ID   BIND_ARBPU              Reviewed;         480 AA.
AC   P24608;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Bindin;
DE   Flags: Precursor;
OS   Arbacia punctulata (Punctuate sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Arbacioida; Arbaciidae; Arbacia.
OX   NCBI_TaxID=7641;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=1991551; DOI=10.1016/0012-1606(91)90078-h;
RA   Glabe C.G., Clark D.;
RT   "The sequence of the Arbacia punctulata bindin cDNA and implications for
RT   the structural basis of species-specific sperm adhesion and
RT   fertilization.";
RL   Dev. Biol. 143:282-288(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       membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: A.punctulata bindin forms multilamellar structures
CC       reminiscent of lipid bilayers.
CC   -!- SIMILARITY: Belongs to the bindin family. {ECO:0000305}.
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DR   EMBL; X54155; CAA38094.1; -; mRNA.
DR   PIR; S14394; S14394.
DR   AlphaFoldDB; P24608; -.
DR   GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..247
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000020809"
FT   CHAIN           248..480
FT                   /note="Bindin"
FT                   /id="PRO_0000020810"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          161..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..385
FT                   /note="Fucose-binding domain"
FT                   /evidence="ECO:0000255"
FT   REGION          452..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  51567 MW;  5AF100604860E1AB CRC64;
     MDSQVLPLIL LIIVFAASSA HGHFPHRTNQ DSDCPEASNG CWCHDSFAQC WKTYEVANIA
     RKKDVIRKLE LLSLQLEDVL KYIAQLPNLE AIKLGPEGDD HLFECSCDNV LELSGSVVSV
     VNANDVHVTG CLEHGWSRDI YTMNAFATRC RRRLILESGG AEMRHRRSAK DDDVNKRASP
     RKGSSPAGKK VQIMEQDAGK GDAHNEKEVV KDQKPTKELF DFFMGHRRKR RSIDDVIGEM
     RAERQRRYAQ GAGGMQGGYG YPQAGGAQYG GQPVQGYMNQ GPPMGQRPAA AGPAGGFGAP
     QGQPPVGQPI GEAAGGGEFL GEPGVGGESE FAEYSSSIGE GETINAEVME KIKAVLGATK
     IDLPVDINDP YDLGLLLRHL RHHSNLLANI GDPEVRNQVL TAMQEEEEEE EQDAANGVRD
     NVLNNLNEGP GAGAVAGAAM AAGMPPYPGG AQGGMRVGGQ PQNPMGGNAY NPMTGYRQQG