ID   BIND_MESFR              Reviewed;         485 AA.
AC   P23118;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Bindin;
DE   Flags: Precursor;
OS   Mesocentrotus franciscanus (Giant red sea urchin) (Strongylocentrotus
OS   franciscanus).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Mesocentrotus.
OX   NCBI_TaxID=1328066;
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).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE OF 248-320.
RA   Vacquier V.D., Moy G.W.;
RL   (In) Dirksen E.R., Prescott D., Fox C.F. (eds.);
RL   Cell reproduction, pp.12:379-389, Academic Press, New York (1978).
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; M59490; AAA30037.1; -; mRNA.
DR   PIR; B40552; B40552.
DR   AlphaFoldDB; P23118; -.
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   1: Evidence at protein level;
KW   Cell adhesion; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW   Direct protein sequencing; Fertilization; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..247
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000020813"
FT   CHAIN           248..485
FT                   /note="Bindin"
FT                   /id="PRO_0000020814"
FT   REGION          157..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..379
FT                   /note="Fucose-binding domain"
FT                   /evidence="ECO:0000255"
FT   REGION          459..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  51940 MW;  DB4577EFF55260F8 CRC64;
     MGFHQISVII VVLALASARA ADEFPSHTDT PTDCPEADHG CWCHGSFAQC WRTYEDSRMT
     EEIGNRITQL ELLYQPSEEV VTYIRRISAL RELRISEDGM SLDCSCDVIY ALDDKQVTLV
     NQAELTFGNC RERGWPRERM AARPFVHRCH VLRMQDGETR KRRGADDNDG DDVSKRASPR
     KGDEPAGHKL KDLAPQNTHH LVNIHDADKH PASEFVNFIS GHRRSRRSTD DDAAVSDDSE
     RGARKKRYGN QGNYPQAMNP QSRGVNYGQP AQQGYGAQGM GGAFGGGQGM GGAVRGGQGM
     GGAVGGGQFG AFSPGEAEAD NADYDEYSDS LDEGDTTISA AVMDDIKAVL GATKIDLPVD
     INDPYDLGLL LRHLRHHSNL LANIGDPAVR EQVLSAMQEE EEEEEEDAAN GVRQNVLNNI
     NANAPGNAGY GGQGGMGAFG GGGGGMGAIG GGGGAMMGQQ GMGGVPQRMG GQPQGNAYNQ
     GYRQG