ISP2_HEMAM
ID ISP2_HEMAM Reviewed; 163 AA.
AC P05140;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Type-2 ice-structuring protein;
DE AltName: Full=Type II antifreeze protein;
DE Short=AFP;
DE Flags: Precursor;
OS Hemitripterus americanus (Sea raven).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Cottales; Agonidae; Hemitripterinae;
OC Hemitripterus.
OX NCBI_TaxID=8094;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3782083; DOI=10.1016/s0021-9258(18)66772-9;
RA Ng N.F.L., Trinh K.-Y., Hew C.-L.;
RT "Structure of an antifreeze polypeptide precursor from the sea raven,
RT Hemitripterus americanus.";
RL J. Biol. Chem. 261:15690-15695(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 36-41; 52-63;
RP 95-97; 111-116 AND 121-137, SUBCELLULAR LOCATION, AND PTM.
RX PubMed=2572595; DOI=10.1016/s0021-9258(18)51532-5;
RA Hayes P., Scott G.K., Ng N.F.L., Hew C.-L., Davies P.L.;
RT "Cystine-rich type II antifreeze protein precursor is initiated from the
RT third AUG codon of its mRNA.";
RL J. Biol. Chem. 264:18761-18767(1989).
RN [3]
RP PRELIMINARY DISULFIDE BONDS, AND SIMILARITY TO C-TYPE LECTINS.
RX PubMed=1644794; DOI=10.1016/s0021-9258(18)41967-9;
RA Ng N.F.L., Hew C.-L.;
RT "Structure of an antifreeze polypeptide from the sea raven. Disulfide bonds
RT and similarity to lectin-binding proteins.";
RL J. Biol. Chem. 267:16069-16075(1992).
RN [4]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=9537986; DOI=10.1021/bi972788c;
RA Gronwald W., Loewen M.C., Lix B., Daugulis A.J., Soennichsen F.D.,
RA Davies P.L., Sykes B.D.;
RT "The solution structure of type II antifreeze protein reveals a new member
RT of the lectin family.";
RL Biochemistry 37:4712-4721(1998).
CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2572595}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:2572595}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA49617.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J02593; AAA49617.1; ALT_INIT; mRNA.
DR EMBL; J05100; AAA49618.1; -; Genomic_DNA.
DR PIR; A34313; A34313.
DR PDB; 2AFP; NMR; -; A=35-163.
DR PDBsum; 2AFP; -.
DR AlphaFoldDB; P05140; -.
DR BMRB; P05140; -.
DR SMR; P05140; -.
DR EvolutionaryTrace; P05140; -.
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; Direct protein sequencing;
KW Disulfide bond; Lectin; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..34
FT /evidence="ECO:0000305|PubMed:2572595"
FT /id="PRO_0000017544"
FT CHAIN 35..163
FT /note="Type-2 ice-structuring protein"
FT /evidence="ECO:0000305|PubMed:2572595"
FT /id="PRO_0000017545"
FT DOMAIN 39..163
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 41..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:9537986"
FT DISULFID 69..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:9537986"
FT DISULFID 103..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:9537986"
FT DISULFID 123..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:9537986"
FT DISULFID 135..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:9537986"
FT CONFLICT 38
FT /note="P -> G (in Ref. 2; AAA49618)"
FT /evidence="ECO:0000305"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2AFP"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2AFP"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:2AFP"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2AFP"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:2AFP"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:2AFP"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2AFP"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2AFP"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2AFP"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2AFP"
SQ SEQUENCE 163 AA; 17509 MW; 52C2D284F65E8A47 CRC64;
MLTVSLLVCA MMALTQANDD KILKGTATEA GPVSQRAPPN CPAGWQPLGD RCIYYETTAM
TWALAETNCM KLGGHLASIH SQEEHSFIQT LNAGVVWIGG SACLQAGAWT WSDGTPMNFR
SWCSTKPDDV LAACCMQMTA AADQCWDDLP CPASHKSVCA MTF
