RL7_ECOLI
ID RL7_ECOLI Reviewed; 121 AA.
AC P0A7K2; P02392; Q2M8S2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
DE AltName: Full=L8;
DE AltName: Full=Large ribosomal subunit protein bL12 {ECO:0000303|PubMed:24524803};
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368};
GN OrderedLocusNames=b3986, JW3949;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=377281; DOI=10.1073/pnas.76.4.1697;
RA Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.;
RT "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the
RT gene for RNA polymerase subunit beta in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gurevich A.I., Avakov A.E.;
RT "Sequence determination in 3'-end proximalely labelled DNA.";
RL Bioorg. Khim. 5:301-304(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-121, ACETYLATION AT SER-2, AND METHYLATION AT LYS-82.
RC STRAIN=MRE-600;
RX PubMed=4573678; DOI=10.1111/j.1432-1033.1973.tb02740.x;
RA Terhorst C., Moeller W., Laursen R., Wittmann-Liebold B.;
RT "The primary structure of an acidic protein from 50-S ribosomes of
RT Escherichia coli which is involved in GTP hydrolysis dependent on
RT elongation factors G and T.";
RL Eur. J. Biochem. 34:138-152(1973).
RN [7]
RP PROTEIN SEQUENCE OF 2-121.
RC STRAIN=MRE-600;
RX PubMed=773698; DOI=10.1016/0014-5793(76)80267-0;
RA Pettersson I., Hardy S.J.S., Liljas A.;
RT "The ribosomal protein L8 is a complex L7/L12 and L10.";
RL FEBS Lett. 64:135-138(1976).
RN [8]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [10]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-121.
RA Gurevich A.I., Avakov A.E., Kolosov M.N.;
RT "The nucleotide sequence at the proximal end of rpoB gene of Escherichia
RT coli.";
RL Bioorg. Khim. 5:1735-1739(1979).
RN [12]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [13]
RP MASS SPECTROMETRY.
RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
RX PubMed=10094780; DOI=10.1006/abio.1998.3077;
RA Arnold R.J., Reilly J.P.;
RT "Observation of Escherichia coli ribosomal proteins and their
RT posttranslational modifications by mass spectrometry.";
RL Anal. Biochem. 269:105-112(1999).
RN [14]
RP FUNCTION, BINDING OF EF-TU AND EF-G, SUBUNIT, AND MUTAGENESIS OF LYS-66;
RP VAL-67; ILE-70; LYS-71; ARG-74 AND LYS-85.
RX PubMed=15989950; DOI=10.1016/j.cell.2005.04.015;
RA Diaconu M., Kothe U., Schlunzen F., Fischer N., Harms J.M.,
RA Tonevitsky A.G., Stark H., Rodnina M.V., Wahl M.C.;
RT "Structural basis for the function of the ribosomal L7/12 stalk in factor
RT binding and GTPase activation.";
RL Cell 121:991-1004(2005).
RN [15]
RP SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY.
RX PubMed=15923259; DOI=10.1073/pnas.0502193102;
RA Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., Nierhaus K.H.,
RA Robinson C.V.;
RT "Heptameric (L12)6/L10 rather than canonical pentameric complexes are found
RT by tandem MS of intact ribosomes from thermophilic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005).
RN [16]
RP FUNCTION IN IF-2 (INFB) AND EF-G (FUSA) ASSOCIATION WITH RIBOSOME.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22102582; DOI=10.1093/nar/gkr1031;
RA Mandava C.S., Peisker K., Ederth J., Kumar R., Ge X., Szaflarski W.,
RA Sanyal S.;
RT "Bacterial ribosome requires multiple L12 dimers for efficient initiation
RT and elongation of protein synthesis involving IF2 and EF-G.";
RL Nucleic Acids Res. 40:2054-2064(2012).
RN [17]
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 [18]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=3309338; DOI=10.1016/0022-2836(87)90183-5;
RA Leijonmarck M., Liljas A.;
RT "Structure of the C-terminal domain of the ribosomal protein L7/L12 from
RT Escherichia coli at 1.7 A.";
RL J. Mol. Biol. 195:555-580(1987).
RN [19]
RP STRUCTURE BY NMR.
RX PubMed=8603708; DOI=10.1016/0014-5793(95)01531-0;
RA Bocharov E.V., Gudkov A.T., Arseniev A.S.;
RT "Topology of the secondary structure elements of ribosomal protein L7/L12
RT from E. coli in solution.";
RL FEBS Lett. 379:291-294(1996).
RN [20]
RP STRUCTURE BY NMR.
RX PubMed=9515737; DOI=10.1016/s0014-5793(98)00121-5;
RA Bocharov E.V., Gudkov A.T., Budovskaya E.V., Arseniev A.S.;
RT "Conformational independence of N- and C-domains in ribosomal protein
RT L7/L12 and in the complex with protein L10.";
RL FEBS Lett. 423:347-350(1998).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 2-31 IN TNAC-STALLED
RP 50S RIBOSOMAL SUBUNIT.
RC STRAIN=K12 / A19 / KC6;
RX PubMed=25310980; DOI=10.1016/j.celrep.2014.09.011;
RA Bischoff L., Berninghausen O., Beckmann R.;
RT "Molecular basis for the ribosome functioning as an L-tryptophan sensor.";
RL Cell Rep. 9:469-475(2014).
CC -!- FUNCTION: The binding site for several of the GTPase factors involved
CC in protein synthesis (IF-2, EF-Tu, EF-G and RF3). Is thus essential for
CC accurate translation. Deletion of 1 of the L12 dimers from the ribosome
CC (by deleting the binding site on L10) leads to decreased IF-2
CC association with the 70S ribosome and decreased stimulation of the
CC GTPase activity of EF-G. {ECO:0000269|PubMed:15989950,
CC ECO:0000269|PubMed:22102582}.
CC -!- SUBUNIT: Homodimer. Part of the 50S ribosomal subunit; present in 4
CC copies per ribosome. L7/L12 forms dimers with an elongated shape. Two
CC dimers associate with a copy of L10 to form part of the ribosomal stalk
CC (called L8). The ribosomal stalk helps the ribosome interact with GTP-
CC bound translation factors. Forms a pentameric L10(L12)2(L12)2 complex,
CC where L10 forms an elongated spine to which 2 L12 dimers bind in a
CC sequential fashion. {ECO:0000269|PubMed:15923259,
CC ECO:0000269|PubMed:15989950}.
CC -!- INTERACTION:
CC P0A7K2; P0ACJ8: crp; NbExp=2; IntAct=EBI-543702, EBI-547513;
CC P0A7K2; P10443: dnaE; NbExp=3; IntAct=EBI-543702, EBI-549111;
CC P0A7K2; P0AB74: kbaY; NbExp=2; IntAct=EBI-543702, EBI-543669;
CC P0A7K2; P30748: moaD; NbExp=2; IntAct=EBI-543702, EBI-554366;
CC P0A7K2; P0A6Z6: nikR; NbExp=3; IntAct=EBI-543702, EBI-562488;
CC P0A7K2; P42641: obgE; NbExp=3; IntAct=EBI-543702, EBI-370839;
CC P0A7K2; P0AFI2: parC; NbExp=3; IntAct=EBI-543702, EBI-878544;
CC P0A7K2; P24188: trhO; NbExp=3; IntAct=EBI-543702, EBI-560455;
CC P0A7K2; P39177: uspG; NbExp=3; IntAct=EBI-543702, EBI-561722;
CC P0A7K2; P75874: yccU; NbExp=2; IntAct=EBI-543702, EBI-544472;
CC -!- PTM: Acetylation of Ser-2 converts L12 to L7.
CC -!- PTM: Lys-82 was found to be 50% monomethylated.
CC {ECO:0000269|PubMed:4573678}.
CC -!- MASS SPECTROMETRY: Mass=12206.7; Method=MALDI; Note=Non-methylated.;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- MASS SPECTROMETRY: Mass=66643; Mass_error=13; Method=Electrospray;
CC Note=Isolated L10(L12)4.; Evidence={ECO:0000269|PubMed:15923259};
CC -!- MASS SPECTROMETRY: Mass=12223; Mass_error=1; Method=Electrospray;
CC Note=L7, acetylated Ser-2.; Evidence={ECO:0000269|PubMed:15923259};
CC -!- MASS SPECTROMETRY: Mass=12164; Mass_error=1; Method=Electrospray;
CC Note=L12, unacetylated.; Evidence={ECO:0000269|PubMed:15923259};
CC -!- MISCELLANEOUS: Ribosomal protein L8 appears to be an aggregate of
CC ribosomal proteins L7/L12 and L10. {ECO:0000269|PubMed:773698}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000255|HAMAP-Rule:MF_00368}.
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DR EMBL; V00339; CAA23624.1; -; Genomic_DNA.
DR EMBL; M38301; AAA24573.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43084.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76960.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77334.1; -; Genomic_DNA.
DR PIR; S12575; R5EC7.
DR RefSeq; NP_418413.1; NC_000913.3.
DR RefSeq; WP_000028878.1; NZ_STEB01000045.1.
DR PDB; 1CTF; X-ray; 1.70 A; A=48-121.
DR PDB; 1RQS; NMR; -; A=48-121.
DR PDB; 1RQT; NMR; -; A/B=2-38.
DR PDB; 1RQU; NMR; -; A/B=2-121.
DR PDB; 1RQV; NMR; -; A/B=2-121.
DR PDB; 2BCW; EM; 11.20 A; B=54-121.
DR PDB; 3J7Z; EM; 3.90 A; 6=1-121.
DR PDB; 4UY8; EM; 3.80 A; 6=2-31.
DR PDB; 4V4V; EM; 15.00 A; B3/B5=3-121.
DR PDB; 4V4W; EM; 15.00 A; B3/B5=3-121.
DR PDB; 4V5M; EM; 7.80 A; BL=1-121.
DR PDB; 4V5N; EM; 7.60 A; BL=1-121.
DR PDB; 4V7B; EM; 6.80 A; B6=1-121.
DR PDB; 4V7D; EM; 7.60 A; AL=2-121.
DR PDB; 4V85; X-ray; 3.20 A; BJ/BK/BL/BM=1-121.
DR PDB; 4V89; X-ray; 3.70 A; BJ/BK/BL/BM=1-121.
DR PDB; 4V9O; X-ray; 2.90 A; A6=1-121.
DR PDB; 5KCS; EM; 3.90 A; 1L=1-121.
DR PDB; 6I0Y; EM; 3.20 A; 6=1-121.
DR PDB; 7N2C; EM; 2.72 A; LG=1-121.
DR PDBsum; 1CTF; -.
DR PDBsum; 1RQS; -.
DR PDBsum; 1RQT; -.
DR PDBsum; 1RQU; -.
DR PDBsum; 1RQV; -.
DR PDBsum; 2BCW; -.
DR PDBsum; 3J7Z; -.
DR PDBsum; 4UY8; -.
DR PDBsum; 4V4V; -.
DR PDBsum; 4V4W; -.
DR PDBsum; 4V5M; -.
DR PDBsum; 4V5N; -.
DR PDBsum; 4V7B; -.
DR PDBsum; 4V7D; -.
DR PDBsum; 4V85; -.
DR PDBsum; 4V89; -.
DR PDBsum; 4V9O; -.
DR PDBsum; 5KCS; -.
DR PDBsum; 6I0Y; -.
DR PDBsum; 7N2C; -.
DR AlphaFoldDB; P0A7K2; -.
DR SMR; P0A7K2; -.
DR BioGRID; 852783; 3.
DR ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR DIP; DIP-36009N; -.
DR IntAct; P0A7K2; 135.
DR STRING; 511145.b3986; -.
DR iPTMnet; P0A7K2; -.
DR MetOSite; P0A7K2; -.
DR SWISS-2DPAGE; P0A7K2; -.
DR jPOST; P0A7K2; -.
DR PaxDb; P0A7K2; -.
DR PRIDE; P0A7K2; -.
DR EnsemblBacteria; AAC76960; AAC76960; b3986.
DR EnsemblBacteria; BAE77334; BAE77334; BAE77334.
DR GeneID; 67415313; -.
DR GeneID; 948489; -.
DR KEGG; ecj:JW3949; -.
DR KEGG; eco:b3986; -.
DR PATRIC; fig|1411691.4.peg.2726; -.
DR EchoBASE; EB0866; -.
DR eggNOG; COG0222; Bacteria.
DR HOGENOM; CLU_086499_3_2_6; -.
DR InParanoid; P0A7K2; -.
DR OMA; LEDKWGV; -.
DR PhylomeDB; P0A7K2; -.
DR BioCyc; EcoCyc:EG10873-MON; -.
DR BioCyc; MetaCyc:EG10873-MON; -.
DR EvolutionaryTrace; P0A7K2; -.
DR PRO; PR:P0A7K2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:EcoliWiki.
DR GO; GO:0015934; C:large ribosomal subunit; IDA:CAFA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0043022; F:ribosome binding; IDA:CAFA.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; IMP:CAFA.
DR CDD; cd00387; Ribosomal_L7_L12; 1.
DR DisProt; DP01650; -.
DR Gene3D; 1.20.5.710; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR InterPro; IPR000206; Ribosomal_L7/12.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR InterPro; IPR013823; Ribosomal_L7/L12_C.
DR InterPro; IPR008932; Ribosomal_L7/L12_oligo.
DR InterPro; IPR036235; Ribosomal_L7/L12_oligo_N_sf.
DR PANTHER; PTHR45987; PTHR45987; 1.
DR Pfam; PF00542; Ribosomal_L12; 1.
DR Pfam; PF16320; Ribosomal_L12_N; 1.
DR SUPFAM; SSF48300; SSF48300; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
DR TIGRFAMs; TIGR00855; L12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Methylation;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4573678,
FT ECO:0000269|PubMed:773698, ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9600841, ECO:0000269|PubMed:9868784"
FT CHAIN 2..121
FT /note="50S ribosomal protein L7/L12"
FT /id="PRO_0000157528"
FT REGION 54..121
FT /note="Required for recruitment of EF-Tu and EF-G, and for
FT EF-Tu and EF-G-promoted GTP hydrolysis"
FT MOD_RES 2
FT /note="N-acetylserine; in L7"
FT /evidence="ECO:0000269|PubMed:4573678"
FT MOD_RES 82
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|PubMed:4573678"
FT MUTAGEN 66
FT /note="K->A: EF-Tu-binding and EF-Tu-promoted GTP
FT hydrolysis reduced."
FT /evidence="ECO:0000269|PubMed:15989950"
FT MUTAGEN 67
FT /note="V->D: EF-Tu-binding and EF-Tu-promoted GTP
FT hydrolysis reduced."
FT /evidence="ECO:0000269|PubMed:15989950"
FT MUTAGEN 70
FT /note="I->A: EF-Tu-binding and EF-Tu-promoted GTP
FT hydrolysis reduced."
FT /evidence="ECO:0000269|PubMed:15989950"
FT MUTAGEN 71
FT /note="K->A: EF-Tu-binding and EF-Tu-promoted GTP
FT hydrolysis reduced."
FT /evidence="ECO:0000269|PubMed:15989950"
FT MUTAGEN 74
FT /note="R->M: EF-Tu-binding and EF-Tu-promoted GTP
FT hydrolysis reduced."
FT /evidence="ECO:0000269|PubMed:15989950"
FT MUTAGEN 85
FT /note="K->A: EF-Tu-binding and EF-Tu-promoted GTP
FT hydrolysis reduced."
FT /evidence="ECO:0000269|PubMed:15989950"
FT CONFLICT 6
FT /note="D -> F (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:6I0Y"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:6I0Y"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:6I0Y"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6I0Y"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:6I0Y"
FT HELIX 33..50
FT /evidence="ECO:0007829|PDB:1RQV"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1CTF"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1CTF"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:1CTF"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:1CTF"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1CTF"
FT HELIX 101..114
FT /evidence="ECO:0007829|PDB:1CTF"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1CTF"
SQ SEQUENCE 121 AA; 12295 MW; 08B051A0CDAA527E CRC64;
MSITKDQIIE AVAAMSVMDV VELISAMEEK FGVSAAAAVA VAAGPVEAAE EKTEFDVILK
AAGANKVAVI KAVRGATGLG LKEAKDLVES APAALKEGVS KDDAEALKKA LEEAGAEVEV
K
