ID   LEC2_MEGRO              Reviewed;         173 AA.
AC   P17346;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Lectin BRA-2;
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   PROTEIN SEQUENCE.
RC   TISSUE=Coelomic fluid;
RX   PubMed=2354200; DOI=10.1016/0167-4838(90)90224-4;
RA   Muramoto K., Kamiya H.;
RT   "The amino-acid sequence of multiple lectins of the acorn barnacle
RT   Megabalanus rosa and its homology with animal lectins.";
RL   Biochim. Biophys. Acta 1039:42-51(1990).
RN   [2]
RP   DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-39.
RX   PubMed=2354201; DOI=10.1016/0167-4838(90)90225-5;
RA   Muramoto K., Kamiya H.;
RT   "The positions of the disulfide bonds and the glycosylation site in a
RT   lectin of the acorn barnacle Megabalanus rosa.";
RL   Biochim. Biophys. Acta 1039:52-60(1990).
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: Homohexamer; disulfide-linked. {ECO:0000269|PubMed:2354201}.
CC   -!- TISSUE SPECIFICITY: Coelemic fluid.
CC   -!- MISCELLANEOUS: This lectin binds galactose.
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DR   PIR; S10548; S10548.
DR   AlphaFoldDB; P17346; -.
DR   SMR; P17346; -.
DR   iPTMnet; P17346; -.
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; Glycoprotein; Lectin.
FT   CHAIN           1..173
FT                   /note="Lectin BRA-2"
FT                   /id="PRO_0000046647"
FT   DOMAIN          51..170
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:2354201"
FT   DISULFID        14
FT                   /note="Interchain (with C-50)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:2354201"
FT   DISULFID        47..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:2354201"
FT   DISULFID        50
FT                   /note="Interchain (with C-14)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:2354201"
FT   DISULFID        78..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:2354201"
FT   DISULFID        144..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:2354201"
SQ   SEQUENCE   173 AA;  19581 MW;  0D90DCA1F805D818 CRC64;
     YGVPEEPPPV PDTCGHVAEE RVTQAFAELT TKLSELQENV TNTFHGCNHC PNGWVTSENK
     CFHVPLEKAS WMVAHGVCAR LDSRARLASI DAADQAVVEP LSSEKMWIGL SYDSANDAAV
     WADDSHSSHR NWYATQPDDE SELCVLIKED QYRQWHDYNC NDRYNFVCEI VLH