RHG27_HUMAN
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 03-AUG-2022, entry version 162.
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}; 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};
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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. [Q6ZUM4-1]
DR PDB; 3PP2; X-ray; 1.42 A; A/B=491-613.
DR PDBsum; 3PP2; -.
DR AlphaFoldDB; Q6ZUM4; -.
DR SMR; Q6ZUM4; -.
DR BioGRID; 128369; 10.
DR IntAct; Q6ZUM4; 3.
DR STRING; 9606.ENSP00000403323; -.
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; Q6ZUM4; -.
DR PeptideAtlas; Q6ZUM4; -.
DR PRIDE; Q6ZUM4; -.
DR ProteomicsDB; 68341; -. [Q6ZUM4-1]
DR ProteomicsDB; 68342; -. [Q6ZUM4-2]
DR ProteomicsDB; 68343; -. [Q6ZUM4-3]
DR ProteomicsDB; 68344; -. [Q6ZUM4-4]
DR Antibodypedia; 49843; 144 antibodies from 23 providers.
DR DNASU; 201176; -.
DR Ensembl; ENST00000290470.3; ENSP00000290470.3; ENSG00000159314.12. [Q6ZUM4-4]
DR Ensembl; ENST00000376922.6; ENSP00000366121.2; ENSG00000159314.12. [Q6ZUM4-2]
DR Ensembl; ENST00000428638.5; ENSP00000403323.1; ENSG00000159314.12. [Q6ZUM4-1]
DR Ensembl; ENST00000528273.5; ENSP00000436137.1; ENSG00000159314.12. [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; ENSG00000159314.12. [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 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; WSCHVGP; -.
DR OrthoDB; 1300981at2759; -.
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; 17 hits in 1071 CRISPR screens.
DR ChiTaRS; ARHGAP27; human.
DR GenomeRNAi; 201176; -.
DR Pharos; Q6ZUM4; Tdark.
DR PRO; PR:Q6ZUM4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6ZUM4; protein.
DR Bgee; ENSG00000159314; Expressed in lower esophagus mucosa and 93 other tissues.
DR ExpressionAtlas; Q6ZUM4; baseline and differential.
DR Genevisible; Q6ZUM4; HS.
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:0043087; P:regulation of GTPase activity; IBA:GO_Central.
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; cd00201; WW; 3.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR015767; ARHGAP27.
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; PTHR23176:SF104; 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; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
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
