ID RS17A_YEAST Reviewed; 136 AA. AC P02407; D6VZF0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 193. DE RecName: Full=Small ribosomal subunit protein eS17A {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S17-A {ECO:0000303|PubMed:9559554}; DE AltName: Full=RP51A; GN Name=RPS17A {ECO:0000303|PubMed:9559554}; Synonyms=RP51A; GN OrderedLocusNames=YML024W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RY26; RX PubMed=6308621; DOI=10.1073/pnas.80.14.4403; RA Teem J.L., Rosbash M.; RT "Expression of a beta-galactosidase gene containing the ribosomal protein RT 51 intron is sensitive to the rna2 mutation of yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 80:4403-4407(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NOMENCLATURE, AND SUBUNIT. RX PubMed=9559554; RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u; RA Planta R.J., Mager W.H.; RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."; RL Yeast 14:471-477(1998). RN [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP NOMENCLATURE. RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002; RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R., RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A., RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V., RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J., RA Williamson J.R., Wilson D., Yonath A., Yusupov M.; RT "A new system for naming ribosomal proteins."; RL Curr. Opin. Struct. Biol. 24:165-169(2014). RN [8] RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME. RX PubMed=21109664; DOI=10.1126/science.1194294; RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.; RT "Crystal structure of the eukaryotic ribosome."; RL Science 330:1203-1209(2010). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=22096102; DOI=10.1126/science.1212642; RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G., RA Yusupov M.; RT "The structure of the eukaryotic ribosome at 3.0 A resolution."; RL Science 334:1524-1529(2011). CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex CC responsible for the synthesis of proteins in the cell. The small CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) CC molecules. The large subunit (LSU) contains the ribosomal catalytic CC site termed the peptidyl transferase center (PTC), which catalyzes the CC formation of peptide bonds, thereby polymerizing the amino acids CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides CC leave the ribosome through a tunnel in the LSU and interact with CC protein factors that function in enzymatic processing, targeting, and CC the membrane insertion of nascent chains at the exit of the ribosomal CC tunnel. {ECO:0000305|PubMed:22096102}. CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature yeast CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 CC different proteins (encoded by 57 genes). The large 60S subunit CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different CC proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:22096102}. CC -!- MISCELLANEOUS: Present with 30900 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- MISCELLANEOUS: There are 2 genes for eS17 in yeast. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS17 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J01349; AAA88733.1; -; Genomic_DNA. DR EMBL; Z46659; CAA86631.1; -; Genomic_DNA. DR EMBL; BK006946; DAA09874.1; -; Genomic_DNA. DR PIR; A02784; R5BY51. DR RefSeq; NP_013688.1; NM_001182382.1. DR PDB; 3J6X; EM; 6.10 A; 17=1-136. DR PDB; 3J6Y; EM; 6.10 A; 17=1-136. DR PDB; 3J77; EM; 6.20 A; 17=1-136. DR PDB; 3J78; EM; 6.30 A; 17=1-136. DR PDB; 4U3M; X-ray; 3.00 A; C7/c7=1-136. DR PDB; 4U3N; X-ray; 3.20 A; C7/c7=1-136. DR PDB; 4U3U; X-ray; 2.90 A; C7/c7=1-136. DR PDB; 4U4N; X-ray; 3.10 A; C7/c7=1-136. DR PDB; 4U4O; X-ray; 3.60 A; C7/c7=1-136. DR PDB; 4U4Q; X-ray; 3.00 A; C7/c7=1-136. DR PDB; 4U4R; X-ray; 2.80 A; C7/c7=1-136. DR PDB; 4U4U; X-ray; 3.00 A; C7/c7=1-136. DR PDB; 4U4Y; X-ray; 3.20 A; C7/c7=1-136. DR PDB; 4U4Z; X-ray; 3.10 A; C7/c7=1-136. DR PDB; 4U50; X-ray; 3.20 A; C7/c7=1-136. DR PDB; 4U51; X-ray; 3.20 A; C7/c7=1-136. DR PDB; 4U52; X-ray; 3.00 A; C7/c7=1-136. DR PDB; 4U53; X-ray; 3.30 A; C7/c7=1-136. DR PDB; 4U55; X-ray; 3.20 A; C7/c7=1-136. DR PDB; 4U56; X-ray; 3.45 A; C7/c7=1-136. DR PDB; 4U6F; X-ray; 3.10 A; C7/c7=1-136. DR PDB; 4V6I; EM; 8.80 A; AQ=1-136. DR PDB; 4V7R; X-ray; 4.00 A; AK/CK=1-136. DR PDB; 4V88; X-ray; 3.00 A; AR/CR=1-136. DR PDB; 4V8Y; EM; 4.30 A; AR=1-136. DR PDB; 4V8Z; EM; 6.60 A; AR=1-136. DR PDB; 4V92; EM; 3.70 A; R=2-125. DR PDB; 5DAT; X-ray; 3.15 A; C7/c7=1-136. DR PDB; 5DC3; X-ray; 3.25 A; C7/c7=1-136. DR PDB; 5DGE; X-ray; 3.45 A; C7/c7=1-136. DR PDB; 5DGF; X-ray; 3.30 A; C7/c7=1-136. DR PDB; 5DGV; X-ray; 3.10 A; C7/c7=1-136. DR PDB; 5FCI; X-ray; 3.40 A; C7/c7=1-136. DR PDB; 5FCJ; X-ray; 3.10 A; C7/c7=1-136. DR PDB; 5I4L; X-ray; 3.10 A; C7/c7=1-136. DR PDB; 5JUO; EM; 4.00 A; OB=1-136. DR PDB; 5JUP; EM; 3.50 A; OB=1-136. DR PDB; 5JUS; EM; 4.20 A; OB=1-136. DR PDB; 5JUT; EM; 4.00 A; OB=1-136. DR PDB; 5JUU; EM; 4.00 A; OB=1-136. DR PDB; 5LYB; X-ray; 3.25 A; C7/c7=2-126. DR PDB; 5MEI; X-ray; 3.50 A; c7=2-122. DR PDB; 5NDG; X-ray; 3.70 A; C7/c7=1-136. DR PDB; 5NDV; X-ray; 3.30 A; C7/c7=1-136. DR PDB; 5NDW; X-ray; 3.70 A; C7/c7=1-136. DR PDB; 5OBM; X-ray; 3.40 A; C7/c7=1-136. DR PDB; 5ON6; X-ray; 3.10 A; S/c7=2-126. DR PDB; 5TBW; X-ray; 3.00 A; S=2-126, c7=2-122. DR PDB; 6EML; EM; 3.60 A; C=1-136. DR PDB; 6FAI; EM; 3.40 A; R=1-136. DR PDB; 6HHQ; X-ray; 3.10 A; S/c7=1-136. DR PDB; 6I7O; EM; 5.30 A; G/Gb=2-126. DR PDB; 6Q8Y; EM; 3.10 A; G=2-126. DR PDB; 6RBD; EM; 3.47 A; R=1-136. DR PDB; 6RBE; EM; 3.80 A; R=1-136. DR PDB; 6S47; EM; 3.28 A; BS=2-136. DR PDB; 6T4Q; EM; 2.60 A; SR=2-126. DR PDB; 6WDR; EM; 3.70 A; R=2-126. DR PDB; 6Y7C; EM; 3.80 A; R=1-136. DR PDB; 6Z6J; EM; 3.40 A; SR=1-136. DR PDB; 6Z6K; EM; 3.40 A; SR=1-136. DR PDB; 6ZCE; EM; 5.30 A; S=1-136. DR PDB; 6ZU9; EM; 6.20 A; I=1-136. DR PDB; 6ZVI; EM; 3.00 A; z=2-126. DR PDB; 7MPI; EM; 3.05 A; BR=2-126. DR PDB; 7MPJ; EM; 2.70 A; BR=2-126. DR PDB; 7N8B; EM; 3.05 A; BR=2-126. DR PDB; 7ZRS; EM; 4.80 A; AR=1-136. DR PDB; 7ZUW; EM; 4.30 A; AR=1-136. DR PDB; 7ZUX; EM; 2.50 A; DR=1-136. DR PDB; 7ZW0; EM; 2.40 A; sG=1-136. DR PDB; 8BQD; EM; 3.90 A; G=2-126. DR PDB; 8BQX; EM; 3.80 A; G=2-126. DR PDB; 8C01; EM; 2.70 A; C=1-136. DR PDB; 8CAH; EM; 3.00 A; H=1-136. DR PDB; 8CAS; EM; 3.30 A; I=1-136. DR PDB; 8CBJ; EM; 3.80 A; R=1-136. DR PDB; 8CCS; EM; 1.97 A; t=1-136. DR PDB; 8CDL; EM; 2.72 A; t=1-136. DR PDB; 8CDR; EM; 2.04 A; t=1-136. DR PDB; 8CEH; EM; 2.05 A; t=1-136. DR PDB; 8CF5; EM; 2.71 A; t=1-136. DR PDB; 8CG8; EM; 2.57 A; t=1-136. DR PDB; 8CGN; EM; 2.28 A; t=1-136. DR PDB; 8CIV; EM; 2.47 A; t=1-136. DR PDB; 8CKU; EM; 3.11 A; t=1-136. DR PDB; 8CMJ; EM; 3.79 A; t=1-136. DR PDB; 8EUB; EM; 2.52 A; BR=1-136. DR PDB; 8EVP; EM; 2.38 A; BR=1-136. DR PDB; 8EVQ; EM; 2.72 A; BR=1-136. DR PDB; 8EVR; EM; 2.87 A; BR=1-136. DR PDB; 8EVS; EM; 2.62 A; BR=1-136. DR PDB; 8EVT; EM; 2.20 A; BR=1-136. DR PDB; 8EWB; EM; 2.87 A; BR=1-136. DR PDB; 8EWC; EM; 2.45 A; BR=1-136. DR PDBsum; 3J6X; -. DR PDBsum; 3J6Y; -. DR PDBsum; 3J77; -. DR PDBsum; 3J78; -. DR PDBsum; 4U3M; -. DR PDBsum; 4U3N; -. DR PDBsum; 4U3U; -. DR PDBsum; 4U4N; -. DR PDBsum; 4U4O; -. DR PDBsum; 4U4Q; -. DR PDBsum; 4U4R; -. DR PDBsum; 4U4U; -. DR PDBsum; 4U4Y; -. DR PDBsum; 4U4Z; -. DR PDBsum; 4U50; -. DR PDBsum; 4U51; -. DR PDBsum; 4U52; -. DR PDBsum; 4U53; -. DR PDBsum; 4U55; -. DR PDBsum; 4U56; -. DR PDBsum; 4U6F; -. DR PDBsum; 4V6I; -. DR PDBsum; 4V7R; -. DR PDBsum; 4V88; -. DR PDBsum; 4V8Y; -. DR PDBsum; 4V8Z; -. DR PDBsum; 4V92; -. DR PDBsum; 5DAT; -. DR PDBsum; 5DC3; -. DR PDBsum; 5DGE; -. DR PDBsum; 5DGF; -. DR PDBsum; 5DGV; -. DR PDBsum; 5FCI; -. DR PDBsum; 5FCJ; -. DR PDBsum; 5I4L; -. DR PDBsum; 5JUO; -. DR PDBsum; 5JUP; -. DR PDBsum; 5JUS; -. DR PDBsum; 5JUT; -. DR PDBsum; 5JUU; -. DR PDBsum; 5LYB; -. DR PDBsum; 5MEI; -. DR PDBsum; 5NDG; -. DR PDBsum; 5NDV; -. DR PDBsum; 5NDW; -. DR PDBsum; 5OBM; -. DR PDBsum; 5ON6; -. DR PDBsum; 5TBW; -. DR PDBsum; 6EML; -. DR PDBsum; 6FAI; -. DR PDBsum; 6HHQ; -. DR PDBsum; 6I7O; -. DR PDBsum; 6Q8Y; -. DR PDBsum; 6RBD; -. DR PDBsum; 6RBE; -. DR PDBsum; 6S47; -. DR PDBsum; 6T4Q; -. DR PDBsum; 6WDR; -. DR PDBsum; 6Y7C; -. DR PDBsum; 6Z6J; -. DR PDBsum; 6Z6K; -. DR PDBsum; 6ZCE; -. DR PDBsum; 6ZU9; -. DR PDBsum; 6ZVI; -. DR PDBsum; 7MPI; -. DR PDBsum; 7MPJ; -. DR PDBsum; 7N8B; -. DR PDBsum; 7ZRS; -. DR PDBsum; 7ZUW; -. DR PDBsum; 7ZUX; -. DR PDBsum; 7ZW0; -. DR PDBsum; 8BQD; -. DR PDBsum; 8BQX; -. DR PDBsum; 8C01; -. DR PDBsum; 8CAH; -. DR PDBsum; 8CAS; -. DR PDBsum; 8CBJ; -. DR PDBsum; 8CCS; -. DR PDBsum; 8CDL; -. DR PDBsum; 8CDR; -. DR PDBsum; 8CEH; -. DR PDBsum; 8CF5; -. DR PDBsum; 8CG8; -. DR PDBsum; 8CGN; -. DR PDBsum; 8CIV; -. DR PDBsum; 8CKU; -. DR PDBsum; 8CMJ; -. DR PDBsum; 8EUB; -. DR PDBsum; 8EVP; -. DR PDBsum; 8EVQ; -. DR PDBsum; 8EVR; -. DR PDBsum; 8EVS; -. DR PDBsum; 8EVT; -. DR PDBsum; 8EWB; -. DR PDBsum; 8EWC; -. DR AlphaFoldDB; P02407; -. DR EMDB; EMD-10098; -. DR EMDB; EMD-10377; -. DR EMDB; EMD-10713; -. DR EMDB; EMD-11096; -. DR EMDB; EMD-11097; -. DR EMDB; EMD-11160; -. DR EMDB; EMD-11439; -. DR EMDB; EMD-11457; -. DR EMDB; EMD-14990; -. DR EMDB; EMD-16563; -. DR EMDB; EMD-16591; -. DR EMDB; EMD-16594; -. DR EMDB; EMD-16609; -. DR EMDB; EMD-16616; -. DR EMDB; EMD-16634; -. DR EMDB; EMD-16648; -. DR EMDB; EMD-16684; -. DR EMDB; EMD-16702; -. DR EMDB; EMD-16729; -. DR EMDB; EMD-21644; -. DR EMDB; EMD-23934; -. DR EMDB; EMD-23935; -. DR EMDB; EMD-24235; -. DR EMDB; EMD-28610; -. DR EMDB; EMD-28632; -. DR EMDB; EMD-28633; -. DR EMDB; EMD-28634; -. DR EMDB; EMD-28635; -. DR EMDB; EMD-28636; -. DR EMDB; EMD-28642; -. DR EMDB; EMD-28643; -. DR EMDB; EMD-4214; -. DR EMDB; EMD-4427; -. DR EMDB; EMD-4474; -. DR EMDB; EMD-4792; -. DR EMDB; EMD-4793; -. DR SMR; P02407; -. DR BioGRID; 35145; 636. DR IntAct; P02407; 65. DR MINT; P02407; -. DR STRING; 4932.YML024W; -. DR iPTMnet; P02407; -. DR MaxQB; P02407; -. DR PaxDb; 4932-YML024W; -. DR PeptideAtlas; P02407; -. DR EnsemblFungi; YML024W_mRNA; YML024W; YML024W. DR GeneID; 854984; -. DR KEGG; sce:YML024W; -. DR AGR; SGD:S000004486; -. DR SGD; S000004486; RPS17A. DR VEuPathDB; FungiDB:YML024W; -. DR eggNOG; KOG0187; Eukaryota. DR GeneTree; ENSGT00390000006548; -. DR HOGENOM; CLU_112958_0_1_1; -. DR InParanoid; P02407; -. DR OMA; HYNKGPR; -. DR OrthoDB; 5480552at2759; -. DR BioCyc; YEAST:G3O-32626-MONOMER; -. DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane. DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR Reactome; R-SCE-72649; Translation initiation complex formation. DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits. DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex. DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition. DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit. DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR BioGRID-ORCS; 854984; 0 hits in 10 CRISPR screens. DR PRO; PR:P02407; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P02407; Protein. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; NAS:SGD. DR GO; GO:0003735; F:structural constituent of ribosome; NAS:SGD. DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD. DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:SGD. DR Gene3D; 1.10.60.20; Ribosomal protein S17e-like; 1. DR HAMAP; MF_00511; Ribosomal_eS17; 1. DR InterPro; IPR001210; Ribosomal_eS17. DR InterPro; IPR018273; Ribosomal_eS17_CS. DR InterPro; IPR036401; Ribosomal_eS17_sf. DR PANTHER; PTHR10732; 40S RIBOSOMAL PROTEIN S17; 1. DR PANTHER; PTHR10732:SF0; 40S RIBOSOMAL PROTEIN S17; 1. DR Pfam; PF00833; Ribosomal_S17e; 1. DR SUPFAM; SSF116820; Rps17e-like; 1. DR PROSITE; PS00712; RIBOSOMAL_S17E; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1..136 FT /note="Small ribosomal subunit protein eS17A" FT /id="PRO_0000141546" FT HELIX 7..17 FT /evidence="ECO:0007829|PDB:6ZVI" FT TURN 18..20 FT /evidence="ECO:0007829|PDB:6ZVI" FT HELIX 21..23 FT /evidence="ECO:0007829|PDB:6ZVI" FT TURN 29..31 FT /evidence="ECO:0007829|PDB:6ZVI" FT HELIX 32..38 FT /evidence="ECO:0007829|PDB:6ZVI" FT HELIX 44..59 FT /evidence="ECO:0007829|PDB:6ZVI" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:6ZVI" FT HELIX 72..81 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:6RBD" FT HELIX 93..96 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 104..113 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 119..122 FT /evidence="ECO:0007829|PDB:8C01" SQ SEQUENCE 136 AA; 15788 MW; 956E5382870EA289 CRC64; MGRVRTKTVK RASKALIERY YPKLTLDFQT NKRLCDEIAT IQSKRLRNKI AGYTTHLMKR IQKGPVRGIS FKLQEEERER KDQYVPEVSA LDLSRSNGVL NVDNQTSDLV KSLGLKLPLS VINVSAQRDR RYRKRV //