ID   LECE_HELCR              Reviewed;         147 AA.
AC   P06027;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Echinoidin;
OS   Heliocidaris crassispina (Sea urchin) (Anthocidaris crassispina).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinometridae;
OC   Heliocidaris.
OX   NCBI_TaxID=1043166;
RN   [1]
RP   PROTEIN SEQUENCE, AND GLYCOSYLATION AT SER-38.
RX   PubMed=3571253; DOI=10.1016/s0021-9258(18)45556-1;
RA   Giga Y., Ikai A., Takahashi K.;
RT   "The complete amino acid sequence of echinoidin, a lectin from the coelomic
RT   fluid of the sea urchin Anthocidaris crassispina. Homologies with mammalian
RT   and insect lectins.";
RL   J. Biol. Chem. 262:6197-6203(1987).
CC   -!- FUNCTION: Role in the defense system of the organism against
CC       microorganisms. This lectin is specific for Gal-GalNAc.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Coelemic fluid.
CC   -!- PTM: The identity of the saccharide is not reported in PubMed:3571253,
CC       and it is unlikely to be N-acetylgalactosamine. The sugar attached to
CC       Ser-38 is represented simply as Hex.
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DR   PIR; A26697; A26697.
DR   AlphaFoldDB; P06027; -.
DR   SMR; P06027; -.
DR   iPTMnet; P06027; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd03589; CLECT_CEL-1_like; 1.
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; IPR033988; CEL1-like_CTLD.
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   Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin; Secreted.
FT   CHAIN           1..147
FT                   /note="Echinoidin"
FT                   /id="PRO_0000046641"
FT   DOMAIN          1..143
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   MOTIF           39..41
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        38
FT                   /note="O-linked (Hex) serine"
FT                   /evidence="ECO:0000269|PubMed:3571253"
FT   DISULFID        2
FT                   /note="Interchain"
FT   DISULFID        3..14
FT   DISULFID        31..141
FT   DISULFID        116..132
SQ   SEQUENCE   147 AA;  16661 MW;  849E98645481A062 CRC64;
     GCCPTFWTSF GSNCYRFFAV SLTWAEGEQF CQSFSVPSRG DIDSIGHLVS IHSETEQNFV
     YHYFETSTKD DTTPEMWLGF NDRTTEGNFQ WTDGSPNDFT AWVGSNPDNY GSGEDCTQMV
     MGAGLNWIDL PCSSTRHYLI CKLPLWE