ID SIL1_CYLFU Reviewed; 265 AA. AC Q9SE35; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 25-MAY-2022, entry version 63. DE RecName: Full=Silaffin-1; DE AltName: Full=natSil-1; DE Contains: DE RecName: Full=Silaffin-1B; DE Contains: DE RecName: Full=Silaffin-1A2; DE Contains: DE RecName: Full=Silaffin-1A1; DE Flags: Precursor; GN Name=SIL1; OS Cylindrotheca fusiformis (Marine diatom). OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; OC Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae; OC Cylindrotheca. OX NCBI_TaxID=2853; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 108-120; 141-151 AND RP 163-173, FUNCTION, METHYLATION AT LYS-144 AND LYS-166, AND RP METHYLAMINOPROPYLATION AT LYS-143 AND LYS-165. RX PubMed=10550045; DOI=10.1126/science.286.5442.1129; RA Kroeger N., Deutzmann R., Sumper M.; RT "Polycationic peptides from diatom biosilica that direct silica nanosphere RT formation."; RL Science 286:1129-1132(1999). RN [2] RP PROTEIN SEQUENCE OF 141-158 AND 163-177, MASS SPECTROMETRY, METHYLATION AT RP LYS-111; LYS-144; LYS-155; LYS-166; LYS-185; LYS-204; LYS-223 AND LYS-242, RP METHYLAMINOPROPYLATION AT LYS-110; LYS-143; LYS-154; LYS-165; LYS-177; RP LYS-184; LYS-196; LYS-203; LYS-215; LYS-222; LYS-234; LYS-241 AND LYS-253, RP AND METHYLHYDROXYLATION AT LYS-174; LYS-193; LYS-212; LYS-231 AND LYS-250. RX PubMed=11349130; DOI=10.1074/jbc.m102093200; RA Kroeger N., Deutzmann R., Sumper M.; RT "Silica-precipitating peptides from diatoms. The chemical structure of RT silaffin-A from Cylindrotheca fusiformis."; RL J. Biol. Chem. 276:26066-26070(2001). RN [3] RP FUNCTION. RX PubMed=11106386; DOI=10.1073/pnas.260496497; RA Kroeger N., Deutzmann R., Bergsdorf C., Sumper M.; RT "Species-specific polyamines from diatoms control silica morphology."; RL Proc. Natl. Acad. Sci. U.S.A. 97:14133-14138(2000). RN [4] RP FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-163; SER-164; SER-167; SER-169; RP SER-171; SER-173; SER-176; SER-182; SER-183; SER-186; SER-188; SER-190; RP SER-192; SER-195; SER-201; SER-202; SER-205; SER-207; SER-209; SER-211; RP SER-214; SER-220; SER-221; SER-224; SER-226; SER-228; SER-230; SER-233; RP SER-239; SER-240; SER-243; SER-245; SER-247; SER-249 AND SER-252, AND RP METHYLHYDROXYLATION AT LYS-174; LYS-193; LYS-212; LYS-231 AND LYS-250. RX PubMed=12386330; DOI=10.1126/science.1076221; RA Kroeger N., Lorenz S., Brunner E., Sumper M.; RT "Self-assembly of highly phosphorylated silaffins and their function in RT biosilica morphogenesis."; RL Science 298:584-586(2002). RN [5] RP BIOTECHNOLOGICAL RELEVANCE. RX PubMed=11565027; DOI=10.1038/35095031; RA Brott L.L., Naik R.R., Pikas D.J., Kirkpatrick S.M., Tomlin D.W., RA Whitlock P.W., Clarson S.J., Stone M.O.; RT "Ultrafast holographic nanopatterning of biocatalytically formed silica."; RL Nature 413:291-293(2001). RN [6] RP BIOTECHNOLOGICAL RELEVANCE. RX PubMed=14716316; DOI=10.1038/nbt931; RA Luckarift H.R., Spain J.C., Naik R.R., Stone M.O.; RT "Enzyme immobilization in a biomimetic silica support."; RL Nat. Biotechnol. 22:211-213(2004). CC -!- FUNCTION: Catalyzes the polymerization of silica spheres from a CC silicilic acid solution. It therefore plays a central role in the CC formation of silica cell wall of diatoms. {ECO:0000269|PubMed:10550045, CC ECO:0000269|PubMed:11106386, ECO:0000269|PubMed:12386330}. CC -!- SUBUNIT: Silaffin-1A peptides form large aggregates via electrostatic CC interactions due to intermolecular interactions between the negatively CC charged phosphate groups and the polyamine moieties. CC {ECO:0000269|PubMed:12386330}. CC -!- DOMAIN: It is unknown whether the acidic chain located at the N- CC terminus is functional or whether it represents a propeptide. CC -!- PTM: N6-polymethylaminopropylated. Two lysine residues of each peptide CC bears 6 to 11 repeats of methyl-propylamine, which gives a possible CC template for nucleation, and may also control the silica colloid size CC within the silica deposition vesicle (SDV). CC -!- PTM: Phosphorylated. All serine residues of the Silaffin-1A1 peptide CC are phosphorylated. Only minor amounts of the Silaffin-1A2 peptide are CC phosphorylated. Phosphorylation is essential for the activity. It may CC represent a source of anions required for silica formation of diatoms. CC {ECO:0000269|PubMed:12386330}. CC -!- MASS SPECTROMETRY: [Silaffin-1A1]: Mass=2485.7; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:11349130}; CC -!- MASS SPECTROMETRY: [Silaffin-1A1]: Mass=2557.1; Mass_error=71.4; CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11349130}; CC -!- MASS SPECTROMETRY: [Silaffin-1A1]: Mass=2628.2; Mass_error=71.1; CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11349130}; CC -!- MASS SPECTROMETRY: [Silaffin-1A1]: Mass=2699.3; Mass_error=71.1; CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11349130}; CC -!- MASS SPECTROMETRY: [Silaffin-1A1]: Mass=2770.4; Mass_error=71.1; CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11349130}; CC -!- MASS SPECTROMETRY: [Silaffin-1A2]: Mass=2878.3; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:11349130}; CC -!- MASS SPECTROMETRY: [Silaffin-1A2]: Mass=2949.4; Mass_error=71.1; CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11349130}; CC -!- MASS SPECTROMETRY: [Silaffin-1A2]: Mass=3020.8; Mass_error=71.4; CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11349130}; CC -!- MASS SPECTROMETRY: [Silaffin-1A2]: Mass=3091.8; Mass_error=71; CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11349130}; CC -!- MASS SPECTROMETRY: [Silaffin-1A2]: Mass=3162.9; Mass_error=71.1; CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11349130}; CC -!- BIOTECHNOLOGY: Due to its ability to synthesize simple silica CC nanospheres in vitro from silanes at nearly neutral pH and at ambient CC temperatures and pressures, it is of great interest in nanotechnology. CC May be of practical use for the fabrication of photonic devices. CC {ECO:0000269|PubMed:11565027, ECO:0000269|PubMed:14716316}. CC -!- MISCELLANEOUS: The results of the mass spectrometry differ for the same CC peptide due to the length of the methyl-propylamine chains that vary CC from 14 to 18 units for the Silaffin-1A2 peptide (141-158) and from 13 CC to 17 units for the Silaffin-1A1 peptide (163-177). CC -!- MISCELLANEOUS: The species-specific pattern of biosilica pattern of CC diatoms may be generated by polyamines of different chain lengths as CC well as by a synergistic action of long-chain polyamines and silaffins. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Miniature masonry - Issue 43 CC of February 2004; CC URL="https://web.expasy.org/spotlight/back_issues/043"; 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; AF191634; AAF16940.1; -; Genomic_DNA. DR PIR; A59141; A59141. DR AlphaFoldDB; Q9SE35; -. DR SMR; Q9SE35; -. DR DIP; DIP-62079N; -. DR iPTMnet; Q9SE35; -. DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Biomineralization; Cleavage on pair of basic residues; KW Direct protein sequencing; Hydroxylation; Methylation; Phosphoprotein; KW Repeat; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT PROPEP 20..107 FT /note="Acidic" FT /evidence="ECO:0000269|PubMed:10550045" FT /id="PRO_0000032597" FT PEPTIDE 108..136 FT /note="Silaffin-1B" FT /evidence="ECO:0000305" FT /id="PRO_0000032598" FT PROPEP 137..140 FT /evidence="ECO:0000305" FT /id="PRO_0000032599" FT PEPTIDE 141..158 FT /note="Silaffin-1A2" FT /id="PRO_0000032600" FT PROPEP 159..162 FT /evidence="ECO:0000305" FT /id="PRO_0000032601" FT PEPTIDE 163..177 FT /note="Silaffin-1A1" FT /id="PRO_0000032602" FT PROPEP 178..181 FT /evidence="ECO:0000305" FT /id="PRO_0000032603" FT PEPTIDE 182..196 FT /note="Silaffin-1A1" FT /id="PRO_0000032604" FT PROPEP 197..200 FT /evidence="ECO:0000305" FT /id="PRO_0000032605" FT PEPTIDE 201..215 FT /note="Silaffin-1A1" FT /id="PRO_0000032606" FT PROPEP 216..219 FT /evidence="ECO:0000305" FT /id="PRO_0000032607" FT PEPTIDE 220..234 FT /note="Silaffin-1A1" FT /id="PRO_0000032608" FT PROPEP 235..238 FT /evidence="ECO:0000305" FT /id="PRO_0000032609" FT PEPTIDE 239..253 FT /note="Silaffin-1A1" FT /id="PRO_0000032610" FT PROPEP 254..265 FT /evidence="ECO:0000305" FT /id="PRO_0000032611" FT REPEAT 108..140 FT /note="R1; atypical" FT REPEAT 141..162 FT /note="R2; atypical" FT REPEAT 163..181 FT /note="R3" FT REPEAT 182..200 FT /note="R4" FT REPEAT 201..219 FT /note="R5" FT REPEAT 220..238 FT /note="R6" FT REPEAT 239..257 FT /note="R7" FT REGION 37..106 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 108..257 FT /note="7 X 19 AA repeat of S-S-K-K-S-G-S-Y-S-G-S-K-G-S-K-R- FT R-[IL]-L" FT REGION 122..265 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 37..92 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 122..252 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 110 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000305|PubMed:11349130" FT MOD_RES 111 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000305|PubMed:11349130" FT MOD_RES 143 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 144 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 154 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:11349130" FT MOD_RES 155 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:11349130" FT MOD_RES 163 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 164 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 165 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 166 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 167 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 169 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 174 FT /note="N6,N6,N6-trimethyl-5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:11349130, FT ECO:0000269|PubMed:12386330" FT MOD_RES 176 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 177 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:11349130" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 184 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 185 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 186 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 192 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 193 FT /note="N6,N6,N6-trimethyl-5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:11349130, FT ECO:0000269|PubMed:12386330" FT MOD_RES 195 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 196 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:11349130" FT MOD_RES 201 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 202 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 203 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 204 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 211 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 212 FT /note="N6,N6,N6-trimethyl-5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:11349130, FT ECO:0000269|PubMed:12386330" FT MOD_RES 214 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 215 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:11349130" FT MOD_RES 220 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 221 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 222 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 223 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 224 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 226 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 228 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 230 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 231 FT /note="N6,N6,N6-trimethyl-5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:11349130, FT ECO:0000269|PubMed:12386330" FT MOD_RES 233 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 234 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:11349130" FT MOD_RES 239 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 240 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 241 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 242 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:10550045, FT ECO:0000269|PubMed:11349130" FT MOD_RES 243 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 245 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 249 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 250 FT /note="N6,N6,N6-trimethyl-5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:11349130, FT ECO:0000269|PubMed:12386330" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12386330" FT MOD_RES 253 FT /note="N6-poly(methylaminopropyl)lysine" FT /evidence="ECO:0000269|PubMed:11349130" SQ SEQUENCE 265 AA; 27500 MW; E628FAF40E1B051B CRC64; MKLTAIFPLL FTAVGYCAAQ SIADLAAANL STEDSKSAQL ISADSSDDAS DSSVESVDAA SSDVSGSSVE SVDVSGSSLE SVDVSGSSLE SVDDSSEDSE EEELRILSSK KSGSYYSYGT KKSGSYSGYS TKKSASRRIL SSKKSGSYSG YSTKKSGSRR ILSSKKSGSY SGSKGSKRRI LSSKKSGSYS GSKGSKRRNL SSKKSGSYSG SKGSKRRILS SKKSGSYSGS KGSKRRNLSS KKSGSYSGSK GSKRRILSGG LRGSM //