IBPKA_TYPIS
ID IBPKA_TYPIS Reviewed; 243 AA.
AC Q76CE8;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Ice-binding protein K1-A {ECO:0000305};
DE AltName: Full=Antifreeze protein 8 {ECO:0000303|PubMed:27613857};
DE Short=AFP8 {ECO:0000303|PubMed:27613857};
DE AltName: Full=TAFP-3 {ECO:0000303|Ref.1};
DE AltName: Full=TisAFP8 {ECO:0000303|PubMed:20030710, ECO:0000303|PubMed:27613857};
DE Flags: Precursor;
GN Name=K1-A {ECO:0000312|EMBL:BAD02891.1};
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 21-39, FUNCTION,
RP SUBCELLULAR LOCATION, INDUCTION, MASS 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, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=20030710; DOI=10.1111/j.1742-4658.2009.07490.x;
RA Xiao N., Suzuki K., Nishimiya Y., Kondo H., Miura A., Tsuda S., Hoshino T.;
RT "Comparison of functional properties of two fungal antifreeze proteins from
RT Antarctomyces psychrotrophicus and Typhula ishikariensis.";
RL FEBS J. 277:394-403(2010).
RN [3] {ECO:0007744|PDB:5B5H}
RP X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) OF 21-243, FUNCTION, SITE,
RP MUTAGENESIS OF ALA-40; PRO-145; ALA-167; GLY-171; LEU-172; SER-198 AND
RP ALA-232, AND CIRCULAR DICHROISM ANALYSIS.
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).
CC -!- FUNCTION: Binds to the surface of ice crystals (Ref.1, PubMed:20030710,
CC PubMed:27613857). Inhibits growth of the ice crystals
CC (PubMed:20030710). Has antifreeze activity for survival under snow
CC cover. Has high thermal hysteresis (TH) activity, which is the ability
CC to lower the freezing point of an aqueous solution below its melting
CC point, and thus the freezing of the cell fluid can be prevented
CC protecting the organism from ice damage (PubMed:20030710,
CC PubMed:27613857). The TH activity of this protein is 2.0 degrees
CC Celsius at 0.11 mM (PubMed:27613857). {ECO:0000269|PubMed:20030710,
CC ECO:0000269|PubMed:27613857, ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.8. {ECO:0000269|PubMed:20030710};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20030710,
CC ECO:0000269|Ref.1}.
CC -!- INDUCTION: By low temperatures, 0 degree Celsius. {ECO:0000269|Ref.1}.
CC -!- MASS SPECTROMETRY: Mass=22021; 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; AB109742; BAD02891.1; -; mRNA.
DR PDB; 5B5H; X-ray; 1.00 A; A=21-243.
DR PDBsum; 5B5H; -.
DR AlphaFoldDB; Q76CE8; -.
DR SMR; Q76CE8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR021884; Ice-bd_prot.
DR Pfam; PF11999; Ice_binding; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antifreeze protein; Direct protein sequencing; Secreted;
KW Signal; Stress response.
FT SIGNAL 1..20
FT /evidence="ECO:0000255, ECO:0000269|Ref.1"
FT CHAIN 21..243
FT /note="Ice-binding protein K1-A"
FT /evidence="ECO:0000255"
FT /id="PRO_5004286028"
FT SITE 40
FT /note="Ice-binding"
FT /evidence="ECO:0000305|PubMed:27613857"
FT SITE 232
FT /note="Ice-binding"
FT /evidence="ECO:0000305|PubMed:27613857"
FT MUTAGEN 40
FT /note="A->T: Has 46% thermal hysteresis (TH) activity of
FT that of the wild-type. Has 25% thermal hysteresis (TH)
FT activity of that of the wild-type; when associated with S-
FT 232."
FT /evidence="ECO:0000269|PubMed:27613857"
FT MUTAGEN 145
FT /note="P->S: Has 58% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:27613857"
FT MUTAGEN 167
FT /note="A->D: Has 63% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:27613857"
FT MUTAGEN 171
FT /note="G->D: Has 81% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:27613857"
FT MUTAGEN 172
FT /note="L->V: Has 66% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:27613857"
FT MUTAGEN 198
FT /note="S->N: Has 63% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:27613857"
FT MUTAGEN 232
FT /note="A->S: Has 32% thermal hysteresis (TH) activity of
FT that of the wild-type. Has 25% thermal hysteresis (TH)
FT activity of that of the wild-type; when associated with T-
FT 40."
FT /evidence="ECO:0000269|PubMed:27613857"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5B5H"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5B5H"
FT HELIX 96..115
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:5B5H"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5B5H"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:5B5H"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:5B5H"
SQ SEQUENCE 243 AA; 24199 MW; E71441A3D39C9934 CRC64;
MFSSTYLLAI IALAVSSVFA AGPTAVPLGT AGNYAILASA GVSTVPQSVI TGAVGLSPAA
ATFLTGFSLT MSSTGTFSTS TQVTGQLTAA DYGTPTPSIL TTAIGDMGTA YVNAATRSGP
NFLEIYTGAL GGKILPPGLY KWTSPVGASA DFTIIGTSTD TWIFQIAGTL GLAAGKKIIL
AGGAQAKNIV WVVAGAVSIE AGAKFEGVIL AKTAVTLKTG SSLNGRILSQ TAVALQKATV
VQK
