RHG04_HUMAN
ID RHG04_HUMAN Reviewed; 946 AA.
AC P98171; Q14144; Q86UY3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Rho GTPase-activating protein 4 {ECO:0000305};
DE AltName: Full=Rho-GAP hematopoietic protein C1;
DE AltName: Full=Rho-type GTPase-activating protein 4;
DE AltName: Full=p115;
GN Name=ARHGAP4 {ECO:0000312|HGNC:HGNC:674}; Synonyms=KIAA0131, RGC1, RHOGAP4;
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).
RC TISSUE=Embryo;
RX PubMed=8570618; DOI=10.1073/pnas.93.2.695;
RA Tribioli C., Droetto S., Bione S., Cesareni G., Torrisi M.R., Lotti L.V.,
RA Lanfrancone L., Toniolo D., Pelicci P.-G.;
RT "An X chromosome-linked gene encoding a protein with characteristics of a
RT rhoGAP predominantly expressed in hematopoietic cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:695-699(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-946 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-103 (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=7981673; DOI=10.1093/hmg/3.7.1061;
RA Tribioli C., Mancini M., Plassart E., Bione S., Rivella S., Sala C.,
RA Torri G., Toniolo D.;
RT "Isolation of new genes in distal Xq28: transcriptional map and
RT identification of a human homologue of the ARD1 N-acetyl transferase of
RT Saccharomyces cerevisiae.";
RL Hum. Mol. Genet. 3:1061-1068(1994).
RN [7]
RP INTERACTION WITH NCKAP1L.
RX PubMed=16417406; DOI=10.1371/journal.pbio.0040038;
RA Weiner O.D., Rentel M.C., Ott A., Brown G.E., Jedrychowski M., Yaffe M.B.,
RA Gygi S.P., Cantley L.C., Bourne H.R., Kirschner M.W.;
RT "Hem-1 complexes are essential for Rac activation, actin polymerization,
RT and myosin regulation during neutrophil chemotaxis.";
RL PLoS Biol. 4:E38-E38(2006).
RN [8]
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 [9]
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860; SER-901 AND SER-906, 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).
RN [11]
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).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP STRUCTURE BY NMR OF 746-814.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of SH3 domain in Rho-GTPase-activating protein 4.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Inhibitory effect on stress fiber organization. May down-
CC regulate Rho-like GTPase in hematopoietic cells.
CC -!- SUBUNIT: Interacts with NCKAP1L. {ECO:0000269|PubMed:16417406}.
CC -!- INTERACTION:
CC P98171-1; P98171-1: ARHGAP4; NbExp=3; IntAct=EBI-16177615, EBI-16177615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Just below the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P98171-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P98171-2; Sequence=VSP_042902;
CC -!- TISSUE SPECIFICITY: Predominantly in hematopoietic cells (spleen,
CC thymus and leukocytes); low levels in placenta, lung and various fetal
CC tissues.
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DR EMBL; X78817; CAA55394.1; -; mRNA.
DR EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72778.1; -; Genomic_DNA.
DR EMBL; BC052303; AAH52303.1; -; mRNA.
DR EMBL; D50921; BAA09480.1; -; mRNA.
DR CCDS; CCDS14736.1; -. [P98171-1]
DR CCDS; CCDS55540.1; -. [P98171-2]
DR PIR; I38100; I38100.
DR RefSeq; NP_001158213.1; NM_001164741.1. [P98171-2]
DR RefSeq; NP_001657.3; NM_001666.4. [P98171-1]
DR PDB; 2EPD; NMR; -; A=746-814.
DR PDBsum; 2EPD; -.
DR AlphaFoldDB; P98171; -.
DR BMRB; P98171; -.
DR SMR; P98171; -.
DR BioGRID; 106886; 28.
DR DIP; DIP-41592N; -.
DR IntAct; P98171; 9.
DR MINT; P98171; -.
DR STRING; 9606.ENSP00000359045; -.
DR GlyGen; P98171; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; P98171; -.
DR PhosphoSitePlus; P98171; -.
DR BioMuta; ARHGAP4; -.
DR EPD; P98171; -.
DR jPOST; P98171; -.
DR MassIVE; P98171; -.
DR MaxQB; P98171; -.
DR PaxDb; P98171; -.
DR PeptideAtlas; P98171; -.
DR PRIDE; P98171; -.
DR ProteomicsDB; 57804; -. [P98171-1]
DR ProteomicsDB; 57805; -. [P98171-2]
DR Antibodypedia; 360; 130 antibodies from 30 providers.
DR DNASU; 393; -.
DR Ensembl; ENST00000350060.10; ENSP00000203786.8; ENSG00000089820.16. [P98171-1]
DR Ensembl; ENST00000370028.7; ENSP00000359045.3; ENSG00000089820.16. [P98171-2]
DR GeneID; 393; -.
DR KEGG; hsa:393; -.
DR MANE-Select; ENST00000350060.10; ENSP00000203786.8; NM_001666.5; NP_001657.3.
DR UCSC; uc004fjk.3; human. [P98171-1]
DR CTD; 393; -.
DR DisGeNET; 393; -.
DR GeneCards; ARHGAP4; -.
DR HGNC; HGNC:674; ARHGAP4.
DR HPA; ENSG00000089820; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 300023; gene.
DR neXtProt; NX_P98171; -.
DR OpenTargets; ENSG00000089820; -.
DR PharmGKB; PA24958; -.
DR VEuPathDB; HostDB:ENSG00000089820; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000182824; -.
DR HOGENOM; CLU_005715_1_1_1; -.
DR InParanoid; P98171; -.
DR OMA; CPPQRFD; -.
DR OrthoDB; 1245523at2759; -.
DR PhylomeDB; P98171; -.
DR TreeFam; TF315892; -.
DR PathwayCommons; P98171; -.
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; P98171; -.
DR SIGNOR; P98171; -.
DR BioGRID-ORCS; 393; 10 hits in 697 CRISPR screens.
DR ChiTaRS; ARHGAP4; human.
DR EvolutionaryTrace; P98171; -.
DR GeneWiki; ARHGAP4; -.
DR GenomeRNAi; 393; -.
DR Pharos; P98171; Tbio.
DR PRO; PR:P98171; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P98171; protein.
DR Bgee; ENSG00000089820; Expressed in granulocyte and 158 other tissues.
DR ExpressionAtlas; P98171; baseline and differential.
DR Genevisible; P98171; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0030517; P:negative regulation of axon extension; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR CDD; cd11956; SH3_srGAP4; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
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; IPR035678; srGAP4_SH3.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW GTPase activation; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..946
FT /note="Rho GTPase-activating protein 4"
FT /id="PRO_0000056701"
FT DOMAIN 19..317
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 507..695
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 746..805
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 187..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 128..195
FT /evidence="ECO:0000255"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 227
FT /note="K -> KLWPPQRPVAASSCAPVCWLQAGFLVHPPWWGAMCAPSTHQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042902"
FT VARIANT 104
FT /note="A -> V (in dbSNP:rs5987182)"
FT /id="VAR_028413"
FT CONFLICT 609
FT /note="A -> D (in Ref. 1; CAA55394)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="E -> D (in Ref. 1; CAA55394)"
FT /evidence="ECO:0000305"
FT STRAND 749..755
FT /evidence="ECO:0007829|PDB:2EPD"
FT STRAND 772..780
FT /evidence="ECO:0007829|PDB:2EPD"
FT STRAND 783..788
FT /evidence="ECO:0007829|PDB:2EPD"
FT STRAND 791..801
FT /evidence="ECO:0007829|PDB:2EPD"
SQ SEQUENCE 946 AA; 105026 MW; ED3D48C5DAA24969 CRC64;
MAAHGKLRRE RGLQAEYETQ VKEMRWQLSE QLRCLELQGE LRRELLQELA EFMRRRAEVE
LEYSRGLEKL AERFSSRGGR LGSSREHQSF RKEPSLLSPL HCWAVLLQHT RQQSRESAAL
SEVLAGPLAQ RLSHIAEDVG RLVKKSRDLE QQLQDELLEV VSELQTAKKT YQAYHMESVN
AEAKLREAER QEEKRAGRSV PTTTAGATEA GPLRKSSLKK GGRLVEKRQA KFMEHKLKCT
KARNEYLLSL ASVNAAVSNY YLHDVLDLMD CCDTGFHLAL GQVLRSYTAA ESRTQASQVQ
GLGSLEEAVE ALDPPGDKAK VLEVHATVFC PPLRFDYHPH DGDEVAEICV EMELRDEILP
RAQNIQSRLD RQTIETEEVN KTLKATLQAL LEVVASDDGD VLDSFQTSPS TESLKSTSSD
PGSRQAGRRR GQQQETETFY LTKLQEYLSG RSILAKLQAK HEKLQEALQR GDKEEQEVSW
TQYTQRKFQK SRQPRPSSQY NQRLFGGDME KFIQSSGQPV PLVVESCIRF INLNGLQHEG
IFRVSGAQLR VSEIRDAFER GEDPLVEGCT AHDLDSVAGV LKLYFRSLEP PLFPPDLFGE
LLASSELEAT AERVEHVSRL LWRLPAPVLV VLRYLFTFLN HLAQYSDENM MDPYNLAVCF
GPTLLPVPAG QDPVALQGRV NQLVQTLIVQ PDRVFPPLTS LPGPVYEKCM APPSASCLGD
AQLESLGADN EPELEAEMPA QEDDLEGVVE AVACFAYTGR TAQELSFRRG DVLRLHERAS
SDWWRGEHNG MRGLIPHKYI TLPAGTEKQV VGAGLQTAGE SGSSPEGLLA SELVHRPEPC
TSPEAMGPSG HRRRCLVPAS PEQHVEVDKA VAQNMDSVFK ELLGKTSVRQ GLGPASTTSP
SPGPRSPKAP PSSRLGRNKG FSRGPGAPAS PSASHPQGLD TTPKPH
