ID   LEC3_MEGRO              Reviewed;         162 AA.
AC   P07439;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Lectin BRA-3;
DE   Flags: Precursor;
OS   Megabalanus rosa (Acorn barnacle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Cirripedia; Thoracica; Thoracicalcarea; Balanomorpha; Balanoidea;
OC   Balanidae; Megabalaninae; Megabalanus.
OX   NCBI_TaxID=6680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8514190; DOI=10.1016/0378-1119(93)90570-s;
RA   Takamatsu N., Takeda T., Kojima M., Heishi M., Muramoto K., Kamiya H.,
RA   Shiba T.;
RT   "Acorn barnacle Megabalanus rosa lectin (BRA-3): cDNA cloning, gene
RT   structure and seasonal changes of mRNA and protein levels.";
RL   Gene 128:251-255(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-162.
RA   Muramoto K., Kamiya H.;
RT   "The amino-acid sequence of a lectin of the acorn barnacle Megabalanus
RT   rosa.";
RL   Biochim. Biophys. Acta 874:285-295(1986).
CC   -!- FUNCTION: Sugar-binding protein which recognizes specific carbohydrate
CC       structures and agglutinates a variety of animal cells by binding to
CC       cell-surface glycoproteins and glycolipids. Calcium-dependent lectin.
CC       Invertebrate lectins may be involved in defense functions.
CC   -!- SUBUNIT: Homotetramer; disulfide-linked.
CC   -!- TISSUE SPECIFICITY: Coelemic fluid.
CC   -!- MISCELLANEOUS: This lectin binds galactose.
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DR   EMBL; D13302; BAA02556.1; -; Genomic_DNA.
DR   AlphaFoldDB; P07439; -.
DR   SMR; P07439; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Lectin; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           25..162
FT                   /note="Lectin BRA-3"
FT                   /id="PRO_0000017395"
FT   DOMAIN          25..152
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        26..39
FT   DISULFID        56..150
FT   DISULFID        125..142
FT   DISULFID        157
FT                   /note="Interchain (with C-160)"
FT   DISULFID        160
FT                   /note="Interchain (with C-157)"
FT   VARIANT         146
FT                   /note="K -> R"
SQ   SEQUENCE   162 AA;  18328 MW;  EB7F14E91DD1CB81 CRC64;
     MQRSEIVQAV TLLVVVFAIT TAECTCPGNL DWQEYDGHCY WASTYQVRWN DAQLACQTVH
     PGAYLATIQS QLENAFISET VSNNRLWIGL NDIDLEGHYV WSNGEATDFT YWSSNNPNNW
     ENQDCGVVNY DTVTGQWDDD DCNKNKNFLC KMPIIGCPPC GI