ID   ELEL_ECHLU              Reviewed;         103 AA.
AC   C0HK24;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=L-rhamnose-binding lectin ELEL-1 {ECO:0000303|PubMed:25881955};
OS   Echinometra lucunter (Rock-boring urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinometridae;
OC   Echinometra.
OX   NCBI_TaxID=105361 {ECO:0000303|PubMed:25881955};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, LACK OF
RP   GLYCOSYLATION, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Egg {ECO:0000303|PubMed:25881955};
RX   PubMed=25881955; DOI=10.1016/j.ijbiomac.2015.03.072;
RA   Carneiro R.F., Teixeira C.S., de Melo A.A., de Almeida A.S., Cavada B.S.,
RA   de Sousa O.V., da Rocha B.A., Nagano C.S., Sampaio A.H.;
RT   "L-Rhamnose-binding lectin from eggs of the Echinometra lucunter: Amino
RT   acid sequence and molecular modeling.";
RL   Int. J. Biol. Macromol. 78:180-188(2015).
RN   [2]
RP   SEQUENCE REVISION.
RA   Carneiro R.;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- FUNCTION: Rhamnose-binding lectin. Also binds alpha-D-melibiose, alpha-
CC       D-lactose, beta-D-lactose, methyl-alpha-D-galactopyranoside, methyl-
CC       beta-D--galactopyranoside and D-galactose but not D-arabinose, L-
CC       fucose, D-glucose, D-mannose, D-maltose, D-sucrose, N-acetyl-D-
CC       galactosamine, N-acetyl-D-glucosamine, N-acetyl-D-mannosamine-D-xylose
CC       or by glycoproteins orosomucoid, thyroglobulin, ovomucoid and porcine
CC       stomach mucin. Shows cation-independent hemagglutinating activity
CC       against rabbit and human erythrocytes. Agglutinates cells of Gram-
CC       positive bacterial species S.aureus but not those of Gram-negative
CC       E.coli. {ECO:0000269|PubMed:25881955}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Activity is stable between pH 4 and 7 but decreases at basic pH.
CC         {ECO:0000269|PubMed:25881955};
CC       Temperature dependence:
CC         Activity is stable up to 60 degrees Celsius, then decreases and is
CC         lost at 100 degrees Celsius. {ECO:0000269|PubMed:25881955};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:25881955}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:25881955}.
CC   -!- MASS SPECTROMETRY: Mass=22091; Mass_error=2; Method=Electrospray;
CC       Note=Homodimer.; Evidence={ECO:0000269|PubMed:25881955};
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DR   AlphaFoldDB; C0HK24; -.
DR   SMR; C0HK24; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.740; -; 1.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   Pfam; PF02140; Gal_Lectin; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemagglutinin; Lectin.
FT   CHAIN           1..103
FT                   /note="L-rhamnose-binding lectin ELEL-1"
FT                   /evidence="ECO:0000269|PubMed:25881955, ECO:0000269|Ref.2"
FT                   /id="PRO_0000437082"
FT   DOMAIN          13..102
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   DISULFID        7
FT                   /note="Interchain"
FT                   /evidence="ECO:0000303|PubMed:25881955"
FT   DISULFID        14..45
FT                   /evidence="ECO:0000250|UniProtKB:C0HK23"
FT   DISULFID        23..101
FT                   /evidence="ECO:0000250|UniProtKB:C0HK23"
FT   DISULFID        56..88
FT                   /evidence="ECO:0000303|PubMed:25881955"
FT   DISULFID        69..75
FT                   /evidence="ECO:0000250|UniProtKB:C0HK23"
SQ   SEQUENCE   103 AA;  11075 MW;  DB8358C65848C44D CRC64;
     ELVSQLCLKK ERVCEGSSLT ISCPQKGAGI SIARAIYGRT KTQVCPSDGA TSNVNCKASN
     ALNVVRDLCR GKSSCTVEAS NDVFGDPCMH TYKYLELSYD CSK