IQGA3_HUMAN
ID IQGA3_HUMAN Reviewed; 1631 AA.
AC Q86VI3; Q5T3H8;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ras GTPase-activating-like protein IQGAP3;
GN Name=IQGAP3;
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], AND VARIANTS GLY-391 AND CYS-663.
RC TISSUE=Embryonic kidney;
RA Fukata M., Watanabe T., Noritake J., Kaibuchi K.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-391 AND CYS-663.
RA Jinawath N., Furukawa Y., Nakamura Y.;
RT "Isolation of a novel human gene up-regulated in diffuse-type gastric
RT cancer.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-1631.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1424, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539 AND SER-1424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1424, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 1529-1631.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the RGC domain of IQGAP3.";
RL Submitted (SEP-2009) to the PDB data bank.
CC -!- INTERACTION:
CC Q86VI3; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1237354, EBI-10976677;
CC Q86VI3; P22607: FGFR3; NbExp=3; IntAct=EBI-1237354, EBI-348399;
CC Q86VI3; P06396: GSN; NbExp=3; IntAct=EBI-1237354, EBI-351506;
CC Q86VI3; O14901: KLF11; NbExp=3; IntAct=EBI-1237354, EBI-948266;
CC Q86VI3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1237354, EBI-5235340;
CC Q86VI3; Q9Y649; NbExp=3; IntAct=EBI-1237354, EBI-25900580;
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DR EMBL; AY253300; AAP06954.1; -; mRNA.
DR EMBL; AB105103; BAC78211.1; -; mRNA.
DR EMBL; AL365181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122653; BAC85501.1; -; mRNA.
DR CCDS; CCDS1144.1; -.
DR RefSeq; NP_839943.2; NM_178229.4.
DR PDB; 3ISU; X-ray; 1.88 A; A=1529-1631.
DR PDBsum; 3ISU; -.
DR AlphaFoldDB; Q86VI3; -.
DR SMR; Q86VI3; -.
DR BioGRID; 126102; 154.
DR IntAct; Q86VI3; 41.
DR MINT; Q86VI3; -.
DR STRING; 9606.ENSP00000354451; -.
DR GlyGen; Q86VI3; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q86VI3; -.
DR PhosphoSitePlus; Q86VI3; -.
DR BioMuta; IQGAP3; -.
DR DMDM; 229462887; -.
DR EPD; Q86VI3; -.
DR jPOST; Q86VI3; -.
DR MassIVE; Q86VI3; -.
DR MaxQB; Q86VI3; -.
DR PaxDb; Q86VI3; -.
DR PeptideAtlas; Q86VI3; -.
DR PRIDE; Q86VI3; -.
DR ProteomicsDB; 70023; -.
DR Antibodypedia; 34218; 179 antibodies from 25 providers.
DR DNASU; 128239; -.
DR Ensembl; ENST00000361170.7; ENSP00000354451.2; ENSG00000183856.11.
DR GeneID; 128239; -.
DR KEGG; hsa:128239; -.
DR MANE-Select; ENST00000361170.7; ENSP00000354451.2; NM_178229.5; NP_839943.3.
DR UCSC; uc001fpf.4; human.
DR CTD; 128239; -.
DR DisGeNET; 128239; -.
DR GeneCards; IQGAP3; -.
DR HGNC; HGNC:20669; IQGAP3.
DR HPA; ENSG00000183856; Tissue enhanced (bone).
DR neXtProt; NX_Q86VI3; -.
DR OpenTargets; ENSG00000183856; -.
DR PharmGKB; PA134954177; -.
DR VEuPathDB; HostDB:ENSG00000183856; -.
DR eggNOG; KOG2128; Eukaryota.
DR GeneTree; ENSGT00950000183076; -.
DR HOGENOM; CLU_000972_2_1_1; -.
DR InParanoid; Q86VI3; -.
DR OMA; QHNMKDG; -.
DR OrthoDB; 674320at2759; -.
DR PhylomeDB; Q86VI3; -.
DR TreeFam; TF313078; -.
DR PathwayCommons; Q86VI3; -.
DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR SignaLink; Q86VI3; -.
DR BioGRID-ORCS; 128239; 19 hits in 1082 CRISPR screens.
DR ChiTaRS; IQGAP3; human.
DR EvolutionaryTrace; Q86VI3; -.
DR GenomeRNAi; 128239; -.
DR Pharos; Q86VI3; Tbio.
DR PRO; PR:Q86VI3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86VI3; protein.
DR Bgee; ENSG00000183856; Expressed in buccal mucosa cell and 142 other tissues.
DR ExpressionAtlas; Q86VI3; baseline and differential.
DR Genevisible; Q86VI3; HS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0070856; F:myosin VI light chain binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR CDD; cd00014; CH; 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; IPR000593; RasGAP_C.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1631
FT /note="Ras GTPase-activating-like protein IQGAP3"
FT /id="PRO_0000056651"
FT DOMAIN 34..149
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 730..759
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 760..789
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 790..819
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 820..849
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 988..1221
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT MOD_RES 162
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKF1"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VARIANT 391
FT /note="R -> G (in dbSNP:rs2488269)"
FT /evidence="ECO:0000269|Ref.1, ECO:0000269|Ref.2"
FT /id="VAR_055278"
FT VARIANT 410
FT /note="V -> L (in dbSNP:rs11264498)"
FT /id="VAR_055279"
FT VARIANT 645
FT /note="D -> N (in dbSNP:rs11264496)"
FT /id="VAR_055280"
FT VARIANT 663
FT /note="R -> C (in dbSNP:rs744224)"
FT /evidence="ECO:0000269|Ref.1, ECO:0000269|Ref.2"
FT /id="VAR_055281"
FT VARIANT 770
FT /note="H -> Y (in dbSNP:rs1078890)"
FT /id="VAR_055282"
FT VARIANT 1061
FT /note="Q -> H (in dbSNP:rs11804414)"
FT /id="VAR_055283"
FT VARIANT 1097
FT /note="P -> S (in dbSNP:rs12562301)"
FT /id="VAR_055284"
FT CONFLICT 610
FT /note="A -> S (in Ref. 4; BAC85501)"
FT /evidence="ECO:0000305"
FT STRAND 1535..1538
FT /evidence="ECO:0007829|PDB:3ISU"
FT HELIX 1539..1544
FT /evidence="ECO:0007829|PDB:3ISU"
FT STRAND 1547..1551
FT /evidence="ECO:0007829|PDB:3ISU"
FT HELIX 1556..1561
FT /evidence="ECO:0007829|PDB:3ISU"
FT STRAND 1562..1568
FT /evidence="ECO:0007829|PDB:3ISU"
FT STRAND 1574..1581
FT /evidence="ECO:0007829|PDB:3ISU"
FT STRAND 1589..1592
FT /evidence="ECO:0007829|PDB:3ISU"
FT HELIX 1593..1601
FT /evidence="ECO:0007829|PDB:3ISU"
FT STRAND 1606..1609
FT /evidence="ECO:0007829|PDB:3ISU"
FT TURN 1610..1612
FT /evidence="ECO:0007829|PDB:3ISU"
FT STRAND 1613..1616
FT /evidence="ECO:0007829|PDB:3ISU"
FT HELIX 1617..1627
FT /evidence="ECO:0007829|PDB:3ISU"
SQ SEQUENCE 1631 AA; 184699 MW; 93480B30076470DA CRC64;
MERRAAGPGW AAYERLTAEE MDEQRRQNVA YQYLCRLEEA KRWMEACLKE ELPSPVELEE
SLRNGVLLAK LGHCFAPSVV PLKKIYDVEQ LRYQATGLHF RHTDNINFWL SAIAHIGLPS
TFFPETTDIY DKKNMPRVVY CIHALSLFLF RLGLAPQIHD LYGKVKFTAE ELSNMASELA
KYGLQLPAFS KIGGILANEL SVDEAAVHAA VLAINEAVER GVVEDTLAAL QNPSALLENL
REPLAAVYQE MLAQAKMEKA ANARNHDDRE SQDIYDHYLT QAEIQGNINH VNVHGALEVV
DDALERQSPE ALLKALQDPA LALRGVRRDF ADWYLEQLNS DREQKAQELG LVELLEKEEV
QAGVAAANTK GDQEQAMLHA VQRINKAIRR RVAADTVKEL MCPEAQLPPV YPVASSMYQL
ELAVLQQQQG ELGQEELFVA VEMLSAVVLI NRALEARDAS GFWSSLVNPA TGLAEVEGEN
AQRYFDALLK LRQERGMGED FLSWNDLQAT VSQVNAQTQE ETDRVLAVSL INEALDKGSP
EKTLSALLLP AAGLDDVSLP VAPRYHLLLV AAKRQKAQVT GDPGAVLWLE EIRQGVVRAN
QDTNTAQRMA LGVAAINQAI KEGKAAQTER VLRNPAVALR GVVPDCANGY QRALESAMAK
KQRPADTAFW VQHDMKDGTA YYFHLQTFQG IWEQPPGCPL NTSHLTREEI QSAVTKVTAA
YDRQQLWKAN VGFVIQLQAR LRGFLVRQKF AEHSHFLRTW LPAVIKIQAH WRGYRQRKIY
LEWLQYFKAN LDAIIKIQAW ARMWAARRQY LRRLHYFQKN VNSIVKIQAF FRARKAQDDY
RILVHAPHPP LSVVRRFAHL LNQSQQDFLA EAELLKLQEE VVRKIRSNQQ LEQDLNIMDI
KIGLLVKNRI TLQEVVSHCK KLTKRNKEQL SDMMVLDKQK GLKSLSKEKR QKLEAYQHLF
YLLQTQPIYL AKLIFQMPQN KTTKFMEAVI FSLYNYASSR REAYLLLQLF KTALQEEIKS
KVEQPQDVVT GNPTVVRLVV RFYRNGRGQS ALQEILGKVI QDVLEDKVLS VHTDPVHLYK
NWINQTEAQT GQRSHLPYDV TPEQALSHPE VQRRLDIALR NLLAMTDKFL LAITSSVDQI
PYGMRYVAKV LKATLAEKFP DATDSEVYKV VGNLLYYRFL NPAVVAPDAF DIVAMAAGGA
LAAPQRHALG AVAQLLQHAA AGKAFSGQSQ HLRVLNDYLE ETHLKFRKFI HRACQVPEPE
ERFAVDEYSD MVAVAKPMVY ITVGELVNTH RLLLEHQDCI APDHQDPLHE LLEDLGELPT
IPDLIGESIA ADGHTDLSKL EVSLTLTNKF EGLEADADDS NTRSLLLSTK QLLADIIQFH
PGDTLKEILS LSASREQEAA HKQLMSRRQA CTAQTPEPLR RHRSLTAHSL LPLAEKQRRV
LRNLRRLEAL GLVSARNGYQ GLVDELAKDI RNQHRHRHRR KAELVKLQAT LQGLSTKTTF
YEEQGDYYSQ YIRACLDHLA PDSKSSGKGK KQPSLHYTAA QLLEKGVLVE IEDLPASHFR
NVIFDITPGD EAGKFEVNAK FLGVDMERFQ LHYQDLLQLQ YEGVAVMKLF NKAKVNVNLL
IFLLNKKFLR K
