ID   CSL3_ONCKE              Reviewed;         195 AA.
AC   P86179;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=L-rhamnose-binding lectin CSL3 {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, human type A erythrocytes, human type B
CC       erythrocytes, human type O erythrocytes and sheep erythrocytes.
CC       Hemagglutinating activity is inhibited by smooth-type
CC       lipopolysaccharide (LPS) from S.flexneri 1A, A.salmonicida and E.coli
CC       K12, but not by rough-type LPS from S.flexneri, E.coli K12 and E.coli
CC       EH100. 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};
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DR   PDB; 2ZX0; X-ray; 1.90 A; A/B=1-195.
DR   PDB; 2ZX1; X-ray; 1.90 A; A/B=1-195.
DR   PDB; 2ZX2; X-ray; 1.80 A; A/B=1-195.
DR   PDB; 2ZX3; X-ray; 2.10 A; A/B=1-195.
DR   PDB; 2ZX4; X-ray; 2.70 A; A/B=1-195.
DR   PDBsum; 2ZX0; -.
DR   PDBsum; 2ZX1; -.
DR   PDBsum; 2ZX2; -.
DR   PDBsum; 2ZX3; -.
DR   PDBsum; 2ZX4; -.
DR   AlphaFoldDB; P86179; -.
DR   SMR; P86179; -.
DR   UniLectin; P86179; -.
DR   EvolutionaryTrace; P86179; -.
DR   GO; GO:0060473; C:cortical granule; ISS:AgBase.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0001674; C:female germ cell nucleus; ISS:AgBase.
DR   GO; GO:0042564; C:NLS-dependent protein nuclear import complex; ISS:AgBase.
DR   GO; GO:0005534; F:galactose binding; ISS:AgBase.
DR   GO; GO:1903777; F:melibiose binding; ISS:AgBase.
DR   GO; GO:0042803; F:protein homodimerization activity; 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   3D-structure; Direct protein sequencing; Hemagglutinin; Lectin; Repeat.
FT   CHAIN           1..195
FT                   /note="L-rhamnose-binding lectin CSL3"
FT                   /id="PRO_0000366204"
FT   DOMAIN          1..95
FT                   /note="SUEL-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   DOMAIN          105..195
FT                   /note="SUEL-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   STRAND          9..14
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   STRAND          18..30
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   HELIX           54..62
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   STRAND          87..95
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   STRAND          109..114
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   STRAND          116..130
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   STRAND          132..135
FT                   /evidence="ECO:0007829|PDB:2ZX4"
FT   HELIX           141..143
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   HELIX           154..162
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   STRAND          166..171
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   HELIX           174..177
FT                   /evidence="ECO:0007829|PDB:2ZX2"
FT   STRAND          187..195
FT                   /evidence="ECO:0007829|PDB:2ZX2"
SQ   SEQUENCE   195 AA;  21476 MW;  9A206D0B4ECDCB47 CRC64;
     AISITCEGSD ALLQCDGAKI HIKRANYGRR QHDVCSIGRP DNQLTDTNCL SQSSTSKMAE
     RCGGKSECIV PASNFVFGDP CVGTYKYLDT KYSCVQQQET ISSIICEGSD SQLLCDRGEI
     RIQRANYGRR QHDVCSIGRP HQQLKNTNCL SQSTTSKMAE RCDGKRQCIV SVSNSVFGDP
     CVGTYKYLDV AYTCD