ARHGI_MOUSE
ID ARHGI_MOUSE Reviewed; 1405 AA.
AC Q6P9R4; E9QK59; Q6A055; Q8BYA4; Q8K227;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Rho guanine nucleotide exchange factor 18;
GN Name=Arhgef18; Synonyms=Kiaa0521;
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 [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 628-1405 (ISOFORM 3).
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-952; SER-961; SER-1336 AND
RP SER-1338, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, 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 [6]
RP IDENTIFICATION (ISOFORM 1).
RX PubMed=29601110; DOI=10.1002/jlb.2ma1017-418rr;
RA Turton K.B., Wilkerson E.M., Hebert A.S., Fogerty F.J., Schira H.M.,
RA Botros F.E., Coon J.J., Mosher D.F.;
RT "Expression of novel 'LOCGEF' isoforms of ARHGEF18 in eosinophils.";
RL J. Leukoc. Biol. 104:135-145(2018).
CC -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA
CC GTPases. May play a role in actin cytoskeleton reorganization in
CC different tissues since its activation induces formation of actin
CC stress fibers. Also acts as a GEF for RAC1, inducing production of
CC reactive oxygen species (ROS). Does not act as a GEF for CDC42. The G
CC protein beta-gamma (Gbetagamma) subunits of heterotrimeric G proteins
CC act as activators, explaining the integrated effects of LPA and other
CC G-protein coupled receptor agonists on actin stress fiber formation,
CC cell shape change and ROS production. Required for EPB41L4B-mediated
CC regulation of the circumferential actomyosin belt in epithelial cells.
CC {ECO:0000250|UniProtKB:Q6ZSZ5}.
CC -!- SUBUNIT: Interacts with SEPT9; interaction may inhibit GEF activity.
CC Interacts with Gbetagamma subunits GNB1 and GNG2 (By similarity).
CC Interacts with EPB41L4B. Interacts with PATJ (via C-terminus).
CC {ECO:0000250|UniProtKB:Q6ZSZ5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZSZ5}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6ZSZ5}. Cell membrane
CC {ECO:0000250|UniProtKB:Q6ZSZ5}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q6ZSZ5}. Note=In unactivated eosinophils,
CC distributed around the cell periphery in the perimembranous region (By
CC similarity). In activated eosinophils, relocates to the tip of the
CC nucleopod, a membrane structure formed during activation when the
CC nucleus moves to one end of the cell, and is also concentrated in
CC membrane protrusions at the opposite end of the cell (By similarity).
CC Localizes to the apical cell membrane in epithelial cells (By
CC similarity). {ECO:0000250|UniProtKB:Q6ZSZ5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6P9R4-4; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P9R4-1; Sequence=VSP_059878;
CC Name=3;
CC IsoId=Q6P9R4-2; Sequence=VSP_059878, VSP_059880;
CC Name=4;
CC IsoId=Q6P9R4-3; Sequence=VSP_059878, VSP_059879;
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DR EMBL; AK041423; BAC30940.1; -; mRNA.
DR EMBL; AC169677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034512; AAH34512.1; -; mRNA.
DR EMBL; BC060639; AAH60639.1; -; mRNA.
DR EMBL; AK172963; BAD32241.1; -; mRNA.
DR CCDS; CCDS22060.1; -. [Q6P9R4-1]
DR RefSeq; NP_598723.3; NM_133962.3. [Q6P9R4-1]
DR PDB; 6BCB; X-ray; 1.40 A; A=686-828.
DR PDBsum; 6BCB; -.
DR AlphaFoldDB; Q6P9R4; -.
DR SMR; Q6P9R4; -.
DR BioGRID; 221794; 17.
DR IntAct; Q6P9R4; 4.
DR STRING; 10090.ENSMUSP00000004684; -.
DR iPTMnet; Q6P9R4; -.
DR PhosphoSitePlus; Q6P9R4; -.
DR EPD; Q6P9R4; -.
DR jPOST; Q6P9R4; -.
DR MaxQB; Q6P9R4; -.
DR PaxDb; Q6P9R4; -.
DR PeptideAtlas; Q6P9R4; -.
DR PRIDE; Q6P9R4; -.
DR ProteomicsDB; 273935; -. [Q6P9R4-4]
DR ProteomicsDB; 273936; -. [Q6P9R4-2]
DR ProteomicsDB; 273937; -. [Q6P9R4-3]
DR Antibodypedia; 24427; 291 antibodies from 31 providers.
DR DNASU; 102098; -.
DR Ensembl; ENSMUST00000004684; ENSMUSP00000004684; ENSMUSG00000004568. [Q6P9R4-1]
DR GeneID; 102098; -.
DR KEGG; mmu:102098; -.
DR UCSC; uc009kri.1; mouse. [Q6P9R4-3]
DR UCSC; uc009krj.1; mouse. [Q6P9R4-4]
DR UCSC; uc009krk.1; mouse. [Q6P9R4-2]
DR CTD; 23370; -.
DR MGI; MGI:2142567; Arhgef18.
DR VEuPathDB; HostDB:ENSMUSG00000004568; -.
DR eggNOG; KOG3520; Eukaryota.
DR GeneTree; ENSGT00940000157375; -.
DR HOGENOM; CLU_002466_0_0_1; -.
DR InParanoid; Q6P9R4; -.
DR PhylomeDB; Q6P9R4; -.
DR TreeFam; TF325887; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 102098; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Arhgef18; mouse.
DR PRO; PR:Q6P9R4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6P9R4; protein.
DR Bgee; ENSMUSG00000004568; Expressed in pigmented layer of retina and 235 other tissues.
DR ExpressionAtlas; Q6P9R4; baseline and differential.
DR Genevisible; Q6P9R4; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0150105; P:protein localization to cell-cell junction; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:MGI.
DR CDD; cd15794; PH_ARHGEF18; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR037744; ARHGEF18_PH.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Guanine-nucleotide releasing factor; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1405
FT /note="Rho guanine nucleotide exchange factor 18"
FT /id="PRO_0000341416"
FT DOMAIN 485..682
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 723..825
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 347..372
FT /note="C2H2-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1084..1181
FT /evidence="ECO:0000255"
FT COMPBIAS 304..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 952
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..384
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_059878"
FT VAR_SEQ 918..1405
FT /note="IEGIQSLICQRHLGSTSSQVEEGSVSAGLPRRAETFGGYDSVGSPSKGGSFK
FT RKVSNSDLRPQDWQGPASSPDSRPCDNSAPSGCCEESPQAVEMPSTESLPTVLELELVH
FT RVQTLSQLLLSLQAVIAQQDSYVEMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQ
FT REERAGVEKLQSQLRQEQQRWERERARQQQELELAGARLQEREGEARQMRQRLDQERTE
FT LERQRQAYQHDLERLREAQRAVDRERERLELLRRFKKQNTVPGALPPEVLAEAQPASHP
FT PSFNGDGLEGHSAPAKAPGTQGSAMLHGTGPDNVERPEVARWDSAPPESRPAKSDVPIQ
FT LLSATNQIQRQTAVQQQIPTKLAASTKGGKEKGSKSRGSQRWESSASFDLKQQLLLSKF
FT IGKDESASRNRRSLSPVLPAAHGSAPASDPCFPAPSPAPAATPPEAFKFGGTSLPPVSP
FT ASSLPTTPLATTDEVSKEDVIFF -> SKLASPLSYAMIFQGGLPGGPKPGSVLYCSPR
FT TTVILLFFIIQGMESSMCNGSTAELYPNPLSTYSTNAPWVTLCSGVGGGGDKA (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_059879"
FT VAR_SEQ 1310..1405
FT /note="ASFDLKQQLLLSKFIGKDESASRNRRSLSPVLPAAHGSAPASDPCFPAPSPA
FT PAATPPEAFKFGGTSLPPVSPASSLPTTPLATTDEVSKEDVIFF -> GELHPTPTTQR
FT SCTPLPVDLSQQHIWNADREADRQAPVCARRQRGSLFQLHFCCDKIP (in isoform
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_059880"
FT CONFLICT 217
FT /note="Q -> H (in Ref. 3; AAH60639)"
FT CONFLICT 437
FT /note="N -> S (in Ref. 1; BAC30940)"
FT CONFLICT 1351
FT /note="S -> P (in Ref. 3; AAH34512)"
FT HELIX 688..698
FT /evidence="ECO:0007829|PDB:6BCB"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:6BCB"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:6BCB"
FT HELIX 715..718
FT /evidence="ECO:0007829|PDB:6BCB"
FT STRAND 724..733
FT /evidence="ECO:0007829|PDB:6BCB"
FT STRAND 739..757
FT /evidence="ECO:0007829|PDB:6BCB"
FT STRAND 760..763
FT /evidence="ECO:0007829|PDB:6BCB"
FT STRAND 771..774
FT /evidence="ECO:0007829|PDB:6BCB"
FT STRAND 779..783
FT /evidence="ECO:0007829|PDB:6BCB"
FT STRAND 786..794
FT /evidence="ECO:0007829|PDB:6BCB"
FT STRAND 801..806
FT /evidence="ECO:0007829|PDB:6BCB"
FT HELIX 810..825
FT /evidence="ECO:0007829|PDB:6BCB"
SQ SEQUENCE 1405 AA; 155982 MW; AD2ACACC62F31FEE CRC64;
MGSEPKPYAQ PLDSAAAAST TKGSCGPRKP ENPDFFSTVE DEQEDGFLRH LSESTEDFSL
DMGALQGSEY LRDLGLGAPS DLHQSEVIMD PETHRQEARR ESSHTSCEGA SALPQRRSWE
RSRSCSGSCR RLSLDASTVD KGACLPRTLA SLALNLSGNG QKIWTQGCLP VSGTPAPSSK
ECSSPEKRLR SKSVPVSCEI SCMELASDSD VCTSPVQGLE PPVLECLEKD HVEPEHVLIV
QQVLQELRQY HGARQRARMS TSPGGAHSNL TWFEFLSESE DGACKIEKPG KSTRVKRSLS
SLRSRVTRQK EKGKSPAHLK DKTQDLPGKR ECVNGHQLMR GTFSGHSSCP LCGEPLLNSA
SLKEHPRTTL LSDGSSPAPS RNVGMTISQK GGLQPTPSPA GSGVRLGPIA GDMDEADSVF
LKLKQTADDS LSLTSSNAES VFIEDPYIAS LRCEIESDAH EFEAESWSLS VDLAYAKKQK
KEVVKRQDVL YELMQTEAHH VRTLKIMLKV YSRALQEELQ FSGQAVSRLF PCADDLLDMH
SHFLARLKER RQEFLEEGSD RNYVIQKIGD VLVQQFSGET GERMKEKYAV FCSGHNDAVG
QYKLLLQQSK KFQNLIKKIG NFSIVRRLGV QECILLVTQR ITKYPVLVER IIQNTEAGTE
DYKDLSQALS LIKDIISQVD AKVSEYEKDQ RLKEIAAKTD QKSSGKLKNG LTFRKEDMLQ
QRQLHLEGAL CWKSTSGRLK DVLAVLLTDV LLLLQEKDQK YVFASVDSKP PVISLQKLIV
REVANEEKAM FLISASMQGP EMYEMYTSSK EDRNIWMAHI RRAVESCPDE EEDVFSEAEE
KKIAEARTMK LQEFQERLSL KDQLIAQSLL EKQQIYLEMA QLSGLEESAQ NRGLFRGGGD
PSETLRGEQI LRSAMSEIEG IQSLICQRHL GSTSSQVEEG SVSAGLPRRA ETFGGYDSVG
SPSKGGSFKR KVSNSDLRPQ DWQGPASSPD SRPCDNSAPS GCCEESPQAV EMPSTESLPT
VLELELVHRV QTLSQLLLSL QAVIAQQDSY VEMQRTAIQE REKQFRLQST RGNLLLEQER
QRNFEKQREE RAGVEKLQSQ LRQEQQRWER ERARQQQELE LAGARLQERE GEARQMRQRL
DQERTELERQ RQAYQHDLER LREAQRAVDR ERERLELLRR FKKQNTVPGA LPPEVLAEAQ
PASHPPSFNG DGLEGHSAPA KAPGTQGSAM LHGTGPDNVE RPEVARWDSA PPESRPAKSD
VPIQLLSATN QIQRQTAVQQ QIPTKLAAST KGGKEKGSKS RGSQRWESSA SFDLKQQLLL
SKFIGKDESA SRNRRSLSPV LPAAHGSAPA SDPCFPAPSP APAATPPEAF KFGGTSLPPV
SPASSLPTTP LATTDEVSKE DVIFF
