GRB2_RAT
ID GRB2_RAT Reviewed; 217 AA.
AC P62994; P29354; Q14450; Q5BKA7; Q63057; Q63059;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Growth factor receptor-bound protein 2;
DE AltName: Full=Adapter protein GRB2;
DE AltName: Full=Protein Ash;
DE AltName: Full=SH2/SH3 adapter GRB2;
GN Name=Grb2; Synonyms=Ash;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Fischer 344; TISSUE=Brain;
RX PubMed=1384039; DOI=10.1073/pnas.89.19.9015;
RA Matuoka K., Yamakawa A., Shibata M., Takenawa T.;
RT "Cloning of ASH, a ubiquitous protein composed of one Src homology region
RT (SH) 2 and two SH3 domains, from human and rat cDNA libraries.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9015-9019(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND FUNCTION.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7775428; DOI=10.1074/jbc.270.23.13733;
RA Watanabe K., Fukuchi T., Hosoya H., Shirasawa T., Matsuoka K., Miki H.,
RA Takenawa T.;
RT "Splicing isoforms of rat Ash/Grb2. Isolation and characterization of the
RT cDNA and genomic DNA clones and implications for the physiological roles of
RT the isoforms.";
RL J. Biol. Chem. 270:13733-13739(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [4]
RP PROTEIN SEQUENCE OF 11-21; 77-86; 101-109; 125-136; 143-149 AND 208-215,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH CSF1R.
RX PubMed=8262059;
RA van der Geer P., Hunter T.;
RT "Mutation of Tyr697, a GRB2-binding site, and Tyr721, a PI 3-kinase binding
RT site, abrogates signal transduction by the murine CSF-1 receptor expressed
RT in Rat-2 fibroblasts.";
RL EMBO J. 12:5161-5172(1993).
RN [6]
RP INTERACTION WITH IRS1.
RX PubMed=8388384; DOI=10.1016/s0021-9258(18)82106-8;
RA Tobe K., Matuoka K., Tamemoto H., Ueki K., Kaburagi Y., Asai S.,
RA Noguchi T., Matsuda M., Tanaka S., Hattori S., Fukui Y., Akanuma Y.,
RA Yazaki Y., Takenawa T., Kadowaki T.;
RT "Insulin stimulates association of insulin receptor substrate-1 with the
RT protein abundant Src homology/growth factor receptor-bound protein 2.";
RL J. Biol. Chem. 268:11167-11171(1993).
CC -!- FUNCTION: Adapter protein that provides a critical link between cell
CC surface growth factor receptors and the Ras signaling pathway.
CC {ECO:0000269|PubMed:7775428}.
CC -!- SUBUNIT: Associates (via SH2 domain) with activated EGF and PDGF
CC receptors (tyrosine phosphorylated). Interacts with PDGFRA (tyrosine
CC phosphorylated); the interaction may be indirect. Interacts with IRS4
CC (when Tyr-phosphorylated). Also associates to other cellular Tyr-
CC phosphorylated proteins such as SIT1, SHC and LNK; probably via the
CC concerted action of both its SH2 and SH3 domains. It also seems to
CC interact with RAS in the signaling pathway leading to DNA synthesis.
CC Interacts with SOS1. Forms a complex with MUC1 and SOS1, through
CC interaction of the SH3 domains with SOS1 and the SH2 domain with
CC phosphorylated MUC1. Interacts with phosphorylated MET. Interacts with
CC phosphorylated TOM1L1. Interacts with the phosphorylated C-terminus of
CC SH2B2. Interacts with phosphorylated SIT1, LAX1, LAT, LAT2 and LIME1
CC upon TCR and/or BCR activation. Interacts with NISCH, PTPNS1 and REPS2.
CC Interacts with syntrophin SNTA1. Interacts (via SH3 domains) with
CC REPS1. Interacts (via SH3 domains) with PIK3C2B. Interacts with CBL and
CC CBLB. Interacts with AJUBA and CLNK. Interacts (via SH2 domain) with
CC TEK/TIE2 (tyrosine phosphorylated). Interacts with SHB, INPP5D/SHIP1,
CC SKAP1 and SKAP2. Interacts with PTPN11. Interacts with PRNP. Interacts
CC with RALGPS1. Interacts also with HCST. Interacts with KDR. Interacts
CC with FLT1 (tyrosine-phosphorylated). Interacts with GAPT and PTPRE.
CC Interacts (via SH2 domain) with KIF26A. Interacts (via SH3 2) with
CC GAB2. Interacts with ADAM15. Interacts with THEMIS2. Interacts (via SH2
CC domain) with AXL (phosphorylated). Interacts (via SH2 domain) with KIT
CC (phosphorylated). Interacts with PTPRJ and BCR. Interacts with PTPN23.
CC Interacts with FLT4 (tyrosine phosphorylated). Interacts with EPHB1 and
CC SHC1; activates the MAPK/ERK cascade to regulate cell migration. Part
CC of a complex including TNK2, GRB2 and one receptor tyrosine kinase
CC (RTK) such as AXL and PDGFRL, in which GRB2 promotes RTK recruitment by
CC TNK2. Interacts with ERBB4. Interacts with NTRK1 (phosphorylated upon
CC ligand-binding). Interacts with PTK2/FAK1 (tyrosine phosphorylated).
CC Interacts with PTK2B/PYK2 (tyrosine phosphorylated). Interacts (via
CC SH2-domain) with SCIMP; this interaction is dependent on
CC phosphorylation on SCIMP 'Tyr-58' (By similarity). Interacts (via SH3
CC domains) with GAREM1 (via proline-rich domain and tyrosine
CC phosphorylated); the interaction occurs upon EGF stimulation. Interacts
CC with DAB2. Interacts with TESPA1. Interacts with THEMIS. Interacts with
CC PLCG1, LAT and THEMIS upon TCR activation in thymocytes; the
CC association is weaker in the absence of TESPA1. Interacts with CD28.
CC Interacts with RAB13; may recruit RAB13 to the leading edge of
CC migrating endothelial cells where it can activate RHOA. Interacts with
CC ASAP3 (phosphorylated form) (By similarity). Interacts (via SH2 domain)
CC with CSF1R and IRS1 (tyrosine phosphorylated) (PubMed:8262059,
CC PubMed:8388384). Interacts (via SH2 domain) with PTPRH (phosphorylated
CC form) (By similarity). Interacts with PTPRO (phosphorylated form) (By
CC similarity). Interacts with PTPRB (phosphorylated form) (By
CC similarity). Interacts (via SH3 domain 2) with PRR14 (via proline-rich
CC region) (By similarity). Interacts with DENND2B (By similarity).
CC Interacts with SPRY2 (By similarity). Interacts with LRRC8A (By
CC similarity). {ECO:0000250|UniProtKB:P62993,
CC ECO:0000250|UniProtKB:Q60631, ECO:0000269|PubMed:8262059,
CC ECO:0000269|PubMed:8388384}.
CC -!- INTERACTION:
CC P62994; P21575: Dnm1; NbExp=3; IntAct=EBI-401775, EBI-80070;
CC P62994; P35739: Ntrk1; NbExp=6; IntAct=EBI-401775, EBI-976667;
CC P62994; P18545: PDE6G; Xeno; NbExp=2; IntAct=EBI-401775, EBI-2622029;
CC P62994; P18031: PTPN1; Xeno; NbExp=3; IntAct=EBI-401775, EBI-968788;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62993}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62993}. Endosome
CC {ECO:0000250|UniProtKB:P62993}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q60631}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Ash-L;
CC IsoId=P62994-1, P29354-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=Ash-M;
CC IsoId=P62994-2, P29354-3;
CC Sequence=VSP_001840;
CC Name=3; Synonyms=Ash-S;
CC IsoId=P62994-3, P29354-4;
CC Sequence=VSP_001838;
CC -!- TISSUE SPECIFICITY: Wide tissue distribution.
CC {ECO:0000269|PubMed:1384039}.
CC -!- DOMAIN: The SH3 domains mediate interaction with RALGPS1 and SHB.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GRB2/sem-5/DRK family. {ECO:0000305}.
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DR EMBL; X62853; CAA44665.1; -; mRNA.
DR EMBL; D49846; BAA08645.1; -; mRNA.
DR EMBL; D49847; BAA08646.1; -; mRNA.
DR EMBL; BC091144; AAH91144.1; -; mRNA.
DR PIR; S26050; S26050.
DR RefSeq; NP_110473.2; NM_030846.2. [P62994-1]
DR AlphaFoldDB; P62994; -.
DR BMRB; P62994; -.
DR SMR; P62994; -.
DR BioGRID; 249501; 13.
DR CORUM; P62994; -.
DR IntAct; P62994; 27.
DR MINT; P62994; -.
DR STRING; 10116.ENSRNOP00000005347; -.
DR iPTMnet; P62994; -.
DR PhosphoSitePlus; P62994; -.
DR SwissPalm; P62994; -.
DR jPOST; P62994; -.
DR PaxDb; P62994; -.
DR PRIDE; P62994; -.
DR Ensembl; ENSRNOT00000095127; ENSRNOP00000080275; ENSRNOG00000003990. [P62994-2]
DR GeneID; 81504; -.
DR KEGG; rno:81504; -.
DR CTD; 2885; -.
DR RGD; 619758; Grb2.
DR VEuPathDB; HostDB:ENSRNOG00000003990; -.
DR eggNOG; KOG3601; Eukaryota.
DR GeneTree; ENSGT00940000155738; -.
DR HOGENOM; CLU_073617_1_0_1; -.
DR InParanoid; P62994; -.
DR OMA; MVPEEML; -.
DR OrthoDB; 1091250at2759; -.
DR PhylomeDB; P62994; -.
DR TreeFam; TF354288; -.
DR Reactome; R-RNO-109704; PI3K Cascade.
DR Reactome; R-RNO-112412; SOS-mediated signalling.
DR Reactome; R-RNO-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-1295596; Spry regulation of FGF signaling.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-1433559; Regulation of KIT signaling.
DR Reactome; R-RNO-167044; Signalling to RAS.
DR Reactome; R-RNO-179812; GRB2 events in EGFR signaling.
DR Reactome; R-RNO-180292; GAB1 signalosome.
DR Reactome; R-RNO-180336; SHC1 events in EGFR signaling.
DR Reactome; R-RNO-182971; EGFR downregulation.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-RNO-1963642; PI3K events in ERBB2 signaling.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
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-2428933; SHC-related events triggered by IGF1R.
DR Reactome; R-RNO-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-RNO-388841; Costimulation by the CD28 family.
DR Reactome; R-RNO-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-RNO-391160; Signal regulatory protein family interactions.
DR Reactome; R-RNO-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-RNO-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-RNO-5654695; PI-3K cascade:FGFR2.
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-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-RNO-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-RNO-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-RNO-5654720; PI-3K cascade:FGFR4.
DR Reactome; R-RNO-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-RNO-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-RNO-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-RNO-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6807004; Negative regulation of MET activity.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-74749; Signal attenuation.
DR Reactome; R-RNO-74751; Insulin receptor signalling cascade.
DR Reactome; R-RNO-8851805; MET activates RAS signaling.
DR Reactome; R-RNO-8851907; MET activates PI3K/AKT signaling.
DR Reactome; R-RNO-8853659; RET signaling.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-8865999; MET activates PTPN11.
DR Reactome; R-RNO-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-RNO-8875656; MET receptor recycling.
DR Reactome; R-RNO-8983432; Interleukin-15 signaling.
DR Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR Reactome; R-RNO-9027284; Erythropoietin activates RAS.
DR Reactome; R-RNO-9028731; Activated NTRK2 signals through FRS2 and FRS3.
DR Reactome; R-RNO-912526; Interleukin receptor SHC signaling.
DR Reactome; R-RNO-912631; Regulation of signaling by CBL.
DR Reactome; R-RNO-9607240; FLT3 Signaling.
DR Reactome; R-RNO-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-RNO-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR PRO; PR:P62994; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003990; Expressed in spleen and 20 other tissues.
DR Genevisible; P62994; RN.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0008180; C:COP9 signalosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0070436; C:Grb2-EGFR complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0012506; C:vesicle membrane; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:RGD.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0043560; F:insulin receptor substrate binding; IPI:RGD.
DR GO; GO:0005168; F:neurotrophin TRKA receptor binding; ISO:RGD.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:RGD.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; ISO:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0007568; P:aging; IPI:RGD.
DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; ISO:RGD.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:RGD.
DR GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; ISO:RGD.
DR CDD; cd11949; SH3_GRB2_C; 1.
DR CDD; cd11946; SH3_GRB2_N; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035643; GRB2_C_SH3.
DR InterPro; IPR035641; GRB2_N_SH3.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Endosome; Golgi apparatus; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; SH2 domain; SH3 domain.
FT CHAIN 1..217
FT /note="Growth factor receptor-bound protein 2"
FT /id="PRO_0000088201"
FT DOMAIN 1..58
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 60..152
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 156..215
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P62993"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62993"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62993"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62993"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62993"
FT VAR_SEQ 60..217
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7775428"
FT /id="VSP_001838"
FT VAR_SEQ 157..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7775428"
FT /id="VSP_001840"
SQ SEQUENCE 217 AA; 25206 MW; 83A4B0BA1B248DC4 CRC64;
MEAIAKYDFK ATADDELSFK RGDILKVLNE ECDQNWYKAE LNGKDGFIPK NYIEMKPHPW
FFGKIPRAKA EEMLSKQRHD GAFLIRESES APGDFSLSVK FGNDVQHFKV LRDGAGKYFL
WVVKFNSLNE LVDYHRSTSV SRNQQIFLRD IEQVPQQPTY VQALFDFDPQ EDGELGFRRG
DFIHVMDNSD PNWWKGACHG QTGMFPRNYV TPVNRNV
