ID   IBP_FLAPO               Reviewed;         247 AA.
AC   B8XC03; B8XC02;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Ice-binding protein {ECO:0000303|PubMed:19121299, ECO:0000312|EMBL:ACL27143.1, ECO:0000312|EMBL:ACL27144.1};
DE   AltName: Full=Antifreeze protein {ECO:0000305};
DE            Short=AFP {ECO:0000305};
DE   Flags: Precursor;
OS   Flammulina populicola (Enokitake mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Physalacriaceae; Flammulina.
OX   NCBI_TaxID=72155;
RN   [1] {ECO:0000312|EMBL:ACL27144.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RX   PubMed=19121299; DOI=10.1016/j.cryobiol.2008.11.009;
RA   Raymond J.A., Janech M.G.;
RT   "Ice-binding proteins from enoki and shiitake mushrooms.";
RL   Cryobiology 58:151-156(2009).
CC   -!- FUNCTION: Binds ice crystals and most probably inhibits their growth in
CC       order to prevent cell damage from extracellular ice.
CC       {ECO:0000305|PubMed:19121299}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ice-binding protein family. {ECO:0000305}.
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DR   EMBL; FJ200000; ACL27143.1; -; mRNA.
DR   EMBL; FJ200001; ACL27144.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8XC03; -.
DR   SMR; B8XC03; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR021884; Ice-bd_prot.
DR   Pfam; PF11999; Ice_binding; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..247
FT                   /note="Ice-binding protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5002880254"
FT   SITE            64
FT                   /note="Ice-binding"
FT                   /evidence="ECO:0000250|UniProtKB:C7F6X3"
FT   SITE            146
FT                   /note="Ice-binding"
FT                   /evidence="ECO:0000250|UniProtKB:C7F6X3"
FT   SITE            218
FT                   /note="Ice-binding"
FT                   /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        45
FT                   /note="P -> L (in Ref. 1; ACL27143)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   247 AA;  24908 MW;  B5F728C439A53826 CRC64;
     MTFSILSIFV FGLISSSVAL GPAPVLLGKA ENFAILSETG VSNVPDSSVN CDIGVSPIGA
     SGVTGFSLTG DSGGSFSTSK QVTGRVYAST YGDPTPASLT TAVFDMENAY KDAQERIDPD
     FTNLHTGALG GAILVPGLYK FTTGVSITAD LVLTGGPTDT YIFQIAGTLS LAAGVKINLV
     GGLLPANVVW AVADSVTVAA TSSFQGILLG KTQVVVNTNA SVEGRILAQT AVVLQKATVI
     VPGVCGA