ID   SXT2_TAKPA              Reviewed;         391 AA.
AC   Q90WJ9;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Saxitoxin and tetrodotoxin-binding protein 2;
DE   Flags: Precursor;
GN   Name=psbp2; Synonyms=pstbp2;
OS   Takifugu pardalis (Panther puffer) (Tetraodon pardalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=98921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-44 AND 116-140,
RP   FUNCTION, SUBUNIT, AND GLYCOSYLATION.
RC   TISSUE=Liver;
RX   PubMed=11722582; DOI=10.1046/j.0014-2956.2001.02547.x;
RA   Yotsu-Yamashita M., Sugimoto A., Terakawa T., Shoji Y., Miyazawa T.,
RA   Yasumoto T.;
RT   "Purification, characterization, and cDNA cloning of a novel soluble
RT   saxitoxin and tetrodotoxin binding protein from plasma of the puffer fish,
RT   Fugu pardalis.";
RL   Eur. J. Biochem. 268:5937-5946(2001).
CC   -!- FUNCTION: Binds both saxitoxin and tetradotoxin. May play a role in
CC       toxin accumulation and/or excretion. {ECO:0000269|PubMed:11722582}.
CC   -!- SUBUNIT: Homodimer or heterodimer of PSTBP1 and PSTBP2.
CC       {ECO:0000269|PubMed:11722582}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:11722582}.
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DR   EMBL; AB037569; BAB55583.1; -; mRNA.
DR   AlphaFoldDB; Q90WJ9; -.
DR   SMR; Q90WJ9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.40.128.20; -; 2.
DR   InterPro; IPR012674; Calycin.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:11722582"
FT   CHAIN           21..391
FT                   /note="Saxitoxin and tetrodotoxin-binding protein 2"
FT                   /id="PRO_0000022460"
FT   REPEAT          24..202
FT                   /note="1"
FT   REPEAT          203..391
FT                   /note="2"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   391 AA;  43886 MW;  6863450D7C040365 CRC64;
     MGAVPGVVLL LMLAVLGIRA APAPEECHKL TKPVLKADVQ NVSGDWVLVW SVANTTERWI
     CENLTSSYVE FKLHSDIIEY TERNLFLGNS CISFYSNLSA STEKQQQFSL NNLQMEEKGV
     VRPFNDNGTV KFFETCVDCL SMEYSGDIGR FLLIYRRDGV HQNVEVLKAA RDESQKLAEC
     LGFSIDEPFI YDGVSDFCHK KSPEECHKLT KPVTKADVQS VSGDWVLVWS VAENISTSNE
     WTKLKSSHVE LRIHSGVIVL NERNMLKNNS CMTFKTNMTA GPESQNTFIY TSGKMEENGV
     DKELDENGTV KFFETCADCL SIDYSGLFGH VLFVYRRDGV HQNVEVLKAA QDESQKLAEC
     LGFSIGEPFI YDGVSDFCHK KSSPEVKPEQ D