ID   LECS_RANJA              Reviewed;         111 AA.
AC   P18839;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Sialic acid-binding lectin;
DE            EC=3.1.27.-;
OS   Rana japonica (Japanese reddish frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX   NCBI_TaxID=8402;
RN   [1]
RP   PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, AND DISULFIDE BONDS.
RC   TISSUE=Egg;
RX   PubMed=2229005; DOI=10.1093/oxfordjournals.jbchem.a123153;
RA   Kamiya Y., Oyama F., Oyama R., Sakakibara F., Nitta K., Kawauchi H.,
RA   Takayanagi Y., Titani K.;
RT   "Amino acid sequence of a lectin from Japanese frog (Rana japonica) eggs.";
RL   J. Biochem. 108:139-143(1990).
CC   -!- FUNCTION: The S-lectins in frog eggs may be involved in the
CC       fertilization and development of the frog embryo. This lectin
CC       preferentially agglutinate a large variety of tumor cells, but it does
CC       not agglutinate non-transformed cells and erythrocytes.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   PIR; JX0120; JX0120.
DR   AlphaFoldDB; P18839; -.
DR   SMR; P18839; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.10.130.10; -; 1.
DR   InterPro; IPR001427; RNaseA.
DR   InterPro; IPR036816; RNaseA-like_dom_sf.
DR   InterPro; IPR023411; RNaseA_AS.
DR   InterPro; IPR023412; RNaseA_domain.
DR   PANTHER; PTHR11437; PTHR11437; 1.
DR   Pfam; PF00074; RnaseA; 1.
DR   SMART; SM00092; RNAse_Pc; 1.
DR   SUPFAM; SSF54076; SSF54076; 1.
DR   PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lectin;
KW   Nuclease; Pyrrolidone carboxylic acid; Secreted.
FT   CHAIN           1..111
FT                   /note="Sialic acid-binding lectin"
FT                   /id="PRO_0000057173"
FT   ACT_SITE        10
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        104
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         5
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         35..39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:2229005"
FT   DISULFID        19..72
FT                   /evidence="ECO:0000269|PubMed:2229005"
FT   DISULFID        34..82
FT                   /evidence="ECO:0000269|PubMed:2229005"
FT   DISULFID        52..97
FT                   /evidence="ECO:0000269|PubMed:2229005"
FT   DISULFID        94..111
FT                   /evidence="ECO:0000269|PubMed:2229005"
SQ   SEQUENCE   111 AA;  12326 MW;  FDEBDDF3834ED679 CRC64;
     QNWAKFQEKH IPNTSNINCN TIMDKSIYIV GGQCKERNTF IISSATTVKA ICSGASTNRN
     VLSTTRFQLN TCIRSATAPR PCPYNSRTET NVICVKCENR LPVHFAGIGR C