ID   BIND_LYTVA              Reviewed;         462 AA.
AC   P23117;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Bindin;
DE   Flags: Precursor;
OS   Lytechinus variegatus (Green sea urchin) (Echinus variegatus).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Temnopleuroida; Toxopneustidae; Lytechinus.
OX   NCBI_TaxID=7654;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1775065; DOI=10.1093/oxfordjournals.molbev.a040690;
RA   Minor J.E., Fromson D.R., Britten R.J., Davidson E.H.;
RT   "Comparison of the bindin proteins of Strongylocentrotus franciscanus, S.
RT   purpuratus, and Lytechinus variegatus: sequences involved in the species
RT   specificity of fertilization.";
RL   Mol. Biol. Evol. 8:781-795(1991).
CC   -!- FUNCTION: Species-specific sea urchin sperm protein required for
CC       adhesion of sperm to the egg surface during fertilization. Bindin coats
CC       the acrosomal process after it is externalized by the acrosome
CC       reaction. It binds to sulfated, fucose-containing polysaccharides on
CC       the vitelline layer receptor proteoglycans which cover the egg plasma
CC       membrane.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       lumen.
CC   -!- SIMILARITY: Belongs to the bindin family. {ECO:0000305}.
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DR   EMBL; M59489; AAA29997.1; -; mRNA.
DR   PIR; A40552; A40552.
DR   AlphaFoldDB; P23117; -.
DR   GO; GO:0043160; C:acrosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IEA:InterPro.
DR   InterPro; IPR000775; Bindin.
DR   Pfam; PF02084; Bindin; 1.
DR   PRINTS; PR00761; BINDIN.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW   Fertilization; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..244
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000020811"
FT   CHAIN           245..462
FT                   /note="Bindin"
FT                   /id="PRO_0000020812"
FT   REGION          155..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..380
FT                   /note="Fucose-binding domain"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        223..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   462 AA;  49987 MW;  3D41586156600B18 CRC64;
     MARQLSVILV ALTLTTALAE NFPTRTSAPS DCPQADQGCW CHKNFAQCWS TYDDSRLTEE
     IGSRITRLEL LYQPNEEVVT YIRRMSALRE IRISEDGMSL DCSCDLVDAM DDKGITLVNQ
     DELEIRNCRQ QGWSRDTMTA RPFLIECRRF RIQDDDRRKR RDAEQDSDDV TKRASPRKGD
     KPAGHKLKDL APKDTHHLVS IDDVEKHPAT DFFNFISGHR RTRRSTGTNE EVSDDSGRSA
     RKKRYGNMNY PQPMNQPMGG GNYPGQPPQQ NYAPQGMGGP VGGGGMGGAV GAGAMGGPVG
     GGGGGMGGPV GGANGIGESV EDEMSVDSDY SSLGGETTIS AKVIQDIKNL LGATKIDLPV
     DINDPYYLGL LLRHLRHHSN LLANIGDPEV REQVLSAMQE EEEEEENDAA NGVRENVLNN
     LNAPGQGGYG GTQGGMRGGA GGGMMGNQGM GGQGYNQGYM QG