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   27-MAR-2024, entry version 195.
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   ChEMBL; CHEMBL5169120; -.
DR   iPTMnet; P20171; -.
DR   PhosphoSitePlus; P20171; -.
DR   SwissPalm; P20171; -.
DR   jPOST; P20171; -.
DR   PaxDb; 10116-ENSRNOP00000022363; -.
DR   ABCD; P20171; 1 sequenced antibody.
DR   GeneID; 293621; -.
DR   KEGG; rno:293621; -.
DR   UCSC; RGD:2827; rat.
DR   AGR; RGD:2827; -.
DR   RGD; 2827; Hras.
DR   VEuPathDB; HostDB:ENSRNOG00000016611; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; P20171; -.
DR   OrthoDB; 8685at2759; -.
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 cell types or tissues.
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: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:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; ISO:RGD.
DR   GO; GO:0060612; P:adipose tissue development; ISO: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:0048144; P:fibroblast proliferation; ISO:RGD.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; 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:0042552; P:myelination; ISO: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:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR   GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR   GO; GO:0090402; P:oncogene-induced cell senescence; 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:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; 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: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:0032729; P:positive regulation of type II interferon production; 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:0032956; P:regulation of actin cytoskeleton organization; ISO: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: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:0014044; P:Schwann cell development; ISO: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   CDD; cd04138; H_N_K_Ras_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR24070:SF385; GTPASE HRAS; 1.
DR   PANTHER; PTHR24070; RAS, DI-RAS, AND RHEB FAMILY MEMBERS OF SMALL GTPASE SUPERFAMILY; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51421; RAS; 1.
DR   Genevisible; P20171; RN.
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
//