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RHG20_HUMAN
ID   RHG20_HUMAN             Reviewed;        1191 AA.
AC   Q9P2F6; A8K8C5; B0YIW7; B0YIW8; Q6RJU1; Q6RJU2; Q6RJU3; Q6RJU5; Q8IXS1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Rho GTPase-activating protein 20;
DE   AltName: Full=Rho-type GTPase-activating protein 20;
GN   Name=ARHGAP20; Synonyms=KIAA1391;
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] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND CHROMOSOMAL TRANSLOCATION WITH BRWD3.
RX   PubMed=15543602; DOI=10.1002/gcc.20131;
RA   Kalla C., Nentwich H., Schlotter M., Mertens D., Wildenberger K.,
RA   Doehner H., Stilgenbauer S., Lichter P.;
RT   "Translocation t(X;11)(q13;q23) in B-cell chronic lymphocytic leukemia
RT   disrupts two novel genes.";
RL   Genes Chromosomes Cancer 42:128-143(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 436-1185 (ISOFORMS 1/2/3/4).
RC   TISSUE=Testis;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 436-1185 (ISOFORMS 1/2/3/4), AND
RP   VARIANT ASP-632.
RC   TISSUE=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   [7]
RP   IDENTIFICATION.
RX   PubMed=14532992;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of human KIAA1391 and mouse Kiaa1391
RT   genes encoding novel RhoGAP family proteins with RA domain and ANXL
RT   repeats.";
RL   Int. J. Oncol. 23:1471-1476(2003).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC       to an inactive GDP-bound state. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=1ad;
CC         IsoId=Q9P2F6-1; Sequence=Displayed;
CC       Name=2; Synonyms=1be;
CC         IsoId=Q9P2F6-2; Sequence=VSP_024294;
CC       Name=3; Synonyms=1c;
CC         IsoId=Q9P2F6-3; Sequence=VSP_024295;
CC       Name=4; Synonyms=1e, 1d;
CC         IsoId=Q9P2F6-4; Sequence=VSP_024296;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the brain. Lower
CC       expression is found in lymph nodes. {ECO:0000269|PubMed:15543602}.
CC   -!- DEVELOPMENTAL STAGE: Low expression is found in fetal liver.
CC       {ECO:0000269|PubMed:15543602}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ARHGAP20 may be a
CC       cause of B-cell chronic lymphocytic leukemia (B-CLL) (PubMed:15543602).
CC       Translocation t(X;11)(q21;q23) with BRWD3 does not result in fusion
CC       transcripts but disrupts both genes (PubMed:15543602).
CC       {ECO:0000269|PubMed:15543602}.
CC   -!- CAUTION: The translocation involving this gene was originally published
CC       as t(X;11)(q13;23), but BRWD3 is localized to Xq21 and not to Xq13.
CC       {ECO:0000305|PubMed:15543602}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH39340.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH39340.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC       Sequence=BAA92629.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAF84979.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAF84979.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ARHGAP20ID42979ch11q23.html";
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DR   EMBL; AY496263; AAS45466.1; -; mRNA.
DR   EMBL; AY496264; AAS45467.1; -; mRNA.
DR   EMBL; AY496265; AAS45468.1; -; mRNA.
DR   EMBL; AY496266; AAS45469.1; -; mRNA.
DR   EMBL; AY496267; AAS45470.1; -; mRNA.
DR   EMBL; AB037812; BAA92629.1; ALT_INIT; mRNA.
DR   EMBL; EF444953; ACA05945.1; -; Genomic_DNA.
DR   EMBL; EF444953; ACA05946.1; -; Genomic_DNA.
DR   EMBL; CH471065; EAW67134.1; -; Genomic_DNA.
DR   EMBL; AK292290; BAF84979.1; ALT_SEQ; mRNA.
DR   EMBL; BC039340; AAH39340.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS31673.1; -. [Q9P2F6-1]
DR   CCDS; CCDS58175.1; -. [Q9P2F6-4]
DR   CCDS; CCDS58176.1; -. [Q9P2F6-2]
DR   CCDS; CCDS58177.1; -. [Q9P2F6-3]
DR   PIR; C59436; C59436.
DR   RefSeq; NP_001245344.1; NM_001258415.1. [Q9P2F6-3]
DR   RefSeq; NP_001245345.1; NM_001258416.1. [Q9P2F6-2]
DR   RefSeq; NP_001245346.1; NM_001258417.1. [Q9P2F6-4]
DR   RefSeq; NP_001245347.1; NM_001258418.1. [Q9P2F6-4]
DR   RefSeq; NP_065860.2; NM_020809.3. [Q9P2F6-1]
DR   RefSeq; XP_006718956.1; XM_006718893.3.
DR   PDB; 3MSX; X-ray; 1.65 A; B=351-551.
DR   PDBsum; 3MSX; -.
DR   AlphaFoldDB; Q9P2F6; -.
DR   SMR; Q9P2F6; -.
DR   BioGRID; 121622; 27.
DR   IntAct; Q9P2F6; 12.
DR   STRING; 9606.ENSP00000260283; -.
DR   iPTMnet; Q9P2F6; -.
DR   PhosphoSitePlus; Q9P2F6; -.
DR   BioMuta; ARHGAP20; -.
DR   DMDM; 143458429; -.
DR   jPOST; Q9P2F6; -.
DR   MassIVE; Q9P2F6; -.
DR   PaxDb; Q9P2F6; -.
DR   PeptideAtlas; Q9P2F6; -.
DR   PRIDE; Q9P2F6; -.
DR   ProteomicsDB; 83803; -. [Q9P2F6-1]
DR   ProteomicsDB; 83804; -. [Q9P2F6-2]
DR   ProteomicsDB; 83805; -. [Q9P2F6-3]
DR   ProteomicsDB; 83806; -. [Q9P2F6-4]
DR   Antibodypedia; 32015; 127 antibodies from 27 providers.
DR   DNASU; 57569; -.
DR   Ensembl; ENST00000260283.8; ENSP00000260283.4; ENSG00000137727.13. [Q9P2F6-1]
DR   Ensembl; ENST00000524756.5; ENSP00000432076.1; ENSG00000137727.13. [Q9P2F6-3]
DR   Ensembl; ENST00000527598.1; ENSP00000431399.1; ENSG00000137727.13. [Q9P2F6-4]
DR   Ensembl; ENST00000528829.5; ENSP00000436319.1; ENSG00000137727.13. [Q9P2F6-4]
DR   Ensembl; ENST00000533353.5; ENSP00000436522.1; ENSG00000137727.13. [Q9P2F6-2]
DR   Ensembl; ENST00000683387.1; ENSP00000507405.1; ENSG00000137727.13. [Q9P2F6-1]
DR   GeneID; 57569; -.
DR   KEGG; hsa:57569; -.
DR   MANE-Select; ENST00000683387.1; ENSP00000507405.1; NM_001384657.1; NP_001371586.1.
DR   UCSC; uc001pky.3; human. [Q9P2F6-1]
DR   CTD; 57569; -.
DR   DisGeNET; 57569; -.
DR   GeneCards; ARHGAP20; -.
DR   HGNC; HGNC:18357; ARHGAP20.
DR   HPA; ENSG00000137727; Low tissue specificity.
DR   MIM; 609568; gene.
DR   neXtProt; NX_Q9P2F6; -.
DR   OpenTargets; ENSG00000137727; -.
DR   PharmGKB; PA134963885; -.
DR   VEuPathDB; HostDB:ENSG00000137727; -.
DR   eggNOG; KOG4724; Eukaryota.
DR   GeneTree; ENSGT00940000154633; -.
DR   HOGENOM; CLU_008526_0_0_1; -.
DR   InParanoid; Q9P2F6; -.
DR   OrthoDB; 148399at2759; -.
DR   PhylomeDB; Q9P2F6; -.
DR   TreeFam; TF331062; -.
DR   PathwayCommons; Q9P2F6; -.
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; Q9P2F6; -.
DR   SIGNOR; Q9P2F6; -.
DR   BioGRID-ORCS; 57569; 8 hits in 1070 CRISPR screens.
DR   EvolutionaryTrace; Q9P2F6; -.
DR   GenomeRNAi; 57569; -.
DR   Pharos; Q9P2F6; Tbio.
DR   PRO; PR:Q9P2F6; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9P2F6; protein.
DR   Bgee; ENSG00000137727; Expressed in cortical plate and 157 other tissues.
DR   ExpressionAtlas; Q9P2F6; baseline and differential.
DR   Genevisible; Q9P2F6; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005096; F:GTPase activator 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   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromosomal rearrangement;
KW   GTPase activation; Phosphoprotein; Reference proteome; Tumor suppressor.
FT   CHAIN           1..1191
FT                   /note="Rho GTPase-activating protein 20"
FT                   /id="PRO_0000283086"
FT   DOMAIN          78..180
FT                   /note="PH"
FT   DOMAIN          194..295
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT   DOMAIN          365..551
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          925..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1052..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1140..1191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..783
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..979
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1013
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1053..1067
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IFT4"
FT   MOD_RES         704
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IFT4"
FT   MOD_RES         730
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IFT4"
FT   VAR_SEQ         1..36
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15543602"
FT                   /id="VSP_024296"
FT   VAR_SEQ         1..34
FT                   /note="MEAMSPQQETLGGQPGRSSSLTGVSRLAGGSCTK -> MTFWIIIN (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15543602"
FT                   /id="VSP_024294"
FT   VAR_SEQ         1..33
FT                   /note="MEAMSPQQETLGGQPGRSSSLTGVSRLAGGSCT -> MSARERQPAL (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15543602"
FT                   /id="VSP_024295"
FT   VARIANT         522
FT                   /note="A -> T (in dbSNP:rs7936020)"
FT                   /id="VAR_031489"
FT   VARIANT         632
FT                   /note="G -> D (in dbSNP:rs17853925)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_031490"
FT   HELIX           367..370
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           372..374
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           378..390
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           391..393
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   TURN            395..399
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           404..415
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           427..439
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   TURN            442..447
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           448..450
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           451..456
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           457..459
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   STRAND          460..462
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           463..474
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           479..496
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           499..502
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           506..517
FT                   /evidence="ECO:0007829|PDB:3MSX"
FT   HELIX           526..550
FT                   /evidence="ECO:0007829|PDB:3MSX"
SQ   SEQUENCE   1191 AA;  132608 MW;  1837B9DF0655AF41 CRC64;
     MEAMSPQQET LGGQPGRSSS LTGVSRLAGG SCTKKKMKTL AERRRSAPSL ILDKALQKRP
     TTRDSPSASV DTCTFLSSLV CSNRTLLIDG RAELKRGLQR QERHLFLFND LFVVAKIKYN
     NNFKIKNKIK LTDMWTASCV DEVGEGNTNA MKSFVLGWPT VNFVATFSSP EQKDKWLSLL
     QRYINLEKEK DYPKSIPLKI FAKDIGNCAY SKTITVMNSD TANEVINMSL PMLGITGSER
     DYQLWVNSGK EEAPYPLIGH EYPYGIKMSH LRDSALLTPG SKDSTTPFNL QEPFLMEQLP
     REMQCQFILK PSRLAAAQQL SDSGHKTFKR RRSIINWAFW RGSSTHLDNL PSSPTSPMPG
     QLFGISLPNI CENDNLPKPV LDMLFFLNQK GPLTKGIFRQ SANVKSCREL KEKLNSGVEV
     HLDCESIFVI ASVLKDFLRN IPGSIFSSDL YDHWVSVMDQ GNDEEKINTV QRLLDQLPRA
     NVVLLRYLFG VLHNIEQHSS SNQMTAFNLA VCVAPSILWP PASSSPELEN EFTKKVSLLI
     QFLIENCLRI FGEEITSLFR EVSVRCDTRE NASDISCFQL NDSSYDSLEN ELNEDVDAPC
     SDLVKKLGQG SRSMDSVLTL SDYDLDQPEV EGLLTLSDFD LAHSKDEDVQ MKRPLESKPV
     NILVYTKIPL RDHARAPSAM CTPSYLSTAA ANAAKSLRRH RRCSEPSIDY LDSKLSYLRE
     FYQKKLRKSS CDAILSQKDE DYLKQNQPLQ EEGKTCFKQS LVTGTDVSKK NATTQNTKKK
     SLSGSEGNHV KLFPKSKPVA ISVASYSPMS SQDHSKNQPF DVNTSGYSPP HTADALKGPR
     THRRCSEPNI EDQNRKLTYL RGIYSKKQHK TSCEAGLLHG EEDYLKRHKS LQMEGQKLIN
     QSLVMGIEVG KSSATNQNTE KVLPPRLNLC PRTSYSSLSS PGTSPSGSSV SSQDSAFSQI
     SEHSVFTPTE TSSPIDCTFQ AQRKREDLSP DFSNASHVSG MPGPSSGQAC SRPAYTKKDT
     MEWHSQMHSV TLHPSTWLRN GVASLKNWSL KKKAKAARPE EEKIASPKGP LEPPPHASGV
     PEANSLQEEQ KDLPLRAAEG LSPVQSAQRC SSSPFQDSER HCSSPFSLVE SRLKLCMKSH
     EEIEPGSQSS SGSLPWERAS ASSWTLEDAT SPDSGPTVVC DIEDRYLTKD I
 
 
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