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   27-MAR-2024, entry version 195.
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,
RC   Pancreas, 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).
RN   [10]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SLC26A4.
RX   PubMed=35601831; DOI=10.3389/fmolb.2022.874186;
RA   Xu J., Barone S., Varasteh Kia M., Holliday L.S., Zahedi K., Soleimani M.;
RT   "Identification of IQGAP1 as a SLC26A4 (Pendrin)-Binding Protein in the
RT   Kidney.";
RL   Front. Mol. Biosci. 9:874186-874186(2022).
RN   [11]
RP   INTERACTION WITH SVEP1.
RX   PubMed=36792666; DOI=10.1038/s41467-023-36486-0;
RA   Elenbaas J.S., Pudupakkam U., Ashworth K.J., Kang C.J., Patel V.,
RA   Santana K., Jung I.H., Lee P.C., Burks K.H., Amrute J.M., Mecham R.P.,
RA   Halabi C.M., Alisio A., Di Paola J., Stitziel N.O.;
RT   "SVEP1 is an endogenous ligand for the orphan receptor PEAR1.";
RL   Nat. Commun. 14:850-850(2023).
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). Interacts with SLC26A4 (PubMed:35601831). This
CC       interaction enhances the chloride-bicarbonate exchange activity of
CC       SLC26A4 (By similarity). Interacts with SVEP1 (PubMed:36792666).
CC       {ECO:0000250|UniProtKB:P46940, ECO:0000269|PubMed:16968698,
CC       ECO:0000269|PubMed:28089576, ECO:0000269|PubMed:35601831,
CC       ECO:0000269|PubMed:36792666}.
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}. Apical cell membrane
CC       {ECO:0000269|PubMed:35601831}. Basolateral cell membrane
CC       {ECO:0000269|PubMed:35601831}. Note=Subcellular distribution is
CC       regulated by the cell cycle, nuclear levels increase at G1/S phase
CC       (PubMed:20883816).
CC   -!- TISSUE SPECIFICITY: Expressed in the kidney (at protein level).
CC       {ECO:0000269|PubMed:35601831}.
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   GlyGen; Q9JKF1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9JKF1; -.
DR   MetOSite; Q9JKF1; -.
DR   PhosphoSitePlus; Q9JKF1; -.
DR   SwissPalm; Q9JKF1; -.
DR   CPTAC; non-CPTAC-3584; -.
DR   EPD; Q9JKF1; -.
DR   jPOST; Q9JKF1; -.
DR   MaxQB; Q9JKF1; -.
DR   PaxDb; 10090-ENSMUSP00000128278; -.
DR   PeptideAtlas; Q9JKF1; -.
DR   ProteomicsDB; 301668; -.
DR   Pumba; Q9JKF1; -.
DR   Antibodypedia; 2891; 497 antibodies from 41 providers.
DR   DNASU; 29875; -.
DR   Ensembl; ENSMUST00000167377.3; ENSMUSP00000128278.2; ENSMUSG00000030536.11.
DR   GeneID; 29875; -.
DR   KEGG; mmu:29875; -.
DR   UCSC; uc009ibc.2; mouse.
DR   AGR; MGI:1352757; -.
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; KGVLVHW; -.
DR   OrthoDB; 12619at2759; -.
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-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 80 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 273 other cell types or tissues.
DR   ExpressionAtlas; Q9JKF1; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
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:0009898; C: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:0005874; C:microtubule; 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:1903479; P:mitotic actomyosin contractile ring assembly actin filament organization; IBA:GO_Central.
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: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:0001817; P:regulation of cytokine production; IMP:MGI.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
DR   CDD; cd21274; CH_IQGAP1; 1.
DR   CDD; cd05133; RasGAP_IQGAP1; 1.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR   InterPro; IPR001715; CH_dom.
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   PANTHER; PTHR14149; RAS GTPASE-ACTIVATING PROTEIN WITH IQ MOTIF; 1.
DR   PANTHER; PTHR14149:SF15; RAS GTPASE-ACTIVATING-LIKE PROTEIN IQGAP1; 1.
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; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF143885; RGC domain-like; 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.
DR   Genevisible; Q9JKF1; MM.
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
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