RS12_YEAST
ID RS12_YEAST Reviewed; 143 AA.
AC P48589; D6W362; Q02545;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=40S ribosomal protein S12 {ECO:0000303|PubMed:9559554};
DE AltName: Full=Small ribosomal subunit protein eS12 {ECO:0000303|PubMed:24524803};
GN Name=RPS12 {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YOR369C;
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 / MRNA].
RX PubMed=8649984; DOI=10.1093/nar/24.9.1669;
RA Siede W., Nusspaumer G., Portillo V., Rodriguez R., Friedberg E.C.;
RT "Cloning and characterization of RAD17, a gene controlling cell cycle
RT responses to DNA damage in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 24:1669-1675(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 44774 / DBY747;
RA Teply R.;
RT "Yeast homologue of ribosomal protein S12.";
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 29-126.
RC STRAIN=ATCC 204660 / DBY746;
RA Moore J., Jacobs H.T., Kaiser K.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-85; LYS-95 AND LYS-114, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [10]
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 [11]
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:22096102}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS12 family.
CC {ECO:0000305}.
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DR EMBL; U37460; AAA80546.1; -; Genomic_DNA.
DR EMBL; U01049; AAA69926.1; -; Genomic_DNA.
DR EMBL; Z75277; CAA99700.1; -; Genomic_DNA.
DR EMBL; U24143; AAA65439.1; ALT_SEQ; mRNA.
DR EMBL; BK006948; DAA11128.1; -; Genomic_DNA.
DR PIR; S62102; S62102.
DR RefSeq; NP_015014.3; NM_001183789.3.
DR PDB; 3J6X; EM; 6.10 A; 12=1-143.
DR PDB; 3J6Y; EM; 6.10 A; 12=1-143.
DR PDB; 3J77; EM; 6.20 A; 12=1-143.
DR PDB; 3J78; EM; 6.30 A; 12=1-143.
DR PDB; 4U3M; X-ray; 3.00 A; C2/c2=2-143.
DR PDB; 4U3N; X-ray; 3.20 A; C2/c2=2-143.
DR PDB; 4U3U; X-ray; 2.90 A; C2/c2=2-143.
DR PDB; 4U4N; X-ray; 3.10 A; C2/c2=2-143.
DR PDB; 4U4O; X-ray; 3.60 A; C2/c2=2-143.
DR PDB; 4U4Q; X-ray; 3.00 A; C2/c2=2-143.
DR PDB; 4U4R; X-ray; 2.80 A; C2/c2=2-143.
DR PDB; 4U4U; X-ray; 3.00 A; C2/c2=2-143.
DR PDB; 4U4Y; X-ray; 3.20 A; C2/c2=2-143.
DR PDB; 4U4Z; X-ray; 3.10 A; C2/c2=2-143.
DR PDB; 4U50; X-ray; 3.20 A; C2/c2=2-143.
DR PDB; 4U51; X-ray; 3.20 A; C2/c2=2-143.
DR PDB; 4U52; X-ray; 3.00 A; C2/c2=2-143.
DR PDB; 4U53; X-ray; 3.30 A; C2/c2=2-143.
DR PDB; 4U55; X-ray; 3.20 A; C2/c2=2-143.
DR PDB; 4U56; X-ray; 3.45 A; C2/c2=2-143.
DR PDB; 4U6F; X-ray; 3.10 A; C2/c2=2-143.
DR PDB; 4V88; X-ray; 3.00 A; AM/CM=1-143.
DR PDB; 4V8Y; EM; 4.30 A; AM=1-143.
DR PDB; 4V8Z; EM; 6.60 A; AM=1-143.
DR PDB; 4V92; EM; 3.70 A; M=24-143.
DR PDB; 5DAT; X-ray; 3.15 A; C2/c2=20-142.
DR PDB; 5DC3; X-ray; 3.25 A; C2/c2=2-143.
DR PDB; 5DGE; X-ray; 3.45 A; C2/c2=2-143.
DR PDB; 5DGV; X-ray; 3.10 A; C2/c2=2-143.
DR PDB; 5FCI; X-ray; 3.40 A; C2/c2=2-143.
DR PDB; 5FCJ; X-ray; 3.10 A; C2/c2=2-143.
DR PDB; 5I4L; X-ray; 3.10 A; C2/c2=20-143.
DR PDB; 5JUO; EM; 4.00 A; JB=1-143.
DR PDB; 5JUP; EM; 3.50 A; JB=1-143.
DR PDB; 5JUS; EM; 4.20 A; JB=1-143.
DR PDB; 5JUT; EM; 4.00 A; JB=1-143.
DR PDB; 5JUU; EM; 4.00 A; JB=1-143.
DR PDB; 5LYB; X-ray; 3.25 A; C2=20-143, c2=25-143.
DR PDB; 5M1J; EM; 3.30 A; M2=20-143.
DR PDB; 5MC6; EM; 3.80 A; D=1-143.
DR PDB; 5MEI; X-ray; 3.50 A; N/c2=20-143.
DR PDB; 5NDG; X-ray; 3.70 A; C2/c2=1-143.
DR PDB; 5NDV; X-ray; 3.30 A; C2/c2=1-143.
DR PDB; 5NDW; X-ray; 3.70 A; C2/c2=1-143.
DR PDB; 5OBM; X-ray; 3.40 A; C2/c2=1-143.
DR PDB; 5ON6; X-ray; 3.10 A; N/c2=20-143.
DR PDB; 5TBW; X-ray; 3.00 A; N/c2=1-143.
DR PDB; 5TGA; X-ray; 3.30 A; C2/c2=20-143.
DR PDB; 5TGM; X-ray; 3.50 A; C2/c2=25-143.
DR PDB; 5WYJ; EM; 8.70 A; SN=1-143.
DR PDB; 6EML; EM; 3.60 A; D=1-143.
DR PDB; 6FAI; EM; 3.40 A; M=1-143.
DR PDB; 6GQ1; EM; 4.40 A; AC=20-143.
DR PDB; 6GQB; EM; 3.90 A; AC=20-143.
DR PDB; 6GQV; EM; 4.00 A; AC=20-143.
DR PDB; 6HHQ; X-ray; 3.10 A; N/c2=1-143.
DR PDB; 6I7O; EM; 5.30 A; D/Db=20-143.
DR PDB; 6KE6; EM; 3.40 A; SN=1-143.
DR PDB; 6LQP; EM; 3.20 A; SN=1-143.
DR PDB; 6LQU; EM; 3.70 A; SN=1-143.
DR PDB; 6Q8Y; EM; 3.10 A; D=23-143.
DR PDB; 6RBD; EM; 3.47 A; M=1-143.
DR PDB; 6RBE; EM; 3.80 A; M=1-143.
DR PDB; 6S47; EM; 3.28 A; BN=2-143.
DR PDB; 6SNT; EM; 2.80 A; M=1-143.
DR PDB; 6SV4; EM; 3.30 A; D/Db/Dc=1-143.
DR PDB; 6T4Q; EM; 2.60 A; SM=23-143.
DR PDB; 6T7I; EM; 3.20 A; SM=1-143.
DR PDB; 6T7T; EM; 3.10 A; SM=1-143.
DR PDB; 6T83; EM; 4.00 A; Mb/n=1-143.
DR PDB; 6TB3; EM; 2.80 A; D=23-143.
DR PDB; 6TNU; EM; 3.10 A; D=23-143.
DR PDB; 6WDR; EM; 3.70 A; M=18-142.
DR PDB; 6WOO; EM; 2.90 A; MM=20-143.
DR PDB; 6Y7C; EM; 3.80 A; M=1-143.
DR PDB; 6Z6J; EM; 3.40 A; SM=1-143.
DR PDB; 6Z6K; EM; 3.40 A; SM=1-143.
DR PDB; 6ZCE; EM; 5.30 A; N=1-143.
DR PDB; 6ZU9; EM; 6.20 A; F=1-143.
DR PDB; 6ZVI; EM; 3.00 A; u=20-143.
DR PDB; 7A1G; EM; 3.00 A; D=23-143.
DR PDB; 7B7D; EM; 3.30 A; D=23-143.
DR PDB; 7D5S; EM; 4.60 A; SN=1-143.
DR PDB; 7NRC; EM; 3.90 A; SD=23-143.
DR PDB; 7NRD; EM; 4.36 A; SD=20-143.
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; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
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; 5M1J; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WDR; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P48589; -.
DR SMR; P48589; -.
DR BioGRID; 34752; 691.
DR ComplexPortal; CPX-1599; 40S cytosolic small ribosomal subunit.
DR IntAct; P48589; 14.
DR MINT; P48589; -.
DR STRING; 4932.YOR369C; -.
DR CarbonylDB; P48589; -.
DR iPTMnet; P48589; -.
DR MaxQB; P48589; -.
DR PaxDb; P48589; -.
DR PRIDE; P48589; -.
DR TopDownProteomics; P48589; -.
DR EnsemblFungi; YOR369C_mRNA; YOR369C; YOR369C.
DR GeneID; 854551; -.
DR KEGG; sce:YOR369C; -.
DR SGD; S000005896; RPS12.
DR VEuPathDB; FungiDB:YOR369C; -.
DR eggNOG; KOG3406; Eukaryota.
DR GeneTree; ENSGT00390000018318; -.
DR HOGENOM; CLU_110343_1_0_1; -.
DR InParanoid; P48589; -.
DR OMA; CDEPMYK; -.
DR BioCyc; YEAST:G3O-33837-MON; -.
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-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 ChiTaRS; RPS12; yeast.
DR PRO; PR:P48589; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P48589; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR000530; Ribosomal_S12e.
DR PANTHER; PTHR11843; PTHR11843; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00972; RIBSOMALS12E.
DR SUPFAM; SSF55315; SSF55315; 1.
DR PROSITE; PS01189; RIBOSOMAL_S12E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..143
FT /note="40S ribosomal protein S12"
FT /id="PRO_0000122340"
FT CROSSLNK 85
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 90..92
FT /note="KVA -> EGLP (in Ref. 2; AAA69926)"
FT /evidence="ECO:0000305"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 98..102
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6RBD"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 143 AA; 15472 MW; 7BD0434EB06A26B3 CRC64;
MSDVEEVVEV QEETVVEQTA EVTIEDALKV VLRTALVHDG LARGLRESTK ALTRGEALLV
VLVSSVTEAN IIKLVEGLAN DPENKVPLIK VADAKQLGEW AGLGKIDREG NARKVVGASV
VVVKNWGAET DELSMIMEHF SQQ
