ISP2_BRASG
ID ISP2_BRASG Reviewed; 168 AA.
AC A0ZT93;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Type-2 ice-structuring protein {ECO:0000305};
DE AltName: Full=Type II antifreeze protein {ECO:0000303|PubMed:16754975, ECO:0000312|EMBL:BAF37106.1};
DE AltName: Full=lpAFP {ECO:0000303|PubMed:16754975};
DE Flags: Precursor;
OS Brachyopsis segaliensis (Sea poacher) (Brachyopsis rostratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Cottales; Agonidae; Brachyopsinae;
OC Brachyopsis.
OX NCBI_TaxID=1633465;
RN [1] {ECO:0000312|EMBL:BAF37106.1}
RP NUCLEOTIDE SEQUENCE [MRNA], CRYSTALLIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=16754975; DOI=10.1107/s1744309106015570;
RA Nishimiya Y., Kondo H., Yasui M., Sugimoto H., Noro N., Sato R., Suzuki M.,
RA Miura A., Tsuda S.;
RT "Crystallization and preliminary X-ray crystallographic analysis of Ca2+-
RT independent and Ca2+-dependent species of the type II antifreeze protein.";
RL Acta Crystallogr. F Struct. Biol. Commun. 62:538-541(2006).
RN [2] {ECO:0007744|PDB:2ZIB}
RP X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS) OF 42-168, FUNCTION, DISULFIDE
RP BONDS, AND MUTAGENESIS OF ILE-99; ALA-112 AND LEU-153.
RX PubMed=18674542; DOI=10.1016/j.jmb.2008.07.042;
RA Nishimiya Y., Kondo H., Takamichi M., Sugimoto H., Suzuki M., Miura A.,
RA Tsuda S.;
RT "Crystal structure and mutational analysis of Ca2+-independent type II
RT antifreeze protein from longsnout poacher, Brachyopsis rostratus.";
RL J. Mol. Biol. 382:734-746(2008).
CC -!- FUNCTION: Has antifreeze activity to protect fish blood from freezing
CC at subzero sea water temperatures (Probable). Binds to ice crystals and
CC inhibits their growth. The thermal hysteresis (TH) activity, the
CC ability to lower the blood freezing point, is approximately 0.45
CC degrees Celsius at 0.15 mM for this protein (PubMed:18674542).
CC {ECO:0000269|PubMed:18674542, ECO:0000305|PubMed:18674542}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16754975}.
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DR EMBL; AB283044; BAF37106.1; -; mRNA.
DR PDB; 2ZIB; X-ray; 1.34 A; A=42-168.
DR PDBsum; 2ZIB; -.
DR AlphaFoldDB; A0ZT93; -.
DR SMR; A0ZT93; -.
DR EvolutionaryTrace; A0ZT93; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR002353; AntifreezeII.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR PRINTS; PR00356; ANTIFREEZEII.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antifreeze protein; Disulfide bond; Lectin; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..34
FT /evidence="ECO:0000250|UniProtKB:P05140"
FT /id="PRO_0000445011"
FT CHAIN 35..168
FT /note="Type-2 ice-structuring protein"
FT /evidence="ECO:0000250|UniProtKB:P05140"
FT /id="PRO_5002631706"
FT DOMAIN 52..164
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 45..56
FT /evidence="ECO:0000269|PubMed:18674542,
FT ECO:0007744|PDB:2ZIB"
FT DISULFID 73..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:18674542, ECO:0007744|PDB:2ZIB"
FT DISULFID 107..138
FT /evidence="ECO:0000269|PubMed:18674542,
FT ECO:0007744|PDB:2ZIB"
FT DISULFID 127..149
FT /evidence="ECO:0000269|PubMed:18674542,
FT ECO:0007744|PDB:2ZIB"
FT DISULFID 139..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:18674542, ECO:0007744|PDB:2ZIB"
FT MUTAGEN 99
FT /note="I->F: Has 60% thermal hysteresis (TH) activity of
FT that of the wild-type. Has 60% thermal hysteresis (TH)
FT activity of that of the wild-type; when associated with F-
FT 112."
FT /evidence="ECO:0000269|PubMed:18674542"
FT MUTAGEN 112
FT /note="A->F: No effect on thermal hysteresis (TH) activity.
FT Has 60% thermal hysteresis (TH) activity of that of the
FT wild-type; when associated with F-99."
FT /evidence="ECO:0000269|PubMed:18674542"
FT MUTAGEN 153
FT /note="L->F: Nearly identical thermal hysteresis (TH)
FT activity with that of the wild-type."
FT /evidence="ECO:0000269|PubMed:18674542"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2ZIB"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:2ZIB"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:2ZIB"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2ZIB"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:2ZIB"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2ZIB"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2ZIB"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2ZIB"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:2ZIB"
SQ SEQUENCE 168 AA; 18023 MW; EFC07EA23214A658 CRC64;
MLTVSLLVCA MMALTQADHD GVLKGTATEA GEVSPVFRSR RALVCPAGWT LHGQRCFYSE
ATAMTWDLAE ANCVNKGGHL ASIHSLEEQL YIKDIVAGIV WIGGSACKVA GAWSWTDGTP
VDYRTWCPTK PNDILSDCCM QMTAAVDKCW DDLPCPASHA SICAKAAI
