ID RHG32_HUMAN Reviewed; 2087 AA. AC A7KAX9; O94820; Q86YL6; Q8IUG4; Q9BWG3; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 14-DEC-2011, entry version 43. DE RecName: Full=Rho GTPase-activating protein 32; DE AltName: Full=Brain-specific Rho GTPase-activating protein; DE AltName: Full=GAB-associated Cdc42/Rac GTPase-activating protein; DE AltName: Full=GC-GAP; DE AltName: Full=GTPase regulator interacting with TrkA; DE AltName: Full=Rho-type GTPase-activating protein 32; DE AltName: Full=Rho/Cdc42/Rac GTPase-activating protein RICS; DE AltName: Full=RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling; DE AltName: Full=p200RhoGAP; DE AltName: Full=p250GAP; GN Name=ARHGAP32; Synonyms=GRIT, KIAA0712, RICS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH RP NTRK1; SHC3; BCAR1; EGFR; CRK AND CRKL, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, PHOSPHORYLATION, AND MUTAGENESIS OF ARG-407. RC TISSUE=Brain; RX MEDLINE=22337253; PubMed=12446789; RX DOI=10.1128/MCB.22.24.8721-8734.2002; RA Nakamura T., Komiya M., Sone K., Hirose E., Gotoh N., Morii H., RA Ohta Y., Mori N.; RT "Grit, a GTPase-activating protein for the Rho family, regulates RT neurite extension through association with the TrkA receptor and N-Shc RT and CrkL/Crk adapter molecules."; RL Mol. Cell. Biol. 22:8721-8734(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH RP GAB1 AND GAB2; BCAR1; CRK AND NCK1, AND SUBCELLULAR LOCATION. RC TISSUE=Brain; RX MEDLINE=22829943; PubMed=12819203; DOI=10.1074/jbc.M304594200; RA Zhao C., Ma H., Bossy-Wetzel E., Lipton S.A., Zhang Z., Feng G.S.; RT "GC-GAP, a Rho family GTPase-activating protein that interacts with RT signaling adapters Gab1 and Gab2."; RL J. Biol. Chem. 278:34641-34653(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-173 AND RP ARG-407. RX PubMed=17663722; DOI=10.1111/j.1365-2443.2007.01101.x; RA Hayashi T., Okabe T., Nasu-Nishimura Y., Sakaue F., Ohwada S., RA Matsuura K., Akiyama T., Nakamura T.; RT "PX-RICS, a novel splicing variant of RICS, is a main isoform RT expressed during neural development."; RL Genes Cells 12:929-939(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX MEDLINE=99087487; PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Colon, and Eye; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, INTERACTION WITH FYN, AND PHOSPHORYLATION (ISOFORM 2). RX PubMed=12788081; DOI=10.1016/S0006-291X(03)00923-9; RA Taniguchi S., Liu H., Nakazawa T., Yokoyama K., Tezuka T., RA Yamamoto T.; RT "p250GAP, a neural RhoGAP protein, is associated with and RT phosphorylated by Fyn."; RL Biochem. Biophys. Res. Commun. 306:151-155(2003). RN [8] RP FUNCTION, AND MUTAGENESIS OF ARG-407. RX PubMed=12454018; DOI=10.1074/jbc.M207789200; RA Moon S.Y., Zang H., Zheng Y.; RT "Characterization of a brain-specific Rho GTPase-activating protein, RT p200RhoGAP."; RL J. Biol. Chem. 278:4151-4159(2003). RN [9] RP FUNCTION, INTERACTION WITH CTNNB1, AND MUTAGENESIS OF ARG-407 AND RP LYS-447. RX PubMed=12531901; DOI=10.1074/jbc.M208872200; RA Okabe T., Nakamura T., Nishimura Y.N., Kohu K., Ohwada S., RA Morishita Y., Akiyama T.; RT "RICS, a novel GTPase-activating protein for Cdc42 and Rac1, is RT involved in the beta-catenin-N-cadherin and N-methyl-D-aspartate RT receptor signaling."; RL J. Biol. Chem. 278:9920-9927(2003). RN [10] RP FUNCTION, INTERACTION WITH GRIN2B, AND MUTAGENESIS OF ARG-407. RX PubMed=12857875; DOI=10.1091/mbc.E02-09-0623; RA Nakazawa T., Watabe A.M., Tezuka T., Yoshida Y., Yokoyama K., RA Umemori H., Inoue A., Okabe S., Manabe T., Yamamoto T.; RT "p250GAP, a novel brain-enriched GTPase-activating protein for Rho RT family GTPases, is involved in the N-methyl-d-aspartate receptor RT signaling."; RL Mol. Biol. Cell 14:2921-2934(2003). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1236, AND MASS RP SPECTROMETRY. 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 RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-856 AND RP SER-871, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1557, AND MASS RP SPECTROMETRY. RC TISSUE=Mammary epithelium; RX PubMed=19534553; DOI=10.1021/pr900044c; RA Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., RA Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., RA Wiley H.S., Qian W.-J.; RT "An extensive survey of tyrosine phosphorylation revealing new sites RT in human mammary epithelial cells."; RL J. Proteome Res. 8:3852-3861(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-892 AND SER-1203, AND RP MASS SPECTROMETRY. 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 [15] RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 367-577. RG Structural genomics consortium (SGC); RT "Crystal structure of the Rho-GAP domain of RICS."; RL Submitted (SEP-2009) to the PDB data bank. CC -!- FUNCTION: GTPase-activating protein (GAP) promoting GTP hydrolysis CC on RHOA, CDC42 and RAC1 small GTPases. May be involved in the CC differentiation of neuronal cells during the formation of neurite CC extensions. Involved in NMDA receptor activity-dependent actin CC reorganization in dendritic spines. May mediate cross-talks CC between Ras- and Rho-regulated signaling pathways in cell growth CC regulation. Isoform 2 has higher GAP activity (By similarity). CC -!- SUBUNIT: Interacts with NTRK1 (via cytoplasmic domain); the CC interaction is independent of the phosphorylation state of NTRK1. CC Interacts with SHC3 (via SH2 domain). Interacts with RASA1 (via CC SH3 domain); the interaction is necessary for the Ras activation CC and cell transforming activities of ARHGAP32 (By similarity). CC Interacts with GAB1 and GAB2. Interacts with CRK and CRKL. Found CC in a complex with CRKL and BCAR1; upon EGF stimulation BCAR1 may CC be replaced by EGFR. Interacts with NCK1 (via SH3 domain); NCK1 CC recruits phosphorylated BCAR1 to the complex. Isoform 2 interacts CC with FYN; the interaction appears to be dependent on tyrosine CC phosphorylation of ARHGAP32. Interacts with EGFR; the interaction CC requires EGF stimulation and is increased by SHC3. Interacts with CC CDC42; the interaction requires constitutively active CDC42. CC Interacts with CTNNB1, DLG4, CDH2 and GRIN2B (By similarity). CC -!- INTERACTION: CC P06241:FYN; NbExp=4; IntAct=EBI-308663, EBI-515315; CC -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell CC membrane, postsynaptic density. Cell projection, dendritic spine CC (By similarity). Cytoplasm, cell cortex. Endosome membrane (By CC similarity). Golgi apparatus membrane (By similarity). Endoplasmic CC reticulum membrane (By similarity). Membrane. Note=Association to CC membrane via PX domain. Associated with cortical actin in CC undifferentiated neuroblastoma cells, but localized to dendritic CC spine and postsynaptic density after differentiation (By CC similarity). Colocalizes with EGFR at the cell membrane upon EGF CC treatment. Colocalizes with GAB2 at the cell membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=PX-RICS; CC IsoId=A7KAX9-1; Sequence=Displayed; CC Name=2; CC IsoId=A7KAX9-2; Sequence=VSP_034933; CC Name=3; CC IsoId=A7KAX9-3; Sequence=VSP_034934, VSP_034935, VSP_034936; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed CC in brain and testis. Isoform 1 is also expressed in other tissues CC such as lung, liver and spleen. CC -!- DOMAIN: The N-terminal PX domain interacts specifically with CC phosphatidylinositides (By similarity). CC -!- PTM: Isoform 2 is phosphorylated on multiple tyrosine residues by CC FYN. Phosphorylated tyrosine residues undergo dephosphorylation CC after stimulation of NMDA receptors (By similarity). CC Phosphorylated in vitro by CaMK2 in the presence of calmodulin and CC calcium; which inhibits GAP activity (By similarity). CC -!- SIMILARITY: Belongs to the PX domain-containing GAP family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC -!- SIMILARITY: Contains 1 Rho-GAP domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAA34432.2; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB079856; BAC24802.1; -; mRNA. DR EMBL; AY194287; AAO43677.1; -; mRNA. DR EMBL; EF127492; ABO33171.1; -; mRNA. DR EMBL; AB018255; BAA34432.2; ALT_INIT; mRNA. DR EMBL; CH471065; EAW67740.1; -; Genomic_DNA. DR EMBL; BC000277; AAH00277.2; -; mRNA. DR EMBL; BC104898; AAI04899.1; -; mRNA. DR EMBL; BC113429; AAI13430.1; -; mRNA. DR IPI; IPI00787743; -. DR IPI; IPI00900354; -. DR IPI; IPI01018779; -. DR RefSeq; NP_001136157.1; NM_001142685.1. DR RefSeq; NP_055530.2; NM_014715.3. DR UniGene; Hs.440379; -. DR PDB; 3IUG; X-ray; 1.77 A; A/B=367-577. DR PDBsum; 3IUG; -. DR ProteinModelPortal; A7KAX9; -. DR SMR; A7KAX9; 264-321, 368-569. DR IntAct; A7KAX9; 6. DR STRING; A7KAX9; -. DR PRIDE; A7KAX9; -. DR Ensembl; ENST00000310343; ENSP00000310561; ENSG00000134909. DR GeneID; 9743; -. DR KEGG; hsa:9743; -. DR CTD; 9743; -. DR GeneCards; GC11M124785; -. DR HGNC; HGNC:17399; ARHGAP32. DR HPA; HPA038389; -. DR MIM; 608541; gene. DR neXtProt; NX_A7KAX9; -. DR PharmGKB; PA165543138; -. DR HOGENOM; HBG445290; -. DR HOVERGEN; HBG108407; -. DR InParanoid; A7KAX9; -. DR OMA; HQEASHR; -. DR OrthoDB; EOG46MBHP; -. DR PhylomeDB; A7KAX9; -. DR Reactome; REACT_111102; Signal Transduction. DR NextBio; 36663; -. DR Bgee; A7KAX9; -. DR Genevestigator; A7KAX9; -. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. DR InterPro; IPR001683; Phox. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR InterPro; IPR001452; SH3_domain. DR Gene3D; G3DSA:3.30.1520.10; PX; 1. DR Gene3D; G3DSA:1.10.555.10; RhoGAP; 1. DR Pfam; PF00787; PX; 1. DR Pfam; PF00620; RhoGAP; 1. DR Pfam; PF00018; SH3_1; 1. DR SMART; SM00324; RhoGAP; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF64268; PX; 1. DR SUPFAM; SSF48350; Rho_GAP; 1. DR SUPFAM; SSF50044; SH3; 1. DR PROSITE; PS50195; PX; FALSE_NEG. DR PROSITE; PS50238; RHOGAP; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Cell projection; Complete proteome; Cytoplasm; Endoplasmic reticulum; KW Endosome; Golgi apparatus; GTPase activation; Membrane; KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; KW SH3 domain; Synapse. FT CHAIN 1 2087 Rho GTPase-activating protein 32. FT /FTId=PRO_0000345203. FT DOMAIN 131 245 PX; atypical. FT DOMAIN 259 321 SH3. FT DOMAIN 372 567 Rho-GAP. FT REGION 1391 1711 Interaction with GAB2. FT REGION 1685 2087 Interaction with FYN. FT COMPBIAS 1031 1036 Poly-Pro. FT COMPBIAS 1305 1310 Poly-Pro. FT MOD_RES 613 613 Phosphoserine. FT MOD_RES 706 706 Phosphoserine (By similarity). FT MOD_RES 856 856 Phosphoserine. FT MOD_RES 871 871 Phosphoserine. FT MOD_RES 892 892 Phosphoserine. FT MOD_RES 952 952 Phosphoserine (By similarity). FT MOD_RES 1203 1203 Phosphoserine. FT MOD_RES 1236 1236 Phosphothreonine. FT MOD_RES 1557 1557 Phosphotyrosine. FT VAR_SEQ 1 349 Missing (in isoform 2). FT /FTId=VSP_034933. FT VAR_SEQ 1 290 Missing (in isoform 3). FT /FTId=VSP_034934. FT VAR_SEQ 567 612 FSGRISMAMQEGAASLSRPKSLLVSSPSTKLLTLEEAQART FT QAQVN -> LPHFSARTELIVPFPLRLLRKQFTPPLLGPMS FT PLNPLVQITVCISI (in isoform 3). FT /FTId=VSP_034935. FT VAR_SEQ 613 2087 Missing (in isoform 3). FT /FTId=VSP_034936. FT MUTAGEN 173 173 Y->A: Loss of binding to phospholipids. FT Cytoplasmic localization. FT MUTAGEN 407 407 R->A: Mild effect on GAP activity and FT neurite-promotion upon nerve growth FT factor stimulation. FT MUTAGEN 407 407 R->I: Loss of GAP activity. FT MUTAGEN 407 407 R->M: Loss of GAP activity. In isoform 1, FT no inhibitory effect on neurite FT extension. FT MUTAGEN 447 447 K->A: Loss of GAP activity. FT HELIX 377 380 FT HELIX 387 398 FT HELIX 412 423 FT TURN 433 437 FT TURN 439 441 FT HELIX 445 452 FT TURN 460 462 FT HELIX 463 470 FT STRAND 472 474 FT HELIX 475 486 FT HELIX 491 508 FT HELIX 511 514 FT HELIX 518 529 FT HELIX 553 561 FT HELIX 563 566 SQ SEQUENCE 2087 AA; 230529 MW; 075E5B4902857D06 CRC64; METESESSTL GDDSVFWLES EVIIQVTDCE EEEREEKFRK MKSSVHSEED DFVPELHRNV HPRERPDWEE TLSAMARGAD VPEIPGDLTL KTCGSTASMK VKHVKKLPFT KGHFPKMAEC AHFHYENVEF GSIQLSLSEE QNEVMKNGCE SKELVYLVQI ACQGKSWIVK RSYEDFRVLD KHLHLCIYDR RFSQLSELPR SDTLKDSPES VTQMLMAYLS RLSAIAGNKI NCGPALTWME IDNKGNHLLV HEESSINTPA VGAAHVIKRY TARAPDELTL EVGDIVSVID MPPKVLSTWW RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM KSRPTKQKLK QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG IVDGIYRLSG VASNIQRLRH EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF RELPNPLLTY QLYEKFSDAV SAATDEERLI KIHDVIQQLP PPHYRTLEFL MRHLSLLADY CSITNMHAKN LAIVWAPNLL RSKQIESACF SGTAAFMEVR IQSVVVEFIL NHVDVLFSGR ISMAMQEGAA SLSRPKSLLV SSPSTKLLTL EEAQARTQAQ VNSPIVTENK YIEVGEGPAA LQGKFHTIIE FPLERKRPQN KMKKSPVGSW RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT LRSAKSEESL TSLHAVDGDS KLFRPRRPRS SSDALSASFN GEMLGNRCNS YDNLPHDNES EEEGGLLHIP ALMSPHSAED VDLSPPDIGV ASLDFDPMSF QCSPPKAESE CLESGASFLD SPGYSKDKPS ANKKDAETGS SQCQTPGSTA SSEPVSPLQE KLSPFFTLDL SPTEDKSSKP SSFTEKVVYA FSPKIGRKLS KSPSMSISEP ISVTLPPRVS EVIGTVSNTT AQNASSSTWD KCVEERDATN RSPTQIVKMK TNETVAQEAY ESEVQPLDQV AAEEVELPGK EDQSVSSSQS KAVASGQTQT GAVTHDPPQD SVPVSSVSLI PPPPPPKNVA RMLALALAES AQQASTQSLK RPGTSQAGYT NYGDIAVATT EDNLSSSYSA VALDKAYFQT DRPAEQFHLQ NNAPGNCDHP LPETTATGDP THSNTTESGE QHHQVDLTGN QPHQAYLSGD PEKARITSVP LDSEKSDDHV SFPEDQSGKN SMPTVSFLDQ DQSPPRFYSG DQPPSYLGAS VDKLHHPLEF ADKSPTPPNL PSDKIYPPSG SPEENTSTAT MTYMTTTPAT AQMSTKEASW DVAEQPTTAD FAAATLQRTH RTNRPLPPPP SQRSAEQPPV VGQVQAATNI GLNNSHKVQG VVPVPERPPE PRAMDDPASA FISDSGAAAA QCPMATAVQP GLPEKVRDGA RVPLLHLRAE SVPAHPCGFP APLPPTRMME SKMIAAIHSS SADATSSSNY HSFVTASSTS VDDALPLPLP VPQPKHASQK TVYSSFARPD VTTEPFGPDN CLHFNMTPNC QYRPQSVPPH HNKLEQHQVY GARSEPPASM GLRYNTYVAP GRNASGHHSK PCSRVEYVSS LSSSVRNTCY PEDIPPYPTI RRVQSLHAPP SSMIRSVPIS RTEVPPDDEP AYCPRPLYQY KPYQSSQARS DYHVTQLQPY FENGRVHYRY SPYSSSSSSY YSPDGALCDV DAYGTVQLRP LHRLPNRDFA FYNPRLQGKS LYSYAGLAPR PRANVTGYFS PNDHNVVSMP PAADVKHTYT SWDLEDMEKY RMQSIRRESR ARQKVKGPVM SQYDNMTPAV QDDLGGIYVI HLRSKSDPGK TGLLSVAEGK ESRHAAKAIS PEGEDRFYRR HPEAEMDRAH HHGGHGSTQP EKPSLPQKQS SLRSRKLPDM GCSLPEHRAH QEASHRQFCE SKNGPPYPQG AGQLDYGSKG IPDTSEPVSY HNSGVKYAAS GQESLRLNHK EVRLSKEMER PWVRQPSAPE KHSRDCYKEE EHLTQSIVPP PKPERSHSLK LHHTQNVERD PSVLYQYQPH GKRQSSVTVV SQYDNLEDYH SLPQHQRGVF GGGGMGTYVP PGFPHPQSRT YATALGQGAF LPAELSLQHP ETQIHAE //