RHG21_MOUSE
ID RHG21_MOUSE Reviewed; 1944 AA.
AC Q6DFV3; A2AL67; Q80TD7; Q80XS1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Rho GTPase-activating protein 21;
DE AltName: Full=Rho GTPase-activating protein 10;
DE AltName: Full=Rho-type GTPase-activating protein 21;
GN Name=Arhgap21; Synonyms=Arhgap10, Kiaa1424;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Head;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 683-1944.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP PROTEIN SEQUENCE OF 1697-1708, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP INTERACTION WITH ARF1.
RX PubMed=17347647; DOI=10.1038/sj.emboj.7601634;
RA Menetrey J., Perderiset M., Cicolari J., Dubois T., Elkhatib N.,
RA El Khadali F., Franco M., Chavrier P., Houdusse A.;
RT "Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi
RT membranes.";
RL EMBO J. 26:1953-1962(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-917, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-850; SER-855;
RP SER-917; SER-919; SER-1426; SER-1655; THR-1668; THR-1901 AND SER-1905, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-568, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Functions as a GTPase-activating protein (GAP) for RHOA and
CC CDC42. Downstream partner of ARF1 which may control Golgi apparatus
CC structure and function. Also required for CTNNA1 recruitment to
CC adherens junctions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTNNA1 (By similarity). Interacts with GTP-
CC bound ARF1 and probably ARF6. {ECO:0000250,
CC ECO:0000269|PubMed:17347647}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell junction {ECO:0000250}.
CC Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localization
CC to the Golgi is dependent on interaction with GTP-bound ARF1.
CC {ECO:0000250}.
CC -!- PTM: Sumoylated with SUMO2 and SUMO3 in proliferating lymphocytes.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM13451.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM16533.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM24301.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX649226; CAM13451.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL773540; CAM13451.1; JOINED; Genomic_DNA.
DR EMBL; AL929100; CAM13451.1; JOINED; Genomic_DNA.
DR EMBL; AL773540; CAM16533.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL929100; CAM16533.1; JOINED; Genomic_DNA.
DR EMBL; BX649226; CAM16533.1; JOINED; Genomic_DNA.
DR EMBL; AL929100; CAM24301.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL773540; CAM24301.1; JOINED; Genomic_DNA.
DR EMBL; BX649226; CAM24301.1; JOINED; Genomic_DNA.
DR EMBL; BC043038; AAH43038.1; -; mRNA.
DR EMBL; BC076629; AAH76629.1; -; mRNA.
DR EMBL; AK122508; BAC65790.1; -; Transcribed_RNA.
DR RefSeq; NP_001074833.3; NM_001081364.3.
DR AlphaFoldDB; Q6DFV3; -.
DR SMR; Q6DFV3; -.
DR BioGRID; 214707; 45.
DR IntAct; Q6DFV3; 5.
DR MINT; Q6DFV3; -.
DR STRING; 10090.ENSMUSP00000133851; -.
DR iPTMnet; Q6DFV3; -.
DR PhosphoSitePlus; Q6DFV3; -.
DR SwissPalm; Q6DFV3; -.
DR EPD; Q6DFV3; -.
DR jPOST; Q6DFV3; -.
DR MaxQB; Q6DFV3; -.
DR PaxDb; Q6DFV3; -.
DR PRIDE; Q6DFV3; -.
DR ProteomicsDB; 255264; -.
DR GeneID; 71435; -.
DR KEGG; mmu:71435; -.
DR CTD; 57584; -.
DR MGI; MGI:1918685; Arhgap21.
DR eggNOG; KOG4407; Eukaryota.
DR InParanoid; Q6DFV3; -.
DR OrthoDB; 142586at2759; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR BioGRID-ORCS; 71435; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Arhgap21; mouse.
DR PRO; PR:Q6DFV3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6DFV3; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0051683; P:establishment of Golgi localization; ISO:MGI.
DR GO; GO:0051645; P:Golgi localization; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0051684; P:maintenance of Golgi location; ISO:MGI.
DR GO; GO:0072384; P:organelle transport along microtubule; ISO:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
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 Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Golgi apparatus; GTPase activation;
KW Isopeptide bond; Membrane; Methylation; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1944
FT /note="Rho GTPase-activating protein 21"
FT /id="PRO_0000305246"
FT DOMAIN 55..164
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 924..1033
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1140..1332
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 25..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..1090
FT /note="Interaction with ARF1 and ARF6"
FT /evidence="ECO:0000250"
FT REGION 1079..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1847
FT /note="Interaction with CTNNA1"
FT /evidence="ECO:0000250"
FT REGION 1648..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1845..1944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1741..1761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1865..1931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 548
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 568
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 740
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 875
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 1425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 1426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1503
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 1655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1668
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5U3"
FT MOD_RES 1901
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1905
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 1437
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CONFLICT 1491
FT /note="P -> S (in Ref. 1; AAH43038, 2 and 3; BAC65790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1944 AA; 215743 MW; A7F832ECD3DBC081 CRC64;
MATHWTGLPE EDGDKLKACG AASACEVSKN KDGKDQGEPV SPSEDEPFSW PGPKTVMLKR
TSQGFGFTLR HFIVYPPESA IQFSYKDEEN GNRGGKQRNR LEPMDTIFVK QVKEGGPAFE
AGLCTGDRII KVNGESVIGK TYSQVIALIQ NSDTTLELSV MPKDEDILQV AYSQDAYLKG
NEAYSGNARN IPEPPPVCYP WLPSTPSATA QPVETCPPDS LPNKQQTSAP VLTQPGRAYR
MEIQVPPSPT DVAKSNTAVC VCNESVRTVI VPSEKVVDLL ANRNNPSGPS HRTEEVRYGV
NEQASTKAAS RTTSPASVPT AHLIHQTTGS RSLEPSGILL KSGNYSGHSE GISSSRSQAV
DSPPVSVNHY SANSHQHIDW KNYKTYKEYI DNRRLHIGCR TIQERLDSLR AASQSAADYN
QVVPTRTTLQ VRRRSTSHDR VPQSVQIRQR SVSQERLEDS VLMKYCPRSA SQGALTSPPV
SFNNHRTRSW DYIEGQTEAT ATVNSESQIP DSNGERKQTY KWSGFTEQDD RRGIHERPRQ
QEMHKPFRGS NLTVAPVVNS DNRRLVGRGV GPVSQFKKIP PDLRPPHSNR NFPTTTGVSL
QRGIAQDRSP LVKVRSNSLK VPPPPVSKPS FSQHSLASMK DQRPVNHLHQ HSVLSQQTQF
RSESTFEHQL ETEVSSCLPG TSAKTSPQLS ENLGTSDLEL PAIPRNGDIN LQEAEIQQPD
VLDNKESVIL REKPQSGRQT PQPLRHQSYI LAVNDQETGS DTTCWLPNDA RREVHIKRME
ERKASSTSPP GDSLASIPFI DEPTSPSIDH EIAHIPASAV ISASTAHVPS IATVPPSLTT
SAPLIRRQLS HDQESVGPPS LDGQHSSKTE RSKSYDEGLD DYREDAKLSF KHVSSLKGIK
ITDSQKSSED SGSRKGSSSE VFSDAAREGW LQFRPLVTDK GKRVGGSIRP WKQMYVVLRG
HSLYLYKDRR EQTTPSEEEQ PISVNACLID ISYSETKRRN VFRLTTSDCE CLFQAEDRDD
MLSWIKTIQE SSNLNEEDTG VTNRDLISRR IKEYNSLLSK TEQLPKTPRQ SLSIRQTLLG
AKSEPKTQSP HSPKEESERK LLSKDDTSPP KDKGTWRRGI PSIVRKTFEK KPAATGTFGV
RLDDCPPAHT NRYIPLIVDI CCKLVEERGL EYTGIYRVPG NNAAISSMQE ELNKGMADID
IQDDKWRDLN VISSLLKSFF RKLPEPLFTN DKYADFIEAN RKEDPLDRLR TLKRLIHDLP
EHHFETLKFL SAHLKTVAEN SEKNKMEPRN LAIVFGPTLV RTSEDNMTHM VTHMPDQYKI
VETLIQHHDW FFTEEGAEEP LTAVQEENTV DSQPVPNIDH LLTNIGRTGV LPGDVSDSAT
SDSAKSKGSW GSGKDQYSRE LLVSSIFAAA SRKRKKPKEK AQPSSSEDEL DSVFFKKENT
EQSHSEIKEE SKRESETSGS KQRVVVAKES NTKKDSGTTK EEKKIPWEEP PPPHSSKRNR
SPTLSCRLAM LKEGPRSLLT QKPHCEETGS DSGTLLSTSS QASLLRSSTK KSTSPETKHS
EFLSIAGTTT SDYSTTSSTT YLTSLDSSRL SPEVQSVAES KGDEADDERS ELVSEGRPVE
TDSESEFPVF PTTLTSDRLF RGKFQEVARV SRRNSEGSEA SCTEGSLTPS LDSRRQQFSS
HRLIECDTLS RKKSARFKSD SGSPGDTRTE KETPALAKMF DVMKKGKSTG SLLTPSRSES
EKQEATWKTK IADRLKLRPR APADDMFGVG NQKPTAETAK RKNIKRRHTL GGHRDATEIS
VLSFWKAHEQ SADKESELSA VNRLKPKCSA QDLSISDWLA RERVRTSASD LSRGEGLEPQ
AESPSVLGTP ISTHSPPSQQ PEARVAATST LASTSQSPLF TPPQSPDQIN RESFQNMSQN
ASSTANIHPH KQSESPDTKA ETPP
