ID RHG22_HUMAN Reviewed; 698 AA. AC Q7Z5H3; A0AVP7; A5YM75; B4DED8; B9EGA0; C9JDM2; O00152; Q6ZSB0; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=Rho GTPase-activating protein 22; DE AltName: Full=Rho-type GTPase-activating protein 22; GN Name=ARHGAP22; Synonyms=RHOGAP2; 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] (ISOFORM 1). RA Huang C.Q., Shan Y.X., Liu S.; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5). RC TISSUE=Cerebellum, and Erythroleukemia; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lung, and Testis; 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 [8] RP IDENTIFICATION. RX PubMed=15254788; RA Katoh M., Katoh M.; RT "Identification and characterization of ARHGAP24 and ARHGAP25 genes in RT silico."; RL Int. J. Mol. Med. 14:333-338(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359 AND SER-395, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 -!- FUNCTION: Rho GTPase-activating protein involved in the signal CC transduction pathway that regulates endothelial cell capillary tube CC formation during angiogenesis. Acts as a GTPase activator for the RAC1 CC by converting it to an inactive GDP-bound state. Inhibits RAC1- CC dependent lamellipodia formation. May also play a role in transcription CC regulation via its interaction with VEZF1, by regulating activity of CC the endothelin-1 (EDN1) promoter (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with VEZF1. {ECO:0000250}. CC -!- INTERACTION: CC Q7Z5H3; O00555: CACNA1A; NbExp=2; IntAct=EBI-3866859, EBI-766279; CC Q7Z5H3; O95273: CCNDBP1; NbExp=3; IntAct=EBI-3866859, EBI-748961; CC Q7Z5H3-2; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-12084490, EBI-745369; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC Note=Mainly cytoplasmic. Some fraction is nuclear (By similarity). CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q7Z5H3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7Z5H3-2; Sequence=VSP_023705; CC Name=3; CC IsoId=Q7Z5H3-3; Sequence=VSP_023704; CC Name=4; CC IsoId=Q7Z5H3-4; Sequence=VSP_023703; CC Name=5; CC IsoId=Q7Z5H3-5; Sequence=VSP_053502; 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; AY324801; AAP85632.1; -; mRNA. DR EMBL; AK127586; BAC87044.1; -; mRNA. DR EMBL; AK293579; BAG57049.1; -; mRNA. DR EMBL; U90908; AAB51057.1; -; mRNA. DR EMBL; EF560749; ABQ59059.1; -; mRNA. DR EMBL; AC016397; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC016399; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC068898; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471187; EAW93127.1; -; Genomic_DNA. DR EMBL; BC126444; AAI26445.1; -; mRNA. DR EMBL; BC136319; AAI36320.1; -; mRNA. DR CCDS; CCDS58079.1; -. [Q7Z5H3-3] DR CCDS; CCDS58080.1; -. [Q7Z5H3-2] DR CCDS; CCDS58081.1; -. [Q7Z5H3-5] DR CCDS; CCDS7227.1; -. [Q7Z5H3-1] DR RefSeq; NP_001242953.1; NM_001256024.1. [Q7Z5H3-2] DR RefSeq; NP_001242954.1; NM_001256025.2. [Q7Z5H3-5] DR RefSeq; NP_001242955.1; NM_001256026.1. [Q7Z5H3-3] DR RefSeq; NP_001334667.1; NM_001347738.1. [Q7Z5H3-5] DR RefSeq; NP_067049.2; NM_021226.3. [Q7Z5H3-1] DR RefSeq; XP_011538306.1; XM_011540004.1. DR AlphaFoldDB; Q7Z5H3; -. DR SASBDB; Q7Z5H3; -. DR SMR; Q7Z5H3; -. DR BioGRID; 121832; 70. DR IntAct; Q7Z5H3; 45. DR MINT; Q7Z5H3; -. DR STRING; 9606.ENSP00000412461; -. DR iPTMnet; Q7Z5H3; -. DR PhosphoSitePlus; Q7Z5H3; -. DR BioMuta; ARHGAP22; -. DR DMDM; 74750129; -. DR EPD; Q7Z5H3; -. DR jPOST; Q7Z5H3; -. DR MassIVE; Q7Z5H3; -. DR MaxQB; Q7Z5H3; -. DR PaxDb; 9606-ENSP00000412461; -. DR PeptideAtlas; Q7Z5H3; -. DR ProteomicsDB; 3948; -. DR ProteomicsDB; 69289; -. [Q7Z5H3-1] DR ProteomicsDB; 69290; -. [Q7Z5H3-2] DR ProteomicsDB; 69291; -. [Q7Z5H3-3] DR ProteomicsDB; 69292; -. [Q7Z5H3-4] DR Pumba; Q7Z5H3; -. DR Antibodypedia; 58456; 168 antibodies from 26 providers. DR DNASU; 58504; -. DR Ensembl; ENST00000249601.9; ENSP00000249601.4; ENSG00000128805.15. [Q7Z5H3-1] DR Ensembl; ENST00000417247.6; ENSP00000410054.2; ENSG00000128805.15. [Q7Z5H3-3] DR Ensembl; ENST00000417912.6; ENSP00000412461.2; ENSG00000128805.15. [Q7Z5H3-2] DR Ensembl; ENST00000435790.6; ENSP00000416701.2; ENSG00000128805.15. [Q7Z5H3-5] DR GeneID; 58504; -. DR KEGG; hsa:58504; -. DR MANE-Select; ENST00000249601.9; ENSP00000249601.4; NM_021226.4; NP_067049.2. DR UCSC; uc001jgs.5; human. [Q7Z5H3-1] DR AGR; HGNC:30320; -. DR CTD; 58504; -. DR DisGeNET; 58504; -. DR GeneCards; ARHGAP22; -. DR HGNC; HGNC:30320; ARHGAP22. DR HPA; ENSG00000128805; Tissue enriched (brain). DR MIM; 610585; gene. DR neXtProt; NX_Q7Z5H3; -. DR OpenTargets; ENSG00000128805; -. DR PharmGKB; PA134979724; -. DR VEuPathDB; HostDB:ENSG00000128805; -. DR eggNOG; KOG4270; Eukaryota. DR GeneTree; ENSGT00950000183015; -. DR HOGENOM; CLU_020795_0_0_1; -. DR InParanoid; Q7Z5H3; -. DR OMA; MAVNHEA; -. DR OrthoDB; 48967at2759; -. DR PhylomeDB; Q7Z5H3; -. DR TreeFam; TF323577; -. DR PathwayCommons; Q7Z5H3; -. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR SignaLink; Q7Z5H3; -. DR SIGNOR; Q7Z5H3; -. DR BioGRID-ORCS; 58504; 14 hits in 1159 CRISPR screens. DR ChiTaRS; ARHGAP22; human. DR GenomeRNAi; 58504; -. DR Pharos; Q7Z5H3; Tbio. DR PRO; PR:Q7Z5H3; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q7Z5H3; Protein. DR Bgee; ENSG00000128805; Expressed in C1 segment of cervical spinal cord and 117 other cell types or tissues. DR ExpressionAtlas; Q7Z5H3; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. 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:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0099175; P:regulation of 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 CDD; cd13378; PH_RhoGAP2; 1. DR CDD; cd04390; RhoGAP_ARHGAP22_24_25; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR PANTHER; PTHR15228:SF22; RHO GTPASE-ACTIVATING PROTEIN 22; 1. DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00324; RhoGAP; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50238; RHOGAP; 1. DR Genevisible; Q7Z5H3; HS. PE 1: Evidence at protein level; KW Alternative splicing; Angiogenesis; Coiled coil; Cytoplasm; KW Developmental protein; Differentiation; GTPase activation; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..698 FT /note="Rho GTPase-activating protein 22" FT /id="PRO_0000280469" FT DOMAIN 37..145 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 155..349 FT /note="Rho-GAP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 373..394 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 406..450 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 469..498 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 540..599 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 590..687 FT /evidence="ECO:0000255" FT COMPBIAS 420..444 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 359 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..329 FT /note="MLSPKIRQARRARSKSLVMGEQSRSPGRMPCPHRLGPVLKAGWLKKQRSIMK FT NWQQRWFVLRGDQLFYYKDKDEIKPQGFISLQGTQVTELPPGPEDPGKHLFEISPGGAG FT EREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGGIFGQRLEETVHHERKYGPR FT LAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVAS FT LLKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELAKQVSNLPQANYNLLRYIC FT KFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTIME -> MGQPREFWHLRSQV FT PVPTCHLLTVQPWCLLPHPTPAGGRERRHSASSLLAALCLRKAVLRPHPAVLPGVGGCV FT VLSSGRMKAPLRGGLALGTGPAPTKLQLLHDWQSEPGPSGWQQGPSPPLFPA (in FT isoform 4)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_023703" FT VAR_SEQ 1..107 FT /note="MLSPKIRQARRARSKSLVMGEQSRSPGRMPCPHRLGPVLKAGWLKKQRSIMK FT NWQQRWFVLRGDQLFYYKDKDEIKPQGFISLQGTQVTELPPGPEDPGKHLFEISP -> FT MPFWPIRCLKRSRRMPR (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023704" FT VAR_SEQ 1..12 FT /note="MLSPKIRQARRA -> MLPTASSKRRTFAARYFT (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053502" FT VAR_SEQ 150 FT /note="G -> GGTARRSHAHPLEPLPP (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023705" FT VARIANT 410 FT /note="T -> K (in dbSNP:rs1867586)" FT /id="VAR_031153" FT VARIANT 612 FT /note="R -> C (in dbSNP:rs3747853)" FT /id="VAR_031154" SQ SEQUENCE 698 AA; 76779 MW; 3CE8CEB0A9E5D0F8 CRC64; MLSPKIRQAR RARSKSLVMG EQSRSPGRMP CPHRLGPVLK AGWLKKQRSI MKNWQQRWFV LRGDQLFYYK DKDEIKPQGF ISLQGTQVTE LPPGPEDPGK HLFEISPGGA GEREKVPANP EALLLMASSQ RDMEDWVQAI RRVIWAPLGG GIFGQRLEET VHHERKYGPR LAPLLVEQCV DFIRERGLTE EGLFRMPGQA NLVRDLQDSF DCGEKPLFDS TTDVHTVASL LKLYLRELPE PVVPFARYED FLSCAQLLTK DEGEGTLELA KQVSNLPQAN YNLLRYICKF LDEVQAYSNV NKMSVQNLAT VFGPNILRPQ VEDPVTIMEG TSLVQHLMTV LIRKHSQLFT APVPEGPTSP RGGLQCAVGW GSEEVTRDSQ GEPGGPGLPA HRTSSLDGAA VAVLSRTAPT GPGSRCSPGK KVQTLPSWKS SFRQPRSLSG SPKGGGSSLE VPIISSGGNW LMNGLSSLRG HRRASSGDRL KDSGSVQRLS TYDNVPAPGL VPGIPSVASM AWSGASSSES SVGGSLSSCT ACRASDSSAR SSLHTDWALE PSPLPSSSED PKSLDLDHSM DEAGAGASNS EPSEPDSPTR EHARRSEALQ GLVTELRAEL CRQRTEYERS VKRIEEGSAD LRKRMSRLEE ELDQEKKKYI MLEIKLRNSE RAREDAERRN QLLQREMEEF FSTLGSLTVG AKGARAPK //