ID RHG27_HUMAN Reviewed; 889 AA. AC Q6ZUM4; A4FU35; A8K3N5; C9JTF3; Q494U0; Q6NWZ8; Q8WY58; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 3. DT 27-MAR-2024, entry version 171. DE RecName: Full=Rho GTPase-activating protein 27; DE AltName: Full=CIN85-associated multi-domain-containing Rho GTPase-activating protein 1; DE AltName: Full=Rho-type GTPase-activating protein 27; DE AltName: Full=SH3 domain-containing protein 20; GN Name=ARHGAP27 {ECO:0000312|HGNC:HGNC:31813}; GN Synonyms=CAMGAP1, SH3D20 {ECO:0000312|HGNC:HGNC:31813}; GN ORFNames=PP905; 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 4). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Embryo, and Prostate; 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 GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 270-889 (ISOFORMS 1 AND 3), AND VARIANT GLN-889. RC TISSUE=Pancreas; 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 [5] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX PubMed=15492870; RA Katoh Y., Katoh M.; RT "Identification and characterization of ARHGAP27 gene in silico."; RL Int. J. Mol. Med. 14:943-947(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-466, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Rho GTPase-activating protein which may be involved in CC clathrin-mediated endocytosis. GTPase activators for the Rho-type CC GTPases act by converting them to an inactive GDP-bound state. Has CC activity toward CDC42 and RAC1 (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with SH3KBP1/CIN85. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6ZUM4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6ZUM4-2; Sequence=VSP_031053; CC Name=3; CC IsoId=Q6ZUM4-3; Sequence=VSP_031056; CC Name=4; Synonyms=SH3D20; CC IsoId=Q6ZUM4-4; Sequence=VSP_031054, VSP_031055; CC -!- TISSUE SPECIFICITY: Expressed in germinal center B-cell, spleen, CC chronic lymphocytic leukemia, pancreatic cancer and lung cancer. CC {ECO:0000269|PubMed:15492870}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI01389.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI01390.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI01391.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AF258593; AAG23796.1; -; mRNA. DR EMBL; AK125535; BAC86196.1; -; mRNA. DR EMBL; AK290650; BAF83339.1; -; mRNA. DR EMBL; AC003070; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC091132; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC067345; AAH67345.1; -; mRNA. DR EMBL; BC101388; AAI01389.1; ALT_INIT; mRNA. DR EMBL; BC101389; AAI01390.1; ALT_INIT; mRNA. DR EMBL; BC101390; AAI01391.1; ALT_INIT; mRNA. DR EMBL; BC101391; AAI01392.3; -; mRNA. DR CCDS; CCDS11498.1; -. [Q6ZUM4-2] DR CCDS; CCDS32670.1; -. [Q6ZUM4-4] DR CCDS; CCDS74082.1; -. [Q6ZUM4-1] DR RefSeq; NP_001269219.1; NM_001282290.1. [Q6ZUM4-1] DR RefSeq; NP_777579.2; NM_174919.3. [Q6ZUM4-4] DR RefSeq; NP_954976.1; NM_199282.2. [Q6ZUM4-2] DR RefSeq; XP_006721808.1; XM_006721745.2. DR PDB; 3PP2; X-ray; 1.42 A; A/B=491-613. DR PDBsum; 3PP2; -. DR AlphaFoldDB; Q6ZUM4; -. DR SMR; Q6ZUM4; -. DR BioGRID; 128369; 13. DR IntAct; Q6ZUM4; 2. DR STRING; 9606.ENSP00000403323; -. DR GlyCosmos; Q6ZUM4; 1 site, 2 glycans. DR GlyGen; Q6ZUM4; 1 site, 2 O-linked glycans (1 site). DR iPTMnet; Q6ZUM4; -. DR PhosphoSitePlus; Q6ZUM4; -. DR BioMuta; ARHGAP27; -. DR DMDM; 300669680; -. DR EPD; Q6ZUM4; -. DR jPOST; Q6ZUM4; -. DR MassIVE; Q6ZUM4; -. DR MaxQB; Q6ZUM4; -. DR PaxDb; 9606-ENSP00000403323; -. DR PeptideAtlas; Q6ZUM4; -. DR ProteomicsDB; 68341; -. [Q6ZUM4-1] DR ProteomicsDB; 68342; -. [Q6ZUM4-2] DR ProteomicsDB; 68343; -. [Q6ZUM4-3] DR ProteomicsDB; 68344; -. [Q6ZUM4-4] DR Pumba; Q6ZUM4; -. DR Antibodypedia; 49843; 157 antibodies from 23 providers. DR DNASU; 201176; -. DR Ensembl; ENST00000290470.3; ENSP00000290470.3; ENSG00000159314.13. [Q6ZUM4-4] DR Ensembl; ENST00000376922.6; ENSP00000366121.2; ENSG00000159314.13. [Q6ZUM4-2] DR Ensembl; ENST00000528273.5; ENSP00000436137.1; ENSG00000159314.13. [Q6ZUM4-4] DR Ensembl; ENST00000610792.3; ENSP00000477741.1; ENSG00000276907.4. [Q6ZUM4-1] DR Ensembl; ENST00000611188.1; ENSP00000481302.1; ENSG00000276907.4. [Q6ZUM4-4] DR Ensembl; ENST00000612916.3; ENSP00000480582.1; ENSG00000276836.4. [Q6ZUM4-2] DR Ensembl; ENST00000616021.2; ENSP00000478738.1; ENSG00000276907.4. [Q6ZUM4-2] DR Ensembl; ENST00000633003.1; ENSP00000487991.1; ENSG00000276907.4. [Q6ZUM4-4] DR Ensembl; ENST00000685559.1; ENSP00000509127.1; ENSG00000159314.13. [Q6ZUM4-1] DR GeneID; 201176; -. DR KEGG; hsa:201176; -. DR MANE-Select; ENST00000685559.1; ENSP00000509127.1; NM_001282290.2; NP_001269219.1. DR UCSC; uc002iix.4; human. [Q6ZUM4-1] DR AGR; HGNC:31813; -. DR CTD; 201176; -. DR DisGeNET; 201176; -. DR GeneCards; ARHGAP27; -. DR HGNC; HGNC:31813; ARHGAP27. DR HPA; ENSG00000159314; Tissue enhanced (esophagus). DR MIM; 610591; gene. DR neXtProt; NX_Q6ZUM4; -. DR OpenTargets; ENSG00000159314; -. DR PharmGKB; PA134873327; -. DR VEuPathDB; HostDB:ENSG00000159314; -. DR eggNOG; KOG1450; Eukaryota. DR eggNOG; KOG4269; Eukaryota. DR GeneTree; ENSGT00950000182860; -. DR HOGENOM; CLU_1140156_0_0_1; -. DR InParanoid; Q6ZUM4; -. DR OMA; RVFFYNA; -. DR OrthoDB; 5395569at2759; -. DR PhylomeDB; Q6ZUM4; -. DR TreeFam; TF329345; -. DR PathwayCommons; Q6ZUM4; -. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR SignaLink; Q6ZUM4; -. DR SIGNOR; Q6ZUM4; -. DR BioGRID-ORCS; 201176; 19 hits in 1144 CRISPR screens. DR ChiTaRS; ARHGAP27; human. DR GenomeRNAi; 201176; -. DR Pharos; Q6ZUM4; Tbio. DR PRO; PR:Q6ZUM4; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q6ZUM4; Protein. DR Bgee; ENSG00000159314; Expressed in lower esophagus mucosa and 95 other cell types or tissues. DR ExpressionAtlas; Q6ZUM4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005096; F:GTPase activator activity; ISS:HGNC-UCL. DR GO; GO:0017124; F:SH3 domain binding; ISS:HGNC-UCL. DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:HGNC-UCL. DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:HGNC-UCL. 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; cd13233; PH_ARHGAP9-like; 1. DR CDD; cd04403; RhoGAP_ARHGAP27_15_12_9; 1. DR CDD; cd12069; SH3_ARHGAP27; 1. DR CDD; cd00201; WW; 3. DR Gene3D; 2.20.70.10; -; 2. 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 Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR23176:SF104; RHO GTPASE-ACTIVATING PROTEIN 27; 1. DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00620; RhoGAP; 1. DR Pfam; PF00397; WW; 2. DR SMART; SM00233; PH; 1. DR SMART; SM00324; RhoGAP; 1. DR SMART; SM00456; WW; 3. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR SUPFAM; SSF51045; WW domain; 2. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50238; RHOGAP; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS50020; WW_DOMAIN_2; 3. DR Genevisible; Q6ZUM4; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Endocytosis; KW GTPase activation; Membrane; Phosphoprotein; Reference proteome; Repeat; KW SH3 domain. FT CHAIN 1..889 FT /note="Rho GTPase-activating protein 27" FT /id="PRO_0000317578" FT DOMAIN 6..69 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 246..280 FT /note="WW 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 299..333 FT /note="WW 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 411..444 FT /note="WW 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 496..612 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 697..886 FT /note="Rho-GAP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172" FT REGION 104..132 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 329..397 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 447..474 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 617..655 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 156 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6TLK4" FT MOD_RES 216 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AB59" FT MOD_RES 249 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 347 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AB59" FT MOD_RES 456 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AB59" FT MOD_RES 461 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:A2AB59" FT MOD_RES 466 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..341 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_031053" FT VAR_SEQ 221..263 FT /note="DDPPEPVYANIERQPRATSPGAAAAPLPSPVWETHTDAGTGRP -> PPRAL FT GRGGGWRARDRARTEPGRKETRSAQRRARRPPLSEDFG (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15498874" FT /id="VSP_031054" FT VAR_SEQ 264..889 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15498874" FT /id="VSP_031055" FT VAR_SEQ 416..442 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031056" FT VARIANT 889 FT /note="H -> Q (in dbSNP:rs117139057)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_038551" FT CONFLICT 41 FT /note="S -> N (in Ref. 1; AAG23796)" FT /evidence="ECO:0000305" FT CONFLICT 162 FT /note="C -> R (in Ref. 2; BAF83339)" FT /evidence="ECO:0000305" FT CONFLICT 213 FT /note="P -> R (in Ref. 4; AAH67345)" FT /evidence="ECO:0000305" FT STRAND 499..510 FT /evidence="ECO:0007829|PDB:3PP2" FT STRAND 521..528 FT /evidence="ECO:0007829|PDB:3PP2" FT STRAND 531..536 FT /evidence="ECO:0007829|PDB:3PP2" FT HELIX 549..552 FT /evidence="ECO:0007829|PDB:3PP2" FT STRAND 554..560 FT /evidence="ECO:0007829|PDB:3PP2" FT STRAND 565..568 FT /evidence="ECO:0007829|PDB:3PP2" FT HELIX 571..573 FT /evidence="ECO:0007829|PDB:3PP2" FT STRAND 575..583 FT /evidence="ECO:0007829|PDB:3PP2" FT STRAND 589..593 FT /evidence="ECO:0007829|PDB:3PP2" FT HELIX 597..611 FT /evidence="ECO:0007829|PDB:3PP2" SQ SEQUENCE 889 AA; 98396 MW; E341CCC4D012DA4C CRC64; MAADVVGDVY VLVEHPFEYT GKDGRRVAIR PNERYRLLRR STEHWWHVRR EPGGRPFYLP AQYVRELPAL GNPAAAAPPG PHPSPAAPEP LAYDYRFVSA AATAGPDGAP EESGGRASSL CGPAQRGAAT QRSSLAPGLP ACLYLRPAAP VRPAQSLNDL ACAAVSPPAG LLGSSGSFKA CSVAGSWVCP RPLARSDSEN VYEVIQDLHV PPPEESAEQV DDPPEPVYAN IERQPRATSP GAAAAPLPSP VWETHTDAGT GRPYYYNPDT GVTTWESPFE AAEGAASPAT SPASVDSHVS LETEWGQYWD EESRRVFFYN PLTGETAWED EAENEPEEEL EMQPGLSPGS PGDPRPPTPE TDYPESLTSY PEEDYSPVGS FGEPGPTSPL TTPPGWSCHV SQDKQMLYTN HFTQEQWVRL EDPHGKPYFY NPEDSSVRWE LPQVPVPAPR SIHKSSQDGD TPAQASPPEE KVPAELDEVG SWEEVSPATA AVRTKTLDKA GVLHRTKTAD KGKRLRKKHW SASWTVLEGG VLTFFKDSKT SAAGGLRQPS KFSTPEYTVE LRGATLSWAP KDKSSRKNVL ELRSRDGSEY LIQHDSEAII STWHKAIAQG IQELSAELPP EESESSRVDF GSSERLGSWQ EKEEDARPNA AAPALGPVGL ESDLSKVRHK LRKFLQRRPT LQSLREKGYI KDQVFGCALA ALCERERSRV PRFVQQCIRA VEARGLDIDG LYRISGNLAT IQKLRYKVDH DERLDLDDGR WEDVHVITGA LKLFFRELPE PLFPFSHFRQ FIAAIKLQDQ ARRSRCVRDL VRSLPAPNHD TLRMLFQHLC RVIEHGEQNR MSVQSVAIVF GPTLLRPEVE ETSMPMTMVF QNQVVELILQ QCADIFPPH //