ID   CSL1_ONCKE              Reviewed;         286 AA.
AC   P86177;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=L-rhamnose-binding lectin CSL1 {ECO:0000303|Ref.1};
OS   Oncorhynchus keta (Chum salmon) (Salmo keta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8018;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Egg {ECO:0000269|Ref.1};
RA   Shiina N., Tateno H., Ogawa T., Muramoto K., Saneyoshi M., Kamiya H.;
RT   "Isolation and characterization of L-rhamnose-binding lectins from chum
RT   salmon (Oncorhynchus keta) eggs.";
RL   Fish. Sci. 68:1352-1366(2002).
CC   -!- FUNCTION: L-rhamnose binding lectin. Has hemagglutinating activity
CC       towards rabbit erythrocytes, but not human type B erythrocytes.
CC       Hemagglutinating activity is inhibited by smooth-type
CC       lipopolysaccharide (LPS) from K.pneumoniae, E.coli K-235, S.flexneri
CC       1A, A.salmonicida and S.minnesota and rough-type LPS from S.flexneri,
CC       but not by rough-type LPS from E.coli K12 and E.coli EH100.
CC       Agglutinates E.coli K12 and B.subtilis. {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Retains hemagglutinating activity after heating at 50 degrees Celsius
CC         for 120 minutes. Activity is abolished by heating at 80 degrees
CC         Celsius for 90 minutes. {ECO:0000269|Ref.1};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P86177; -.
DR   SMR; P86177; -.
DR   GO; GO:0060473; C:cortical granule; ISS:AgBase.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:AgBase.
DR   GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR   GO; GO:0042585; C:germinal vesicle; ISS:AgBase.
DR   GO; GO:0098595; C:perivitelline space; ISS:AgBase.
DR   GO; GO:0005534; F:galactose binding; ISS:AgBase.
DR   GO; GO:1903777; F:melibiose binding; ISS:AgBase.
DR   GO; GO:0033296; F:rhamnose binding; ISS:AgBase.
DR   Gene3D; 2.60.120.740; -; 2.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   Pfam; PF02140; Gal_Lectin; 2.
DR   PROSITE; PS50228; SUEL_LECTIN; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hemagglutinin; Lectin; Repeat.
FT   CHAIN           1..286
FT                   /note="L-rhamnose-binding lectin CSL1"
FT                   /id="PRO_0000366202"
FT   DOMAIN          96..186
FT                   /note="SUEL-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   DOMAIN          193..280
FT                   /note="SUEL-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
SQ   SEQUENCE   286 AA;  31124 MW;  FC9AB68028676D0E CRC64;
     EIQRRFLTCG DPSLQCDYGV IMVYGVQFST IELSSNERPK ACSDTEAKNG PSNRCDGNEK
     CDVATSGSVC DLCNSAYLTN IFLDVTYGCL ESKKVTTCEG VVHLECGDGV VFLQKALYGR
     IDSQTCSQGR PQSQLTNTKC SQEGTLALWS QRCDGKQTCE VNMRVNQISD PCVGTYKYLD
     VTYICLPAKT SITCEGSTSS LDCGKGVIKV FHANYGRRDG STCSAGRHEL SNQNCLQPKT
     LDVVKQWCEG KSQCTLGLDP VFGDPCFGTY KYLEVSYTCL GGSPTV