RASH_RAT
ID RASH_RAT Reviewed; 189 AA.
AC P20171; Q4KLL6; Q5RJJ8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=GTPase HRas;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE AltName: Full=H-Ras-1;
DE AltName: Full=Transforming protein p21;
DE AltName: Full=c-H-ras;
DE AltName: Full=p21ras;
DE Contains:
DE RecName: Full=GTPase HRas, N-terminally processed;
DE Flags: Precursor;
GN Name=Hras; Synonyms=Hras1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3023901; DOI=10.1128/mcb.6.5.1706-1710.1986;
RA Ruta M., Wolford R., Dhar R., Defeo-Jones D., Ellis R.W., Scolnick E.M.;
RT "Nucleotide sequence of the two rat cellular rasH genes.";
RL Mol. Cell. Biol. 6:1706-1710(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Thymus;
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 [GENOMIC DNA] OF 1-37.
RX PubMed=3027702; DOI=10.1073/pnas.84.3.774;
RA Damante G., Filetti S., Rapoport B.;
RT "Nucleotide sequence and characterization of the 5' flanking region of the
RT rat Ha-ras protooncogene.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:774-778(1987).
RN [4]
RP ISOPRENYLATION AT CYS-186, CLEAVAGE, AND METHYLATION AT CYS-186.
RX PubMed=3290900; DOI=10.1073/pnas.85.13.4643;
RA Clarke S., Vogel J.P., Deschenes R.J., Stock J.;
RT "Posttranslational modification of the Ha-ras oncogene protein: evidence
RT for a third class of protein carboxyl methyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4643-4647(1988).
RN [5]
RP INTERACTION WITH PLCE1, AND MUTAGENESIS OF ASN-26; THR-35; GLU-37; ASP-38;
RP TYR-40; GLN-61 AND CYS-186.
RX PubMed=11179219; DOI=10.1093/emboj/20.4.743;
RA Kelley G.G., Reks S.E., Ondrako J.M., Smrcka A.V.;
RT "Phospholipase C(epsilon): a novel Ras effector.";
RL EMBO J. 20:743-754(2001).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH BRAF; MAP2K1; MAPK3 AND RGS14, AND
RP INTERACTION WITH RGS14.
RX PubMed=19319189; DOI=10.1371/journal.pone.0004884;
RA Willard F.S., Willard M.D., Kimple A.J., Soundararajan M., Oestreich E.A.,
RA Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J., Zylka M.J.,
RA Snider W.D., Siderovski D.P.;
RT "Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras
RT effector.";
RL PLoS ONE 4:E4884-E4884(2009).
RN [7]
RP INTERACTION WITH RGS14, AND SUBCELLULAR LOCATION.
RX PubMed=19878719; DOI=10.1016/j.cellsig.2009.10.005;
RA Shu F.J., Ramineni S., Hepler J.R.;
RT "RGS14 is a multifunctional scaffold that integrates G protein and Ras/Raf
RT MAPkinase signalling pathways.";
RL Cell. Signal. 22:366-376(2010).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P01112};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBUNIT: Forms a signaling complex with RASGRP1 and DGKZ (By
CC similarity). In its GTP-bound form interacts with PLCE1
CC (PubMed:11179219). Interacts with TBC1D10C (By similarity). Interacts
CC with RGL3 and RASSF5 (By similarity). Interacts with HSPD1 (By
CC similarity). Interacts with PDE6D (By similarity). Interacts with IKZF3
CC (By similarity). Interacts with RACK1 (By similarity). Found in a
CC complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14
CC (PubMed:19319189). Interacts (active GTP-bound form) with RGS14 (via
CC RBD 1 domain) (PubMed:19319189, PubMed:19878719). Interacts with
CC PIK3CG; the interaction is required for membrane recruitment and beta-
CC gamma G protein dimer-dependent activation of the PI3K gamma complex
CC PIK3CG:PIK3R6 (By similarity). Interacts with RAPGEF2 (By similarity).
CC Interacts (in GTP-bound form) with Oog1 (By similarity).
CC {ECO:0000250|UniProtKB:P01112, ECO:0000250|UniProtKB:Q61411,
CC ECO:0000269|PubMed:19319189, ECO:0000269|PubMed:19878719}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19878719}. Cell
CC membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Shuttles between the
CC plasma membrane and the Golgi apparatus (By similarity). The active
CC GTP-bound form is localized most strongly to membranes than the
CC inactive GDP-bound form. {ECO:0000250}.
CC -!- PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of
CC de- and re-palmitoylation regulates rapid exchange between plasma
CC membrane and Golgi. {ECO:0000250|UniProtKB:P01112}.
CC -!- PTM: S-nitrosylated; critical for redox regulation. Important for
CC stimulating guanine nucleotide exchange. No structural perturbation on
CC nitrosylation. {ECO:0000250|UniProtKB:P01112}.
CC -!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-
CC prostaglandin-J2 is autocatalytic and reversible. It may occur as an
CC alternative to other cysteine modifications, such as S-nitrosylation
CC and S-palmitoylation. {ECO:0000250|UniProtKB:P01112}.
CC -!- PTM: Acetylation at Lys-104 prevents interaction with guanine
CC nucleotide exchange factors (GEFs). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at
CC Lys-170 in a non-degradative manner, leading to inhibit Ras signaling
CC by decreasing Ras association with membranes.
CC {ECO:0000250|UniProtKB:P01112}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH86608.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH99130.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M13011; AAA42009.1; -; Genomic_DNA.
DR EMBL; BC086608; AAH86608.1; ALT_INIT; mRNA.
DR EMBL; BC099130; AAH99130.1; ALT_INIT; mRNA.
DR EMBL; M15188; AAA42008.1; -; Genomic_DNA.
DR PIR; A25229; A25229.
DR RefSeq; NP_001091711.1; NM_001098241.1.
DR RefSeq; NP_001123913.1; NM_001130441.1.
DR PDB; 3V4F; X-ray; 1.39 A; A=1-166.
DR PDBsum; 3V4F; -.
DR AlphaFoldDB; P20171; -.
DR SMR; P20171; -.
DR BioGRID; 254357; 5.
DR CORUM; P20171; -.
DR IntAct; P20171; 1.
DR MINT; P20171; -.
DR STRING; 10116.ENSRNOP00000022363; -.
DR iPTMnet; P20171; -.
DR PhosphoSitePlus; P20171; -.
DR SwissPalm; P20171; -.
DR jPOST; P20171; -.
DR PaxDb; P20171; -.
DR PRIDE; P20171; -.
DR ABCD; P20171; 1 sequenced antibody.
DR GeneID; 293621; -.
DR KEGG; rno:293621; -.
DR UCSC; RGD:2827; rat.
DR CTD; 3265; -.
DR RGD; 2827; Hras.
DR VEuPathDB; HostDB:ENSRNOG00000016611; -.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P20171; -.
DR OMA; HYREQIR; -.
DR OrthoDB; 1259506at2759; -.
DR Reactome; R-RNO-1169092; Activation of RAS in B cells.
DR Reactome; R-RNO-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-171007; p38MAPK events.
DR Reactome; R-RNO-179812; GRB2 events in EGFR signaling.
DR Reactome; R-RNO-180336; SHC1 events in EGFR signaling.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-RNO-210993; Tie2 Signaling.
DR Reactome; R-RNO-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-RNO-2424491; DAP12 signaling.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-RNO-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-RNO-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-RNO-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-RNO-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-RNO-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-RNO-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-RNO-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-RNO-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR Reactome; R-RNO-5673000; RAF activation.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-RNO-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-RNO-8851805; MET activates RAS signaling.
DR Reactome; R-RNO-9607240; FLT3 Signaling.
DR Reactome; R-RNO-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-RNO-9648002; RAS processing.
DR PRO; PR:P20171; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016611; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; P20171; RN.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1905360; C:GTPase complex; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0060612; P:adipose tissue development; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IMP:RGD.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:RGD.
DR GO; GO:0090398; P:cellular senescence; IEP:RGD.
DR GO; GO:0042832; P:defense response to protozoan; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:2000630; P:positive regulation of miRNA metabolic process; ISO:RGD.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISO:RGD.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:MGI.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; IMP:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0043405; P:regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0035900; P:response to isolation stress; IEP:RGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0042088; P:T-helper 1 type immune response; ISO:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Golgi apparatus; GTP-binding;
KW Hydrolase; Isopeptide bond; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Palmitate; Prenylation; Proto-oncogene;
KW Reference proteome; S-nitrosylation; Ubl conjugation.
FT CHAIN 1..186
FT /note="GTPase HRas"
FT /id="PRO_0000326479"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT CHAIN 2..186
FT /note="GTPase HRas, N-terminally processed"
FT /id="PRO_0000043000"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043001"
FT REGION 166..185
FT /note="Hypervariable region"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 2
FT /note="N-acetylthreonine; in GTPase HRas, N-terminally
FT processed"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 118
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 186
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:3290900"
FT LIPID 181
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT LIPID 184
FT /note="S-(15-deoxy-Delta12,14-prostaglandin J2-9-
FT yl)cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT LIPID 184
FT /note="S-palmitoyl cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT LIPID 186
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:3290900"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MUTAGEN 26
FT /note="N->G: Interacts and partially stimulates PLCE1; when
FT associated with L-61."
FT /evidence="ECO:0000269|PubMed:11179219"
FT MUTAGEN 35
FT /note="T->S: No interaction and stimulation of PLCE1; when
FT associated with L-61."
FT /evidence="ECO:0000269|PubMed:11179219"
FT MUTAGEN 37
FT /note="E->G: Reduced interaction and stimulation of PLCE1;
FT when associated with L-61."
FT /evidence="ECO:0000269|PubMed:11179219"
FT MUTAGEN 38
FT /note="D->N: Reduced interaction and stimulation of PLCE1;
FT when associated with L-61."
FT /evidence="ECO:0000269|PubMed:11179219"
FT MUTAGEN 40
FT /note="Y->C: No interaction and stimulation of PLCE1; when
FT associated with L-61."
FT /evidence="ECO:0000269|PubMed:11179219"
FT MUTAGEN 61
FT /note="Q->L: Constitutively active. Constitutively
FT interacts and stimulates PLCE1 phospholipase activity.
FT Reduced interaction and stimulation of PLCE1; when
FT associated with G-37 and N-38. No interaction and
FT stimulation of PLCE1; when associated with S-35 and C-40.
FT Interacts and partially stimulates PLCE1; when associated
FT with G-26. Interacts but does not stimulate PLCE1; when
FT associated with S-186."
FT /evidence="ECO:0000269|PubMed:11179219"
FT MUTAGEN 186
FT /note="C->S: Interacts but does not stimulate PLCE1; when
FT associated with L-61."
FT /evidence="ECO:0000269|PubMed:11179219"
FT CONFLICT 179
FT /note="P -> L (in Ref. 1; AAA42009)"
FT /evidence="ECO:0000305"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:3V4F"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:3V4F"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:3V4F"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3V4F"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3V4F"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:3V4F"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:3V4F"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:3V4F"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:3V4F"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3V4F"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:3V4F"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3V4F"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3V4F"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:3V4F"
SQ SEQUENCE 189 AA; 21298 MW; EE6DC2D933E2856A CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL
AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG
CMSCKCVLS
