SIL1_CYLFU
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";
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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
