IBPKB_TYPIS
ID IBPKB_TYPIS Reviewed; 243 AA.
AC Q76CE6;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Ice-binding protein K3-B1 {ECO:0000305};
DE AltName: Full=Antifreeze protein 6 {ECO:0000303|PubMed:22645341};
DE Short=AFP6 {ECO:0000305};
DE AltName: Full=TAFP-2 {ECO:0000303|Ref.1};
DE AltName: Full=TisAFP6 {ECO:0000303|PubMed:22645341};
DE Flags: Precursor;
GN Name=K3-B1 {ECO:0000312|EMBL:BAD02893.1};
OS Typhula ishikariensis (Gray snow mold fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Thelephorales; Typhulaceae; Typhula.
OX NCBI_TaxID=69361;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-40, INDUCTION, MASS
RP SPECTROMETRY, AND SIGNAL.
RC STRAIN=BRB-1 {ECO:0000303|Ref.1};
RX DOI=10.1139/B03-116;
RA Hoshino T., Kiriaki M., Ohgiya S., Fujiwara M., Kondo H., Nishimiya Y.,
RA Yumoto I., Tsuda S.;
RT "Antifreeze proteins from snow mold fungi.";
RL Can. J. Bot. 81:1175-1181(2003).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF SER-232.
RX PubMed=27613857; DOI=10.1042/bcj20160543;
RA Cheng J., Hanada Y., Miura A., Tsuda S., Kondo H.;
RT "Hydrophobic ice-binding sites confer hyperactivity of an antifreeze
RT protein from a snow mold fungus.";
RL Biochem. J. 473:4011-4026(2016).
RN [3] {ECO:0007744|PDB:3VN3}
RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) OF 21-243, FUNCTION, SITE, AND
RP MUTAGENESIS OF THR-102; ASN-198 AND VAL-241.
RC STRAIN=BRB-1 {ECO:0000303|PubMed:22645341};
RX PubMed=22645341; DOI=10.1073/pnas.1121607109;
RA Kondo H., Hanada Y., Sugimoto H., Hoshino T., Garnham C.P., Davies P.L.,
RA Tsuda S.;
RT "Ice-binding site of snow mold fungus antifreeze protein deviates from
RT structural regularity and high conservation.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:9360-9365(2012).
CC -!- FUNCTION: Binds to the surface of ice crystals. Has low thermal
CC hysteresis (TH) activity, which is the ability to lower the freezing
CC point of an aqueous solution below its melting point (PubMed:22645341).
CC The TH activity of this protein is approximately 0.3 degrees Celsius at
CC 11 mM (PubMed:27613857). {ECO:0000269|PubMed:22645341,
CC ECO:0000269|PubMed:27613857}.
CC -!- INDUCTION: By low temperatures, 0 degree Celsius. {ECO:0000269|Ref.1}.
CC -!- MASS SPECTROMETRY: Mass=21978; Method=MALDI; Note=The measured mass is
CC that of the mature protein.; Evidence={ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the ice-binding protein family. {ECO:0000305}.
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DR EMBL; AB109744; BAD02893.1; -; mRNA.
DR PDB; 3VN3; X-ray; 0.95 A; A/B=21-243.
DR PDBsum; 3VN3; -.
DR AlphaFoldDB; Q76CE6; -.
DR SMR; Q76CE6; -.
DR InterPro; IPR021884; Ice-bd_prot.
DR Pfam; PF11999; Ice_binding; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 21..243
FT /note="Ice-binding protein K3-B1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004287146"
FT SITE 198
FT /note="Ice-binding"
FT /evidence="ECO:0000305|PubMed:22645341"
FT MUTAGEN 102
FT /note="T->Y: Has 85% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:22645341"
FT MUTAGEN 198
FT /note="N->Y: Has 40% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:22645341"
FT MUTAGEN 232
FT /note="S->A: Slight increase in thermal hysteresis (TH)
FT activity (0.48 degrees Celsius) compared with that of the
FT wild-type (0.32 degrees Celsius) at 0.14 mM."
FT /evidence="ECO:0000269|PubMed:27613857"
FT MUTAGEN 241
FT /note="V->Y: Has 85% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:22645341"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:3VN3"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:3VN3"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:3VN3"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:3VN3"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3VN3"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:3VN3"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:3VN3"
SQ SEQUENCE 243 AA; 24093 MW; 063D02E6B34AADDD CRC64;
MFSASSLLAV IALAISSVSA AGPSAVPLGT AGNYVILAST GVSTVPQSVI TGAVGVSPGT
AASLTGFSLI LSGTGTFSTS SQVTGQLTGA DYGTPTPSIL TTAIGDMGTA YINAATRSGP
DFLEIYTGAL GGTTLLPGLY KWTSSVGASA DFTISGTSTD TWIFQIDGTL DVATGKQITL
VGGAQAKNII WVVAGAVNIE VGAKFEGTIL AKTAVTFKTG SSLNGRILAQ TSVALQSATI
VEK
