ID   BIND_STRPU              Reviewed;         481 AA.
AC   P06651;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Bindin;
DE   Flags: Precursor;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3464974; DOI=10.1073/pnas.83.22.8634;
RA   Gao B., Klein L.E., Britten R.J., Davidson E.H.;
RT   "Sequence of mRNA coding for bindin, a species-specific sea urchin sperm
RT   protein required for fertilization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:8634-8638(1986).
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; M14487; AAA30038.1; -; mRNA.
DR   PIR; A26483; A26483.
DR   RefSeq; NP_999683.1; NM_214518.1.
DR   AlphaFoldDB; P06651; -.
DR   EnsemblMetazoa; NM_214518; NP_999683; GeneID_373276.
DR   GeneID; 373276; -.
DR   KEGG; spu:373276; -.
DR   CTD; 373276; -.
DR   eggNOG; ENOG502SXKB; Eukaryota.
DR   HOGENOM; CLU_255139_0_0_1; -.
DR   OMA; CPEADQG; -.
DR   OrthoDB; 1916491at2759; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
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; Reference proteome; Signal.
FT   SIGNAL          1..20
FT   PROPEP          21..245
FT                   /id="PRO_0000020815"
FT   CHAIN           246..481
FT                   /note="Bindin"
FT                   /id="PRO_0000020816"
FT   REGION          154..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..360
FT                   /note="Fucose-binding domain"
FT                   /evidence="ECO:0000255"
FT   REGION          376..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  51200 MW;  D5BFD44A9113CA8A CRC64;
     MGFHQILVTV VALALASVRA EFPSRTDSPT DCPEADQGCW CRGSFAQCWR TYEEAGMTGE
     IGNRITKLDL LYQPSEEIVT YIRRSSAMRE LRISEDGVSL DCSCDLIYAL DDKHVTLVDQ
     AELTFSNCQQ RGWPRDSMTA RSFVNRCHVS RMQDGDLRKR RESEDVDDDD VSKRASPRKG
     DEPAGHTLKD LAPQNTNHLV SIDGADKHPA DELVNFISGH SPTRRATDND AAVSDDSKRG
     ARKKRYVNTM GYPQAMSPQM GGVNYGQPAQ QGYGAQGMGG PVGGGPMGGP PQFGALPPGQ
     ADTDFGSSSS SVDGGDTTIS ARVMDDIKAV LGATKIDLPV DINDPYDLGL LLRHLRHHSN
     LLANIGDPAV REQVLSAMQE EEEEEEEDAA TGAQQGVLNG NAPGQAGFGG GGGGGAMMSP
     QQMGGQPQGM IGQPQGMGFP HEGMGGPPQG MGMPHQGMGG PPQGMGMPPQ GQPYGQGYLQ
     G