ID   ELYS_HALCO              Reviewed;         155 AA.
AC   P19448;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Egg-lysin;
DE   AltName: Full=Sperm-lysin;
DE   Flags: Precursor;
OS   Haliotis corrugata (Pink abalone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX   NCBI_TaxID=6453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=2377618; DOI=10.1073/pnas.87.15.5792;
RA   Vacquier V.D., Carner K.R., Stout C.D.;
RT   "Species-specific sequences of abalone lysin, the sperm protein that
RT   creates a hole in the egg envelope.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5792-5796(1990).
RN   [2]
RP   FUNCTION, INTERACTION WITH VERL, AND TISSUE SPECIFICITY.
RX   PubMed=9192632; DOI=10.1073/pnas.94.13.6724;
RA   Swanson W.J., Vacquier V.D.;
RT   "The abalone egg vitelline envelope receptor for sperm lysin is a giant
RT   multivalent molecule.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:6724-6729(1997).
CC   -!- FUNCTION: Creates a 3 um hole in the egg vitelline layer through which
CC       the sperm passes (PubMed:2377618). Does not have enzyme activity.
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 (By similarity).
CC       Plays a role in ensuring species-specific fertilization
CC       (PubMed:2377618, PubMed:9192632). {ECO:0000250|UniProtKB:P04552,
CC       ECO:0000269|PubMed:2377618, ECO:0000269|PubMed:9192632}.
CC   -!- SUBUNIT: Monomer. Homodimer. Molecules associate into dimers and then
CC       rapidly dissociate again (By similarity). Interacts (as a monomer) with
CC       the egg vitelline layer protein VERL (via VERL repeats); each VERL
CC       chain can bind multiple copies of lysin (PubMed:2377618,
CC       PubMed:9192632). {ECO:0000250|UniProtKB:P04552,
CC       ECO:0000269|PubMed:2377618, ECO:0000269|PubMed:9192632}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       lumen {ECO:0000250|UniProtKB:P04552}.
CC   -!- TISSUE SPECIFICITY: Sperm (at protein level).
CC       {ECO:0000269|PubMed:2377618, ECO:0000269|PubMed:9192632}.
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DR   EMBL; M34389; AAA29197.1; -; mRNA.
DR   PIR; B35960; B35960.
DR   AlphaFoldDB; P19448; -.
DR   SMR; P19448; -.
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   Cytoplasmic vesicle; Fertilization; Signal.
FT   SIGNAL          1..18
FT   CHAIN           19..155
FT                   /note="Egg-lysin"
FT                   /id="PRO_0000021166"
SQ   SEQUENCE   155 AA;  18442 MW;  AB30787F88471213 CRC64;
     MKLLVLCLFA MMATLAVSRH RFRFIPHKYI RKEFEVALKV EIIAGFDRTL VKWLRVHGGR
     LSTVQKKALY FVNRRYMQTH WQNYMLWIVR KTDALGRPPV VADYSRLGAE IGRRIDMAYF
     YNFLNGRNMI PKYLPYMEEI NRMRPADVPV ANRGK