ID   CLC35_PETMA             Reviewed;          17 AA.
AC   Q9PRY2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   11-DEC-2019, entry version 24.
DE   RecName: Full=C-type lectin 35 kDa subunit {ECO:0000303|PubMed:18937980};
DE   AltName: Full=C-type lectin 30 kDa subunit {ECO:0000303|PubMed:8192354};
DE   Flags: Fragment;
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-11, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Plasma {ECO:0000269|PubMed:18937980};
RX   PubMed=18937980; DOI=10.1016/j.vetimm.2008.08.008;
RA   Ourth D.D., Rose W.M., Siefkes M.J.;
RT   "Isolation of mannose-binding C-type lectin from sea lamprey (Petromyzon
RT   marinus) plasma and binding to Aeromonas salmonicida.";
RL   Vet. Immunol. Immunopathol. 126:407-412(2008).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-17, FUNCTION, AND SUBUNIT.
RC   TISSUE=Egg {ECO:0000269|PubMed:8192354};
RX   PubMed=8192354; DOI=10.1111/j.1749-6632.1994.tb33563.x;
RA   Schluter S.F., Schroeder J., Wang E., Marchalonis J.J.;
RT   "Recognition molecules and immunoglobulin domains in invertebrates.";
RL   Ann. N. Y. Acad. Sci. 712:74-81(1994).
CC   -!- FUNCTION: Calcium-dependent lectin involved in innate immune defense.
CC       Binds mannose residues on the surface of the Gram-negative bacterium
CC       A.salmonicida. Shows agglutinating activity towards horse erythrocytes.
CC       {ECO:0000269|PubMed:18937980, ECO:0000269|PubMed:8192354}.
CC   -!- SUBUNIT: Forms an oligomeric complex with the C-type lectin 65 kDa
CC       subunit. {ECO:0000269|PubMed:18937980, ECO:0000269|PubMed:8192354}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18937980}.
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DR   Proteomes; UP000245300; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR   GO; GO:0034120; P:positive regulation of erythrocyte aggregation; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hemagglutinin; Immunity;
KW   Innate immunity; Lectin; Mannose-binding; Reference proteome; Secreted.
FT   CHAIN           1..>17
FT                   /note="C-type lectin 35 kDa subunit"
FT                   /id="PRO_0000392631"
FT   NON_TER         17
FT                   /evidence="ECO:0000303|PubMed:8192354"
SQ   SEQUENCE   17 AA;  1839 MW;  5E0F83DD4185F446 CRC64;
     XWSCTKGCPD AKQCEAT