ID RHG35_CANLF Reviewed; 1500 AA.
AC P83509;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Rho GTPase-activating protein 35 {ECO:0000250|UniProtKB:Q9NRY4};
DE AltName: Full=Glucocorticoid receptor DNA-binding factor 1 {ECO:0000303|PubMed:12234678};
DE AltName: Full=Rho GAP p190A;
DE Short=p190-A;
GN Name=ARHGAP35 {ECO:0000250|UniProtKB:Q9NRY4};
GN Synonyms=GRLF1 {ECO:0000250|UniProtKB:Q9NRY4},
GN P190A {ECO:0000250|UniProtKB:Q9NRY4},
GN p190ARHOGAP {ECO:0000250|UniProtKB:Q9NRY4};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000312|EMBL:AAN16354.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=12234678; DOI=10.1016/s0378-1119(02)00765-5;
RA Zangerl B., Zhang Q., Pearce-Kelling S.E., Aguirre G.D.;
RT "Molecular cloning, characterization and mapping of the canine
RT glucocorticoid receptor DNA binding factor 1 (GRLF1).";
RL Gene 294:167-176(2002).
CC -!- FUNCTION: Rho GTPase-activating protein (GAP). Binds several acidic
CC phospholipids which inhibits the Rho GAP activity to promote the Rac
CC GAP activity. This binding is inhibited by phosphorylation by PRKCA (By
CC similarity). Involved in cell differentiation as well as cell adhesion
CC and migration, plays an important role in retinal tissue morphogenesis,
CC neural tube fusion, midline fusion of the cerebral hemispheres and
CC mammary gland branching morphogenesis (By similarity). Transduces
CC signals from p21-ras to the nucleus, acting via the ras GTPase-
CC activating protein (GAP) (By similarity). Transduces SRC-dependent
CC signals from cell-surface adhesion molecules, such as laminin, to
CC promote neurite outgrowth. Regulates axon outgrowth, guidance and
CC fasciculation (By similarity). Modulates Rho GTPase-dependent F-actin
CC polymerization, organization and assembly, is involved in polarized
CC cell migration and in the positive regulation of ciliogenesis and cilia
CC elongation (By similarity). During mammary gland development, is
CC required in both the epithelial and stromal compartments for ductal
CC outgrowth (By similarity). Represses transcription of the
CC glucocorticoid receptor by binding to the cis-acting regulatory
CC sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this function is however
CC unclear and would need additional experimental evidences (By
CC similarity). {ECO:0000250|UniProtKB:P81128,
CC ECO:0000250|UniProtKB:Q91YM2, ECO:0000250|UniProtKB:Q9NRY4}.
CC -!- SUBUNIT: Interacts with RASA1 (By similarity). Interacts with the
CC general transcription factor GTF2I, the interaction sequesters GTF2I in
CC the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q91YM2,
CC ECO:0000250|UniProtKB:Q9NRY4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q91YM2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q91YM2}. Nucleus {ECO:0000250|UniProtKB:Q91YM2}.
CC Cell membrane {ECO:0000250|UniProtKB:Q91YM2}. Note=In response to
CC integrins and SDC4 and upon phosphorylation by PKC, relocalizes from
CC the cytoplasm to regions of plasma membrane ruffling where it
CC colocalizes with polymerized actin. {ECO:0000250|UniProtKB:Q91YM2}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in retina (photoreceptor layer)
CC and brain. Expression is maximal in the occipital, frontal, temporal
CC lobe and also the cerebellum. Medium expression in the medulla and also
CC in kidney, lung, liver, heart and spleen.
CC {ECO:0000269|PubMed:12234678}.
CC -!- DOMAIN: N-terminal part (1-266) has GTPase activity. Required for
CC proper cellular localization. {ECO:0000250|UniProtKB:Q91YM2}.
CC -!- DOMAIN: The pG1 pseudoGTPase domain does not bind GTP.
CC {ECO:0000250|UniProtKB:Q6NU25}.
CC -!- PTM: Phosphorylation of Tyr-1106 by PTK6 promotes the association with
CC RASA1, inactivating RHOA while activating RAS. Phosphorylation at Tyr-
CC 308 by PDGFRA inhibits binding to GTF2I (By similarity). Phosphorylated
CC by PRKCA at Ser-1222 and Thr-1227, induces relocalization from the
CC cytoplasm to regions of plasma membrane ruffling and prevents the
CC binding and substrate specificity regulation by phospholipids. In
CC brain, phosphorylated by FYN and SRC (By similarity). During focal
CC adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal
CC region, probably at Ser-1452, Ser-1477, Thr-1481 and Ser-1484.
CC Phosphorylation by MAPK1 and MAPK3 inhibits GAP function and localizes
CC ARGHAP35 away from newly forming focal adhesions and stress fibers in
CC cells spreading on fibronectin (By similarity). Phosphorylation at Ser-
CC 1477 and Thr-1481 by GSK3B requires priming by MAPK and inhibits RhoGAP
CC activity and modulates polarized cell migration (By similarity).
CC {ECO:0000250|UniProtKB:P81128, ECO:0000250|UniProtKB:Q91YM2,
CC ECO:0000250|UniProtKB:Q9NRY4}.
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DR EMBL; AF483595; AAN16354.1; -; mRNA.
DR EMBL; AY079157; AAL91068.1; -; Genomic_DNA.
DR EMBL; AY079158; AAL91069.1; -; Genomic_DNA.
DR RefSeq; NP_001003022.1; NM_001003022.1.
DR AlphaFoldDB; P83509; -.
DR BMRB; P83509; -.
DR SMR; P83509; -.
DR STRING; 9615.ENSCAFP00000036971; -.
DR PaxDb; 9612-ENSCAFP00000036971; -.
DR Ensembl; ENSCAFT00000006727.5; ENSCAFP00000006228.3; ENSCAFG00000004190.6.
DR Ensembl; ENSCAFT00030013717.1; ENSCAFP00030011972.1; ENSCAFG00030007402.1.
DR Ensembl; ENSCAFT00040004921.1; ENSCAFP00040004225.1; ENSCAFG00040002575.1.
DR Ensembl; ENSCAFT00805006073; ENSCAFP00805004662; ENSCAFG00805003294.
DR Ensembl; ENSCAFT00845005450.1; ENSCAFP00845004333.1; ENSCAFG00845003086.1.
DR GeneID; 403543; -.
DR KEGG; cfa:403543; -.
DR CTD; 2909; -.
DR VEuPathDB; HostDB:ENSCAFG00845003086; -.
DR VGNC; VGNC:38060; ARHGAP35.
DR eggNOG; KOG4271; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_004268_0_0_1; -.
DR InParanoid; P83509; -.
DR OrthoDB; 5405671at2759; -.
DR Reactome; R-CFA-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-CFA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-CFA-8980692; RHOA GTPase cycle.
DR Reactome; R-CFA-9013026; RHOB GTPase cycle.
DR Reactome; R-CFA-9013106; RHOC GTPase cycle.
DR Reactome; R-CFA-9013148; CDC42 GTPase cycle.
DR Reactome; R-CFA-9013149; RAC1 GTPase cycle.
DR Reactome; R-CFA-9013404; RAC2 GTPase cycle.
DR Reactome; R-CFA-9013405; RHOD GTPase cycle.
DR Reactome; R-CFA-9013408; RHOG GTPase cycle.
DR Reactome; R-CFA-9013409; RHOJ GTPase cycle.
DR Reactome; R-CFA-9696264; RND3 GTPase cycle.
DR Reactome; R-CFA-9696270; RND2 GTPase cycle.
DR Reactome; R-CFA-9696273; RND1 GTPase cycle.
DR Proteomes; UP000002254; Chromosome 1.
DR Proteomes; UP000694429; Chromosome 1.
DR Proteomes; UP000694542; Chromosome 1.
DR Proteomes; UP000805418; Chromosome 1.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; ISS:UniProtKB.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; ISS:UniProtKB.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISS:UniProtKB.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0030879; P:mammary gland development; ISS:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0097485; P:neuron projection guidance; ISS:UniProtKB.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; ISS:UniProtKB.
DR GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0008361; P:regulation of cell size; IBA:GO_Central.
DR GO; GO:0042478; P:regulation of eye photoreceptor cell development; NAS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
DR CDD; cd22221; pseudoGTPaseD_p190RhoGAP-A; 1.
DR CDD; cd04373; RhoGAP_p190; 1.
DR Gene3D; 1.10.10.440; FF domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039007; pG1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR032835; RhoGAP-FF1.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR045786; RhoGAP_pG1_pG2.
DR InterPro; IPR039006; RhoGAP_pG2.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR PANTHER; PTHR46005:SF1; RHO GTPASE-ACTIVATING PROTEIN 35; 1.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16512; RhoGAP-FF1; 1.
DR Pfam; PF19518; RhoGAP_pG1_pG2; 1.
DR SMART; SM00441; FF; 4.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF81698; FF domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51676; FF; 4.
DR PROSITE; PS51852; PG1; 1.
DR PROSITE; PS51853; PG2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; DNA-binding;
KW GTP-binding; GTPase activation; Lipid-binding; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1500
FT /note="Rho GTPase-activating protein 35"
FT /id="PRO_0000056729"
FT DOMAIN 270..327
FT /note="FF 1"
FT /evidence="ECO:0000305"
FT DOMAIN 368..422
FT /note="FF 2"
FT DOMAIN 429..483
FT /note="FF 3"
FT /evidence="ECO:0000305"
FT DOMAIN 485..550
FT /note="FF 4"
FT DOMAIN 592..767
FT /note="pG1 pseudoGTPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01199"
FT DOMAIN 783..947
FT /note="pG2 pseudoGTPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01200"
FT DOMAIN 1250..1437
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..266
FT /note="Has GTPase activity, required for proper
FT localization"
FT /evidence="ECO:0000250|UniProtKB:Q91YM2"
FT REGION 970..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1237
FT /note="Required for phospholipid binding and regulation of
FT the substrate preference"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT REGION 1444..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1486
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 33..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 95..97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 201..203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 229..231
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 308
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YM2"
FT MOD_RES 1002
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1073
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1088
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1106
FT /note="Phosphotyrosine; by ABL2 and PTK6"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YM2"
FT MOD_RES 1151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1227
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT MOD_RES 1473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YM2"
FT MOD_RES 1477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YM2"
FT MOD_RES 1481
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91YM2"
FT MOD_RES 1484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YM2"
SQ SEQUENCE 1500 AA; 170428 MW; EB3AB65FE36E2F18 CRC64;
MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF HLDHTSVLST
SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI DDQTFQPHRS TALQPYIKRA
AATKLASAEK LMYFCTDQLG LEQDFEQKQM PDGKLLIDGF LLGIDVSRGM NRNFDDQLKF
VSNLYNQLAK TKKPIVVVLT KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF
STLVQLIDKS RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWLSVSRKMQ
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEIDH
LSCIKTKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE RIPFDLMDTV PAEQLYEAHL
EKLRNERKRA EMRRAFKENL ETSPFITPGK PWEEARSFIM NEDFYQWLEE SVYMDIYGKH
QKQIIDKAKE EFQELLLEYS ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER
DALILKHIHF VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDPNIDRINL
VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS FQTPTFQPHG
CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL ILVNKRGDTS GETLHSLIQQ
GQQIASKLQC VFLDPASAGI GYGRNINEKQ ISQVLKGLLD SKRNLNLVSS TASIKDLADV
DLRIVMCLMC GDPFSADDIL FPVLQSQTCK SSHCGSNNSV LLELPIGLHK KRIELSILSY
HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAIDVLDNDL
SREQLSEGEE IAQEIDGRFT SIPCSQPQHK LEIFHPFFKD VVDKKNIIEA THMYDNAAEA
CSTTEEVFNS PRAGSPLCNS NLQDSEEDIE PPSYSLFRED TSLPSLSKDH SKLSMELEGN
DGLSFIMSNF ESKLNNKVPP PVKPKPPVQF DITKGDLSYL DQGHRDGQRK SVSSSTWLPP
DGFDPSDYAE PMDAVVKPRN EEENIYSVPH DSTQGKIITI RNINKAQSNG SGNGSDSEMD
TSSLERGRKV SIVSKPVLYR TRCSRLGRFA SYRTSFSVGS DDELGPIRKK EEDQASQGYK
GDNAVIPYET DEDPRRRNIL RSLRRNTKKP KPKPRPSITK ATWESNYFGV PLTTVVTPEK
PIPVFIERCI EYIEATGLST EGIYRVSGNK SEMESLQRQF DQDHNLDLAE KDFTVNTVAG
AMKSFFSELP DPLVPYNMQI DLVEAHKIND REQKLHALKE VLKKFPKENH EVFKYVISHL
NKVSHNNKVN LMTSENLSIC FWPTLMRPDF STMDALTATR TYQTIIELFI QQCPFFFHNR
PISEPPGATP SSPSAVASTV PFLTSTPVTS QPSPPQSPPP TPQSPMQALL PSQLQAEHTL
//
