ID   ELYS_HALFU              Reviewed;         154 AA.
AC   Q01381;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Egg-lysin;
DE   AltName: Full=Sperm-lysin;
DE   Flags: Precursor;
OS   Haliotis fulgens (Green abalone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX   NCBI_TaxID=6456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lee Y.H., Vacquier V.D.;
RT   "The divergence of species-specific abalone sperm lysins is promoted by
RT   positive Darwinian selection.";
RL   Biol. Bull. 182:97-104(1992).
RN   [2] {ECO:0007744|PDB:3LYN}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 19-154, SUBUNIT, AND FUNCTION.
RX   PubMed=10698629; DOI=10.1006/jmbi.2000.3533;
RA   Kresge N., Vacquier V.D., Stout C.D.;
RT   "The high resolution crystal structure of green abalone sperm lysin:
RT   implications for species-specific binding of the egg receptor.";
RL   J. Mol. Biol. 296:1225-1234(2000).
CC   -!- FUNCTION: Creates a 3 um hole in the egg vitelline layer through which
CC       the sperm passes. Does not have enzyme activity (By similarity).
CC       Species-specific interaction between the sperm protein lysin and the
CC       egg protein VERL exposes a basic surface on lysin that may dissociate
CC       the egg vitelline layer via electrostatic repulsion. Plays a role in
CC       ensuring species-specific fertilization (PubMed:10698629).
CC       {ECO:0000250|UniProtKB:P04552, ECO:0000269|PubMed:10698629}.
CC   -!- SUBUNIT: Monomer (By similarity). Homodimer (PubMed:10698629).
CC       Molecules associate into dimers and then rapidly dissociate again.
CC       Interacts (as a monomer) with the egg vitelline layer protein VERL (via
CC       VERL repeats); each VERL chain can bind multiple copies of lysin (By
CC       similarity). {ECO:0000250|UniProtKB:P04552,
CC       ECO:0000269|PubMed:10698629}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       lumen {ECO:0000250|UniProtKB:P04552}.
CC   -!- TISSUE SPECIFICITY: Sperm.
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DR   EMBL; M59972; AAA29202.1; -; mRNA.
DR   PDB; 3LYN; X-ray; 1.70 A; A/B=19-154.
DR   PDBsum; 3LYN; -.
DR   AlphaFoldDB; Q01381; -.
DR   SMR; Q01381; -.
DR   EvolutionaryTrace; Q01381; -.
DR   GO; GO:0043160; C:acrosomal lumen; ISS:UniProtKB.
DR   GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
DR   CDD; cd00243; Lysin-Sp18; 1.
DR   Gene3D; 1.20.150.10; -; 1.
DR   InterPro; IPR001379; Egg_lysin.
DR   InterPro; IPR035916; Fertil_protein_sf.
DR   Pfam; PF01303; Egg_lysin; 1.
DR   PRINTS; PR01882; LYSIN.
DR   SUPFAM; SSF47082; SSF47082; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasmic vesicle; Fertilization; Signal.
FT   SIGNAL          1..18
FT   CHAIN           19..154
FT                   /note="Egg-lysin"
FT                   /id="PRO_0000021168"
FT   HELIX           30..56
FT                   /evidence="ECO:0007829|PDB:3LYN"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:3LYN"
FT   HELIX           62..92
FT                   /evidence="ECO:0007829|PDB:3LYN"
FT   HELIX           100..113
FT                   /evidence="ECO:0007829|PDB:3LYN"
FT   HELIX           116..125
FT                   /evidence="ECO:0007829|PDB:3LYN"
FT   HELIX           134..140
FT                   /evidence="ECO:0007829|PDB:3LYN"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:3LYN"
SQ   SEQUENCE   154 AA;  18340 MW;  69872E2B50AEBEBC CRC64;
     MKLLVLWVFA MMATVAMSRR WTFVRYHYIN KAYEVTMKIQ IISGFDRQLT AWLRVHGRRL
     TNNQKKTLFF VNRRYMQTHW QNYMLWVKRK IKALGRPAAV GDYTRLGAEI GRRVDMVFFY
     NFLSGRKMIP PYSAYMAKLN ALRPADVPVK NHGK