaffold for the organization of
CC a multimolecular complex that would interface incoming signals to the
CC reorganization of the actin cytoskeleton at the plasma membrane. May
CC promote neurite outgrowth. May play a possible role in cell cycle
CC regulation by contributing to cell cycle progression after DNA
CC replication arrest. {ECO:0000250|UniProtKB:P46940,
CC ECO:0000269|PubMed:16968698}.
CC -!- SUBUNIT: Interacts with CDC42; the interaction is demonstrated with
CC IQGAP1 in GTP-bound and in nucleotide-free state (PubMed:16968698).
CC Interacts with RAC1 (By similarity). Does not interact with RHOA (By
CC similarity). Interacts with TSG101 (By similarity). Interacts with PAK6
CC (By similarity). Interacts with SASH1 (By similarity). Interacts with
CC PJVK (PubMed:28089576). {ECO:0000250|UniProtKB:P46940,
CC ECO:0000269|PubMed:16968698, ECO:0000269|PubMed:28089576}.
CC -!- SUBUNIT: (Microbial infection) In case of infection, interacts with
CC S.typhimurium protein sseI (PubMed:19956712).
CC {ECO:0000269|PubMed:19956712}.
CC -!- INTERACTION:
CC Q9JKF1; P98083: Shc1; NbExp=5; IntAct=EBI-644633, EBI-300201;
CC Q9JKF1; P03332: gag; Xeno; NbExp=17; IntAct=EBI-644633, EBI-935477;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P46940}.
CC Nucleus {ECO:0000269|PubMed:20883816}. Cytoplasm
CC {ECO:0000269|PubMed:20883816}. Note=Subcellular distribution is
CC regulated by the cell cycle, nuclear levels increase at G1/S phase
CC (PubMed:20883816).
CC -!- DEVELOPMENTAL STAGE: Expressed widely in developing cortex.
CC {ECO:0000269|PubMed:20883816}.
CC -!- DOMAIN: Regions C1 and C2 can either interact with nucleotide-free
CC CDC42, or interact together. {ECO:0000250|UniProtKB:P46940}.
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DR EMBL; AF240630; AAF60344.1; -; mRNA.
DR EMBL; AC109257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466543; EDL06977.1; -; Genomic_DNA.
DR CCDS; CCDS40001.1; -.
DR RefSeq; NP_057930.2; NM_016721.2.
DR AlphaFoldDB; Q9JKF1; -.
DR BMRB; Q9JKF1; -.
DR SMR; Q9JKF1; -.
DR BioGRID; 205938; 78.
DR CORUM; Q9JKF1; -.
DR IntAct; Q9JKF1; 16.
DR MINT; Q9JKF1; -.
DR STRING; 10090.ENSMUSP00000128278; -.
DR iPTMnet; Q9JKF1; -.
DR PhosphoSitePlus; Q9JKF1; -.
DR SwissPalm; Q9JKF1; -.
DR CPTAC; non-CPTAC-3584; -.
DR EPD; Q9JKF1; -.
DR jPOST; Q9JKF1; -.
DR MaxQB; Q9JKF1; -.
DR PaxDb; Q9JKF1; -.
DR PeptideAtlas; Q9JKF1; -.
DR PRIDE; Q9JKF1; -.
DR ProteomicsDB; 301668; -.
DR Antibodypedia; 2891; 422 antibodies from 41 providers.
DR DNASU; 29875; -.
DR Ensembl; ENSMUST00000167377; ENSMUSP00000128278; ENSMUSG00000030536.
DR GeneID; 29875; -.
DR KEGG; mmu:29875; -.
DR UCSC; uc009ibc.2; mouse.
DR CTD; 8826; -.
DR MGI; MGI:1352757; Iqgap1.
DR VEuPathDB; HostDB:ENSMUSG00000030536; -.
DR eggNOG; KOG2128; Eukaryota.
DR GeneTree; ENSGT00950000183076; -.
DR HOGENOM; CLU_000972_2_1_1; -.
DR InParanoid; Q9JKF1; -.
DR OMA; HQKHFGG; -.
DR OrthoDB; 674320at2759; -.
DR PhylomeDB; Q9JKF1; -.
DR TreeFam; TF313078; -.
DR Reactome; R-MMU-373753; Nephrin family interactions.
DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 29875; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Iqgap1; mouse.
DR PRO; PR:Q9JKF1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JKF1; protein.
DR Bgee; ENSMUSG00000030536; Expressed in left lung lobe and 269 other tissues.
DR ExpressionAtlas; Q9JKF1; baseline and differential.
DR Genevisible; Q9JKF1; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IPI:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IGI:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0036057; C:slit diaphragm; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISO:MGI.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044548; F:S100 protein binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IPI:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010761; P:fibroblast migration; IGI:MGI.
DR GO; GO:0035305; P:negative regulation of dephosphorylation; IGI:MGI.
DR GO; GO:1990138; P:neuron projection extension; ISO:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0072015; P:podocyte development; ISS:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; ISO:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:BHF-UCL.
DR GO; GO:1903829; P:positive regulation of protein localization; ISO:MGI.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0001817; P:regulation of cytokine production; IMP:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
DR CDD; cd00014; CH; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.10.506.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000593; RasGAP_C.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001202; WW_dom.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF03836; RasGAP_C; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calmodulin-binding; Cell membrane; Cytoplasm; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P46940"
FT CHAIN 2..1657
FT /note="Ras GTPase-activating-like protein IQGAP1"
FT /id="PRO_0000056649"
FT DOMAIN 44..159
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 685..710
FT /note="WW"
FT DOMAIN 745..774
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 775..804
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 805..834
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 835..864
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1004..1237
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT REGION 956..1274
FT /note="C1"
FT REGION 1276..1657
FT /note="C2"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P46940"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46940"
FT MOD_RES 172
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46940"
FT MOD_RES 1441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46940"
FT CONFLICT 1268
FT /note="V -> L (in Ref. 1; AAF60344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1657 AA; 188742 MW; 9136695557ADA784 CRC64;
MSAAEEVDGL GVVRPHYGSV LDNERLTAEE MDERRRQNVA YEYLCHLEEA KRWMEACLGE
DLPPTTELEE GLRNGVYLAK LGNFFSPKVV SLKKIYDREQ TRYKATGLHF RHTDNVIQWL
NAMDEIGLPK IFYPETTDIY DRKNMPRCIY CIHALSLYLF KLGLAPQIQD LYGKVDFTEE
EINNMKIELE KYGIQMPAFS KIGGILANEL SVDEAALHAA VIAINEAIDR RVAADTFTAL
KNPNAMLVNL EEGLAPTYQD VLYQAKQDKM TNAKNRTENS DRERDVYEEL LTQAEIQGNV
NKVNTSSALA NISLALEQGC AVTLLKALQS LALGLRGLQT QNSDWYMKQL QSDLQQKRQS
GQTDPLQKEE VQAGVDAANS AAQQYQRRLA AVAAINAAIQ KGIAEKTVLE LMNPEAQLPQ
VYPFAADLYQ KELATLQQQS PEHSLTHPEL TVAVEMLSSV ALINRALESG DMTTVWKQLS
SSVTGLTNIE EENCQRYLDE LMKLKAQAHA ENNAFITWND IQACVDHVNL VVHEEHERIL
AIGLINEALD EGDAQKTLQA LQIPAAKLEG VLAEVAQHYQ DTLIRAKREK AQETQDESAV
LWLDEIQGGI WQSNKDTQEA QRFALGISAI NEAVDSGDVG RTLSALRSPD VGLYGVIPEC
GETYQSDLAE AKKKRLAAGD NNSKWVKHWV KGGYHYYHNL ETQAGGWAEP PDFVQNSVQL
SREEIQSSIS GVTAAYNREQ LWLANEGLIT KLQACCRGYL VRQEFRSRMN FLKKQIPAIT
CIQSQWRGYK QKKAYQDRLA YLHSHKDEVV KIQSLARMHQ ARKRYRDRLQ YFRDHINDII
KIQAFIRANK ARDDYKTLIN AEDPPMIVVR KFVHLLDQSD QDFQEELDLM KMREEVITLI
RSNQQLENDL NLMDIKIGLL VKNKITLQDV VSHSKKLTKK NKEQLSDMMM INKQKGGLKA
LSKEKREKLE AYQHLFYLLQ TNPTYLAKLI FQMPQNKSTK FMDSVIFTLY NYASNQREEY
LLLRLFQTAL QEEIKSKVDQ IQEIVTGNPT VIKMVVSFNR GARGQNALRQ ILAPVVKEIM
DDKSLNIKTD PVDIYKSWVN QMESQTGEAS KLPYDVTPEQ ALSHEEVKTR LDNSIRNMRA
VTDKFLSAIV SSVDKIPYGM RFIAKVLKDS LHEKFPDAGE DELLKIIGNL LYYRYMNPAI
VAPDAFDIID LSAGGQLTTD QRRNLGSIAK MLQHAASNKM FLGDNAHLSI INEYLSQSYQ
KFRRFFQVAC DVPELQDKFN VDEYSDLVTL TKPVIYISIG EIINTHTLLL DHQDAIAPEH
NDPIHELLDD LGEVPTIESL IGESCGNSND PNKEALAKTE VSLTLTNKFD VPGDENAEMD
ARTILLNTKR LIVDVIRFQP GETLTEILET PATNEQEAEH QRAMQRRAIR DAKTPDKMKK
SKPMKEDNNL SLQEKKEKIQ TGLKKLTELG TVDPKNRYQE LINDIAKDIR NQRRYRQRRK
AELVKLQQTY SALNSKATFY GEQVDYYKSY IKTCLDNLAS KGKVSKKPRE MKGKKSKKIS
LKYTAARLHE KGVLLEIEDL QANQFKNVIF EIGPTEEVGD FEVKAKFMGV QMETFMLHYQ
DLLQLQYEGV AVMKLFDRAK VNVNLLIFLL NKKFYGK
