IBP_COLSX
ID IBP_COLSX Reviewed; 253 AA.
AC A5XB26;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Ice-binding protein {ECO:0000303|PubMed:17651136, ECO:0000312|EMBL:ABH08428.1};
DE AltName: Full=Antifreeze protein {ECO:0000303|PubMed:24938370};
DE Short=AFP;
DE Flags: Precursor;
OS Colwellia sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=56799;
RN [1] {ECO:0000312|EMBL:ABH08428.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 179-188 AND 216-227,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=SLW05 {ECO:0000303|PubMed:17651136, ECO:0000312|EMBL:ABH08428.1};
RX PubMed=17651136; DOI=10.1111/j.1574-6941.2007.00345.x;
RA Raymond J.A., Fritsen C., Shen K.;
RT "An ice-binding protein from an Antarctic sea ice bacterium.";
RL FEMS Microbiol. Ecol. 61:214-221(2007).
RN [2] {ECO:0007744|PDB:3WP9}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 28-253, FUNCTION, DISULFIDE BOND,
RP MUTAGENESIS OF THR-214; SER-217; THR-232; ALA-233 AND THR-235, AND CIRCULAR
RP DICHROISM ANALYSIS.
RC STRAIN=SLW05 {ECO:0000303|PubMed:24938370};
RX PubMed=24938370; DOI=10.1111/febs.12878;
RA Hanada Y., Nishimiya Y., Miura A., Tsuda S., Kondo H.;
RT "Hyperactive antifreeze protein from an Antarctic sea ice bacterium
RT Colwellia sp. has a compound ice-binding site without repetitive
RT sequences.";
RL FEBS J. 281:3576-3590(2014).
CC -!- FUNCTION: Binds to the surface of ice crystals and inhibits their
CC growth (PubMed:17651136, PubMed:24938370). Has ice recrystallization
CC inhibition (RI) activity (the ability to prevent the formation of
CC larger grains of ice at the expense of smaller grains), which may
CC protect membranes from freezing injury (Probable). Has high thermal
CC hysteresis (TH) activity, which is the ability to lower the freezing
CC point of an aqueous solution below its melting point, and thus the
CC freezing of the cell fluid can be prevented protecting the organism
CC from ice damage. The TH activity of this protein is 3.8 degrees Celsius
CC at 14 mM (PubMed:24938370). {ECO:0000269|PubMed:17651136,
CC ECO:0000269|PubMed:24938370, ECO:0000305|PubMed:17651136}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17651136}.
CC -!- SIMILARITY: Belongs to the ice-binding protein family. {ECO:0000305}.
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DR EMBL; DQ788793; ABH08428.1; -; Genomic_DNA.
DR PDB; 3WP9; X-ray; 1.60 A; A=28-253.
DR PDBsum; 3WP9; -.
DR AlphaFoldDB; A5XB26; -.
DR SMR; A5XB26; -.
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;
KW Disulfide bond; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..253
FT /note="Ice-binding protein"
FT /evidence="ECO:0000255"
FT /id="PRO_5002689647"
FT MOTIF 220..223
FT /note="Ice-binding site motif (T-A/G-X-T/N) 1"
FT /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT MOTIF 232..235
FT /note="Ice-binding site motif (T-A/G-X-T/N) 2"
FT /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT SITE 67
FT /note="Ice-binding"
FT /evidence="ECO:0000250|UniProtKB:C7F6X3"
FT SITE 220
FT /note="Ice-binding"
FT /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT DISULFID 75..93
FT /evidence="ECO:0000269|PubMed:24938370,
FT ECO:0007744|PDB:3WP9"
FT MUTAGEN 214
FT /note="T->Y: Has 20% thermal hysteresis (TH) activity of
FT that of the wild-type. Has 2.6% thermal hysteresis (TH)
FT activity of that of the wild-type; when associated with Y-
FT 233."
FT /evidence="ECO:0000269|PubMed:24938370"
FT MUTAGEN 217
FT /note="S->Y: No effect on thermal hysteresis (TH)
FT activity."
FT /evidence="ECO:0000269|PubMed:24938370"
FT MUTAGEN 232
FT /note="T->K: Increased thermal hysteresis (TH) activity
FT compared to wild-type."
FT /evidence="ECO:0000269|PubMed:24938370"
FT MUTAGEN 232
FT /note="T->Y: Has 50% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:24938370"
FT MUTAGEN 233
FT /note="A->Y: Significant decrease in thermal hysteresis
FT (TH) activity compared to wild-type. Has 2.6% thermal
FT hysteresis (TH) activity of that of the wild-type; when
FT associated with Y-214."
FT /evidence="ECO:0000269|PubMed:24938370"
FT MUTAGEN 235
FT /note="T->Y: Has 17% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:24938370"
FT CONFLICT 216
FT /note="I -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3WP9"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3WP9"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3WP9"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3WP9"
FT HELIX 98..116
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3WP9"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:3WP9"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 205..214
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:3WP9"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3WP9"
SQ SEQUENCE 253 AA; 26350 MW; BC6CD0F4E1CEB307 CRC64;
MKTLISNSKK VLIPLIMGSI FAGNVMAAGP YAVELGEAGT FTILSKSGIT DVYPSTVTGN
VGTSPITGAA LLLNCDEVTG AMYTVDSAGP LPCSINSPYL LELAVSDMGI AYNDAAGRVP
ADHTELGTGE IGGLTLEPGV YKWSSDVNIS TDVTFNGTMD DVWIMQISGN LNQANAKRVT
LTGGALAKNI FWQVAGYTAL GTYASFEGIV LSKTLISVNT GTTVNGRLLA QTAVTLQKNT
INAPTEQYEE APL
