RHG06_MOUSE
ID RHG06_MOUSE Reviewed; 987 AA.
AC O54834; A2ABW4; A2AC55; Q3TMC2; Q8BG83; Q8C842; Q9QZL8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Rho GTPase-activating protein 6;
DE AltName: Full=Rho-type GTPase-activating protein 6;
DE AltName: Full=Rho-type GTPase-activating protein RhoGAPX-1;
GN Name=Arhgap6;
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] (ISOFORMS 1 AND 2), AND SEQUENCE REVISION TO
RP 600-601.
RC STRAIN=129/Sv;
RX PubMed=10699171; DOI=10.1093/hmg/9.4.477;
RA Prakash S.K., Paylor R., Jenna S., Lamarche-Vane N., Armstrong D.L., Xu B.,
RA Mancini M.A., Zoghbi H.Y.;
RT "Functional analysis of ARHGAP6, a novel GTPase-activating protein for
RT RhoA.";
RL Hum. Mol. Genet. 9:477-488(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Head, Lung, and Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 280-660 (ISOFORM 1).
RC STRAIN=129/Sv;
RX PubMed=9417914; DOI=10.1006/geno.1997.5040;
RA Schaefer L., Prakash S.K., Zoghbi H.Y.;
RT "Cloning and characterization of a novel rho-type GTPase-activating protein
RT gene (ARHGAP6) from the critical region for microphthalmia with linear skin
RT defects.";
RL Genomics 46:268-277(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-669; SER-675; SER-713
RP AND SER-824, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, 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).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. Could regulate the interactions of
CC signaling molecules with the actin cytoskeleton. Promotes continuous
CC elongation of cytoplasmic processes during cell motility and
CC simultaneous retraction of the cell body changing the cell morphology
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O54834-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O54834-2; Sequence=VSP_001643, VSP_001644;
CC Name=3;
CC IsoId=O54834-3; Sequence=VSP_026052, VSP_026053;
CC Name=4;
CC IsoId=O54834-4; Sequence=VSP_026051;
CC -!- TISSUE SPECIFICITY: Expressed in retina and lung.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33263.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC37093.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF012273; AAC53522.2; -; mRNA.
DR EMBL; AF177664; AAD55086.1; -; mRNA.
DR EMBL; AK048162; BAC33263.1; ALT_INIT; mRNA.
DR EMBL; AK048507; BAC33352.1; -; mRNA.
DR EMBL; AK077996; BAC37093.1; ALT_INIT; mRNA.
DR EMBL; AK166015; BAE38520.1; -; mRNA.
DR EMBL; AL663026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL663056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL805974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30534.1; -. [O54834-1]
DR CCDS; CCDS41212.1; -. [O54834-3]
DR CCDS; CCDS72472.1; -. [O54834-4]
DR RefSeq; NP_001274459.1; NM_001287530.1. [O54834-4]
DR RefSeq; NP_033837.2; NM_009707.4. [O54834-1]
DR RefSeq; NP_848869.1; NM_178754.3. [O54834-3]
DR RefSeq; XP_006528757.1; XM_006528694.1. [O54834-1]
DR RefSeq; XP_011246085.1; XM_011247783.1. [O54834-2]
DR AlphaFoldDB; O54834; -.
DR SMR; O54834; -.
DR BioGRID; 198200; 16.
DR IntAct; O54834; 7.
DR STRING; 10090.ENSMUSP00000033721; -.
DR iPTMnet; O54834; -.
DR PhosphoSitePlus; O54834; -.
DR MaxQB; O54834; -.
DR PaxDb; O54834; -.
DR PeptideAtlas; O54834; -.
DR PRIDE; O54834; -.
DR ProteomicsDB; 254865; -. [O54834-1]
DR ProteomicsDB; 254866; -. [O54834-2]
DR ProteomicsDB; 254867; -. [O54834-3]
DR ProteomicsDB; 254868; -. [O54834-4]
DR Antibodypedia; 23727; 67 antibodies from 21 providers.
DR DNASU; 11856; -.
DR Ensembl; ENSMUST00000033721; ENSMUSP00000033721; ENSMUSG00000031355. [O54834-1]
DR Ensembl; ENSMUST00000112127; ENSMUSP00000107755; ENSMUSG00000031355. [O54834-4]
DR Ensembl; ENSMUST00000112131; ENSMUSP00000107759; ENSMUSG00000031355. [O54834-3]
DR GeneID; 11856; -.
DR KEGG; mmu:11856; -.
DR UCSC; uc009uxj.2; mouse. [O54834-1]
DR UCSC; uc009uxo.2; mouse. [O54834-3]
DR UCSC; uc009uxq.2; mouse. [O54834-4]
DR CTD; 395; -.
DR MGI; MGI:1196332; Arhgap6.
DR VEuPathDB; HostDB:ENSMUSG00000031355; -.
DR eggNOG; KOG2710; Eukaryota.
DR GeneTree; ENSGT00940000153904; -.
DR HOGENOM; CLU_012874_0_0_1; -.
DR InParanoid; O54834; -.
DR OMA; GPEQYML; -.
DR OrthoDB; 419555at2759; -.
DR PhylomeDB; O54834; -.
DR TreeFam; TF316710; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 11856; 2 hits in 40 CRISPR screens.
DR ChiTaRS; Arhgap6; mouse.
DR PRO; PR:O54834; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O54834; protein.
DR Bgee; ENSMUSG00000031355; Expressed in lateral septal nucleus and 204 other tissues.
DR ExpressionAtlas; O54834; baseline and differential.
DR Genevisible; O54834; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0016004; F:phospholipase activator activity; ISO:MGI.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IDA:MGI.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISO:MGI.
DR GO; GO:0048041; P:focal adhesion assembly; IDA:MGI.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:BHF-UCL.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; ISO:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04376; RhoGAP_ARHGAP6; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR041852; ARHGAP6_RhoGAP.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR030772; RhoGAP6.
DR InterPro; IPR037863; RHOGAP6/36.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR12635; PTHR12635; 1.
DR PANTHER; PTHR12635:SF6; PTHR12635:SF6; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome; SH3-binding.
FT CHAIN 1..987
FT /note="Rho GTPase-activating protein 6"
FT /id="PRO_0000056705"
FT DOMAIN 403..604
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 344..354
FT /note="SH3-binding"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43182"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43182"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43182"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43182"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43182"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43182"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43182"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43182"
FT MOD_RES 944
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43182"
FT VAR_SEQ 1..197
FT /note="MSAQSLLHSVFSCSSPASGGTASAKGFSKRKLRQTRSLDPALIGGCGSEMGA
FT EGGLRGSTVSRLHSPQLLAEGLGSRLASSPRSQHLRATRFQTPRPLCSSFSTPSTPQEK
FT SPSGSFHFDYEVPLSRSGLKKSMAWDLPSVLAGSGSASSRSPASILSSSGGGPNGIFSS
FT PRRWLQQRKFQPPPNSRSHPYVVWRSE -> MYKIF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026051"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026052"
FT VAR_SEQ 59..197
FT /note="STVSRLHSPQLLAEGLGSRLASSPRSQHLRATRFQTPRPLCSSFSTPSTPQE
FT KSPSGSFHFDYEVPLSRSGLKKSMAWDLPSVLAGSGSASSRSPASILSSSGGGPNGIFS
FT SPRRWLQQRKFQPPPNSRSHPYVVWRSE -> MGDPSYSEKPRLHYA (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026053"
FT VAR_SEQ 639..660
FT /note="SPDILQTEVSFSMGGRHSSTDS -> TSSVLPAAGQACSQSPASDFTP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10699171"
FT /id="VSP_001643"
FT VAR_SEQ 661..987
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10699171"
FT /id="VSP_001644"
FT CONFLICT 58..63
FT /note="GSTVSR -> AHSKP (in Ref. 1; AAC53522/AAD55086)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="K -> N (in Ref. 1; AAC53522/AAD55086)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="L -> V (in Ref. 1; AAC53522/AAD55086)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="K -> N (in Ref. 1; AAC53522/AAD55086)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="L -> P (in Ref. 2; BAE38520)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="S -> P (in Ref. 2; BAE38520)"
FT /evidence="ECO:0000305"
FT CONFLICT 601..602
FT /note="EA -> DS (in Ref. 1; AAC53522/AAD55086)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="S -> F (in Ref. 1; AAC53522)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="P -> S (in Ref. 1; AAC53522)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="P -> Q (in Ref. 2; BAE38520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 987 AA; 108844 MW; B621845ECF1C7EBD CRC64;
MSAQSLLHSV FSCSSPASGG TASAKGFSKR KLRQTRSLDP ALIGGCGSEM GAEGGLRGST
VSRLHSPQLL AEGLGSRLAS SPRSQHLRAT RFQTPRPLCS SFSTPSTPQE KSPSGSFHFD
YEVPLSRSGL KKSMAWDLPS VLAGSGSASS RSPASILSSS GGGPNGIFSS PRRWLQQRKF
QPPPNSRSHP YVVWRSEGDF TWNSMSGRSV RLRSVPIQSL SELERARLQE VAFYQLQQDC
DLGCQITIPK DGQKRKKSLR KKLDSLGKEK NKDKEFIPQA FGMPLSQVIA NDRAYKLKQD
LQREEQKDAS SDFVSSLLPF GNKKQNKELS SSNSSLSSTS ETPNESTSPN TPEPAPRARR
RGAMSVDSIT DLDDNQSRLL EALQLSLPAE AQSKKEKARD KKLSLNPIYR QVPRLVDSCC
QHLEKHGLQT VGIFRVGSSK KRVRQLREEF DRGVDVCLEE EHSVHDVAAL LKEFLRDMPD
PLLTRELYTA FINTLLLEPE EQLGTLQLLI YLLPPCNCDT LHRLLQFLSI VARHADDNVS
KDGQEVTGNK MTSLNLATIF GPNLLHKQKS SDKEYSVQSS ARAEESTAII AVVQKMIENY
EALFMVPPDL QNEVLISLLE TDPDVVDYLL RRKASQSSSP DILQTEVSFS MGGRHSSTDS
NKASSGDISP YDNNSPVLSE RSLLAMQEDR ARGGSEKLYK VPEQYTLVGH LSSPKSKSRE
SSPGPRLGKE MSEEPFNIWG TWHSTLKSGS KDPGMTGSYG DIFESSSLRP RPCSLSQGNL
SLNWPRCQGS PTGLDSGTQV IRRTQTAATV EQCSVHLPVS RVCSTPHIQD GSRGTRRPAA
SSDPFLSLNS TEDLAEGKED VAWLQSQARP VYQRPQESGK DDRRPPPPYP GSGKPATTSA
QLPLEPPLWR LQRHEEGSET AVEGGQQASG EHQTRPKKLS SAYSLSASEQ DKQNLGEASW
LDWQRERWQI WELLSTDNPD ALPETLV
