RHG39_HUMAN
ID RHG39_HUMAN Reviewed; 1083 AA.
AC Q9C0H5; B4E1I1;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Rho GTPase-activating protein 39;
GN Name=ARHGAP39; Synonyms=KIAA1688;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 407-1083 (ISOFORM 2).
RC TISSUE=Trachea;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-407, AND
RP IDENTIFICATION BY 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-604, 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-286; SER-407;
RP SER-604 AND SER-690, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C0H5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0H5-2; Sequence=VSP_040749;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21779.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG64793.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB051475; BAB21779.1; ALT_INIT; mRNA.
DR EMBL; AC084125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK303851; BAG64793.1; ALT_INIT; mRNA.
DR CCDS; CCDS34971.1; -. [Q9C0H5-2]
DR CCDS; CCDS78374.1; -. [Q9C0H5-1]
DR PIR; C59434; C59434.
DR RefSeq; NP_001295136.1; NM_001308207.1. [Q9C0H5-1]
DR RefSeq; NP_001295137.1; NM_001308208.1. [Q9C0H5-1]
DR RefSeq; NP_079527.1; NM_025251.2. [Q9C0H5-2]
DR RefSeq; XP_011515610.1; XM_011517308.1. [Q9C0H5-2]
DR RefSeq; XP_011515611.1; XM_011517309.1. [Q9C0H5-2]
DR RefSeq; XP_016869359.1; XM_017013870.1. [Q9C0H5-2]
DR RefSeq; XP_016869360.1; XM_017013871.1.
DR AlphaFoldDB; Q9C0H5; -.
DR SMR; Q9C0H5; -.
DR BioGRID; 123278; 114.
DR IntAct; Q9C0H5; 31.
DR MINT; Q9C0H5; -.
DR STRING; 9606.ENSP00000366522; -.
DR iPTMnet; Q9C0H5; -.
DR PhosphoSitePlus; Q9C0H5; -.
DR BioMuta; ARHGAP39; -.
DR DMDM; 28380079; -.
DR EPD; Q9C0H5; -.
DR jPOST; Q9C0H5; -.
DR MassIVE; Q9C0H5; -.
DR MaxQB; Q9C0H5; -.
DR PaxDb; Q9C0H5; -.
DR PeptideAtlas; Q9C0H5; -.
DR PRIDE; Q9C0H5; -.
DR ProteomicsDB; 80042; -. [Q9C0H5-1]
DR ProteomicsDB; 80043; -. [Q9C0H5-2]
DR Antibodypedia; 49512; 79 antibodies from 21 providers.
DR DNASU; 80728; -.
DR Ensembl; ENST00000276826.5; ENSP00000276826.5; ENSG00000147799.12. [Q9C0H5-1]
DR Ensembl; ENST00000377307.7; ENSP00000366522.2; ENSG00000147799.12. [Q9C0H5-2]
DR GeneID; 80728; -.
DR KEGG; hsa:80728; -.
DR MANE-Select; ENST00000377307.7; ENSP00000366522.2; NM_025251.3; NP_079527.1. [Q9C0H5-2]
DR UCSC; uc064rpe.1; human. [Q9C0H5-1]
DR CTD; 80728; -.
DR DisGeNET; 80728; -.
DR GeneCards; ARHGAP39; -.
DR HGNC; HGNC:29351; ARHGAP39.
DR HPA; ENSG00000147799; Tissue enhanced (testis).
DR MIM; 615880; gene.
DR neXtProt; NX_Q9C0H5; -.
DR OpenTargets; ENSG00000147799; -.
DR PharmGKB; PA165585391; -.
DR VEuPathDB; HostDB:ENSG00000147799; -.
DR eggNOG; ENOG502QR6X; Eukaryota.
DR GeneTree; ENSGT00390000003161; -.
DR HOGENOM; CLU_005171_0_0_1; -.
DR InParanoid; Q9C0H5; -.
DR OMA; FMEVSKW; -.
DR OrthoDB; 1123653at2759; -.
DR PhylomeDB; Q9C0H5; -.
DR TreeFam; TF323577; -.
DR PathwayCommons; Q9C0H5; -.
DR Reactome; R-HSA-428543; Inactivation of CDC42 and RAC1.
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-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q9C0H5; -.
DR SIGNOR; Q9C0H5; -.
DR BioGRID-ORCS; 80728; 9 hits in 1025 CRISPR screens.
DR ChiTaRS; ARHGAP39; human.
DR GenomeRNAi; 80728; -.
DR Pharos; Q9C0H5; Tbio.
DR PRO; PR:Q9C0H5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9C0H5; protein.
DR Bgee; ENSG00000147799; Expressed in sural nerve and 127 other tissues.
DR Genevisible; Q9C0H5; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0099173; P:postsynapse organization; IDA:SynGO.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.25.40.530; -; 1.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00784; MyTH4; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00139; MyTH4; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS51016; MYTH4; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1083
FT /note="Rho GTPase-activating protein 39"
FT /id="PRO_0000076092"
FT DOMAIN 25..58
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 63..97
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 722..879
FT /note="MyTH4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 890..1078
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 110..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59281"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59281"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59281"
FT VAR_SEQ 840
FT /note="K -> KVTQHIKELLERNTKKKSKLRKKPKPYVEEPD (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040749"
SQ SEQUENCE 1083 AA; 121286 MW; 782B213B1DCB4072 CRC64;
MSQTQDYECR SHNVDLPESR IPGSNTRLEW VEIIEPRTRE RMYANLVTGE CVWDPPAGVR
IKRTSENQWW ELFDPNTSRF YYYNASTQRT VWHRPQGCDI IPLAKLQTLK QNTESPRASA
ESSPGRGSSV SREGSTSSSL EPEPDTEKAQ ELPARAGRPA AFGTVKEDSG SSSPPGVFLE
KDYEIYRDYS ADGQLLHYRT SSLRWNSGAK ERMLIKVADR EPSFLAAQGN GYAPDGPPGV
RSRRPSGSQH SPSLQTFAPE ADGTIFFPER RPSPFLKRAE LPGSSSPLLA QPRKPSGDSQ
PSSPRYGYEP PLYEEPPVEY QAPIYDEPPM DVQFEAGGGY QAGSPQRSPG RKPRPFLQPN
KQGPPSPCQQ LVLTKQKCPE RFLSLEYSPA GKEYVRQLVY VEQAGSSPKL RAGPRHKYAP
NPGGGSYSLQ PSPCLLRDQR LGVKSGDYST MEGPELRHSQ PPTPLPQAQE DAMSWSSQQD
TLSSTGYSPG TRKRKSRKPS LCQATSATPT EGPGDLLVEQ PLAEEQPPCG TSLAPVKRAE
GEAEGARGAA EPFLAQARLA WEAQQAHFHM KQRSSWDSQQ DGSGYESDGA LPLPMPGPVV
RAFSEDEALA QQENRHWRRG TFEKLGFPQI LLEKSVSVQT NLASPEPYLH PSQSEDLAAC
AQFESSRQSR SGVPSSSCVF PTFTLRKPSS ETDIENWASK HFNKHTQGLF RRKVSIANML
AWSSESIKKP MIVTSDRHVK KEACELFKLI QMYMGDRRAK ADPLHVALEV ATKGWSVQGL
RDELYIQLCR QTTENFRLES LARGWELMAI CLAFFPPTPK FHSYLEGYIY RHMDPVNDTK
GVAISTYAKY CYHKLQKAAL TGAKKGLKKP NVEEIRHAKN AVFSPSMFGS ALQEVMGMQR
ERYPERQLPW VQTRLSEEVL ALNGDQTEGI FRVPGDIDEV NALKLQVDQW KVPTGLEDPH
VPASLLKLWY RELEEPLIPH EFYEQCIAHY DSPEAAVAVV HALPRINRMV LCYLIRFLQV
FVQPANVAVT KMDVSNLAMV MAPNCLRCQS DDPRVIFENT RKEMSFLRVL IQHLDTSFME
GVL
