ID   IBP_LENED               Reviewed;         288 AA.
AC   B8XC04;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Ice-binding protein {ECO:0000303|PubMed:19121299, ECO:0000312|EMBL:ACL27145.1};
DE   AltName: Full=Antifreeze protein {ECO:0000305};
DE            Short=AFP {ECO:0000305};
DE   Flags: Precursor;
OS   Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Omphalotaceae; Lentinula.
OX   NCBI_TaxID=5353 {ECO:0000312|EMBL:ACL27145.1};
RN   [1] {ECO:0000312|EMBL:ACL27145.1}
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; FJ200002; ACL27145.1; -; mRNA.
DR   EMBL; FJ200003; ACL27146.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8XC04; -.
DR   SMR; B8XC04; -.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..288
FT                   /note="Ice-binding protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5007645459"
FT   MOTIF           75..78
FT                   /note="Ice-binding site motif (T-A/G-X-T/N) 1"
FT                   /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT   MOTIF           154..157
FT                   /note="Ice-binding site motif (T-A/G-X-T/N) 2"
FT                   /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT   MOTIF           196..199
FT                   /note="Ice-binding site motif (T-A/G-X-T/N) 3"
FT                   /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT   MOTIF           265..268
FT                   /note="Ice-binding site motif (T-A/G-X-T/N) 4"
FT                   /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT   SITE            110
FT                   /note="Ice-binding"
FT                   /evidence="ECO:0000250|UniProtKB:C7F6X3"
FT   SITE            192
FT                   /note="Ice-binding"
FT                   /evidence="ECO:0000250|UniProtKB:C7F6X3"
FT   SITE            265
FT                   /note="Ice-binding"
FT                   /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT   SITE            280
FT                   /note="Ice-binding"
FT                   /evidence="ECO:0000250|UniProtKB:C7F6X3"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   288 AA;  27986 MW;  DE52DA04A0463B68 CRC64;
     MFSTTLINTF SLGLLAVVSV VAAPGGISVG PISIGPGGIS LGPGGISIGP GGINLGPGGG
     PGAINAGPAA VNLGTAGNYA ILAKSGISTV PESIISGNIG VSPISTTAFT GFSETLDSTG
     KFATSQQVVG ELFAASFAAP TPTTLTTAVS DMQTAFNDAT GRVTPDFTNL GGGELGGLVL
     TPGLYKWTGA VSVNSTGVTI AGTPLDHFIF QIPATLGFAA ASRVTLVGGI PASNIVWAAT
     SVVTAGAGSH IEGVVLAKTA VTLETGATMN GRILAQTFVA LQSATVIG