ID   SAL_SILAS               Reviewed;         308 AA.
AC   Q9PVW8;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Rhamnose-binding lectin;
DE   AltName: Full=RBL;
DE   AltName: Full=Roe lectin;
DE   AltName: Full=SAL;
DE   Flags: Precursor;
OS   Silurus asotus (Amur catfish) (Parasilurus asotus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Siluridae; Silurus.
OX   NCBI_TaxID=30991;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-71.
RX   PubMed=10564781; DOI=10.1016/s0304-4165(99)00185-3;
RA   Hosono M., Ishikawa K., Mineki R., Murayama K., Numata C., Ogawa Y.,
RA   Takayanagi Y., Nitta K.;
RT   "Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus
RT   asotus) eggs.";
RL   Biochim. Biophys. Acta 1472:668-675(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-52, AND CHARACTERIZATION.
RC   TISSUE=Egg;
RX   PubMed=8369743; DOI=10.1248/bpb.16.1;
RA   Hosono M., Kawauchi H., Nitta K., Takayanagi Y., Shiokawa H., Mineki R.,
RA   Murayama K.;
RT   "Purification and characterization of Silurus asotus (catfish) roe
RT   lectin.";
RL   Biol. Pharm. Bull. 16:1-5(1993).
RN   [3]
RP   SUBUNIT.
RX   PubMed=9177694; DOI=10.1006/abio.1997.2058;
RA   Murayama K., Taka H., Kaga N., Fujimura T., Mineki R., Shindo N.,
RA   Morita M., Hosono M., Nitta K.;
RT   "The structure of Silurus asotus (catfish) roe lectin (SAL): identification
RT   of a noncovalent trimer by mass spectrometry and analytical
RT   ultracentrifugation.";
RL   Anal. Biochem. 247:319-326(1997).
CC   -!- FUNCTION: Lectin that binds L-rhamnose. Binds also monosaccharides
CC       possessing steric similarity to the hydroxyl group orientation at C2
CC       and C4 of the pyranose ring structure of L-rhamnose, such as L-mannose
CC       and L-lyxose.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:9177694}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in eggs, but not in liver.
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DR   EMBL; AB020571; BAA87860.1; -; mRNA.
DR   AlphaFoldDB; Q9PVW8; -.
DR   SMR; Q9PVW8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.740; -; 3.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   Pfam; PF02140; Gal_Lectin; 3.
DR   PROSITE; PS50228; SUEL_LECTIN; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Lectin; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:10564781,
FT                   ECO:0000269|PubMed:8369743"
FT   CHAIN           24..308
FT                   /note="Rhamnose-binding lectin"
FT                   /id="PRO_0000017670"
FT   DOMAIN          27..115
FT                   /note="SUEL-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   DOMAIN          123..213
FT                   /note="SUEL-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   DOMAIN          218..308
FT                   /note="SUEL-type lectin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   308 AA;  32770 MW;  043DBC2E786A79B7 CRC64;
     MMLILKLSLL SLLIATPGLL VSGANMITCY GDVQKLHCET GLIIVKSSLY GRTDSTTCST
     NRPPAQVAVT TCSLPITTIG DRCNGLPDCE LKTDLLGNTD PCQGTYKYYN TSFDCINGNY
     AVICEHGYST LDCGNDAILI VNANYGRASS QICSNGLPNG LTQNTNCYAA NTLTTVAGLC
     NGKKSCTVEA LNTIFSDPCS GTVKYLTVTY ICTKEMVVCE GGSASINCGA QTIKTIWANY
     GRTDSTVCST GRPGSQLLNT NCYTSDTLNK VAAGCDHLST CTIPANNNFF GDPCPNTYKY
     LRIVYACV