ELYS_HALRU
ID ELYS_HALRU Reviewed; 154 AA.
AC P04552;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Egg-lysin;
DE AltName: Full=Sperm-lysin;
DE Flags: Precursor;
OS Haliotis rufescens (California red abalone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX NCBI_TaxID=6454;
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 PROTEIN SEQUENCE OF 19-152, AND TISSUE SPECIFICITY.
RX PubMed=3894351; DOI=10.1016/s0021-9258(17)39334-1;
RA Fridberger A., Sundelin J., Vacquier V.D., Peterson P.A.;
RT "Amino acid sequence of an egg-lysin protein from abalone spermatozoa that
RT solubilizes the vitelline layer.";
RL J. Biol. Chem. 260:9092-9099(1985).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7106382; DOI=10.1016/0012-1606(82)90167-1;
RA Lewis C.A., Talbot C.F., Vacquier V.D.;
RT "A protein from abalone sperm dissolves the egg vitelline layer by a
RT nonenzymatic mechanism.";
RL Dev. Biol. 92:227-239(1982).
RN [4]
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 19-154.
RX PubMed=8266073; DOI=10.1126/science.8266073;
RA Shaw A., McRee D.E., Vacquier V.D., Stout C.D.;
RT "The crystal structure of lysin, a fertilization protein.";
RL Science 262:1864-1867(1993).
RN [6] {ECO:0007744|PDB:1LYN}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 19-154, AND SUBUNIT.
RX PubMed=7657696; DOI=10.1083/jcb.130.5.1117;
RA Shaw A., Fortes P.A., Stout C.D., Vacquier V.D.;
RT "Crystal structure and subunit dynamics of the abalone sperm lysin dimer:
RT egg envelopes dissociate dimers, the monomer is the active species.";
RL J. Cell Biol. 130:1117-1125(1995).
RN [7] {ECO:0007744|PDB:2LIS, ECO:0007744|PDB:2LYN}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 19-154, AND SUBUNIT.
RX PubMed=10666624; DOI=10.1107/s0907444999014626;
RA Kresge N., Vacquier V.D., Stout C.D.;
RT "1.35 and 2.07 A resolution structures of the red abalone sperm lysin
RT monomer and dimer reveal features involved in receptor binding.";
RL Acta Crystallogr. D 56:34-41(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 19-154 IN COMPLEXES WITH VERL,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF 78-THR-HIS-79; PHE-119; LYS-150 AND
RP TYR-151.
RX PubMed=28622512; DOI=10.1016/j.cell.2017.05.033;
RA Raj I., Sadat Al Hosseini H., Dioguardi E., Nishimura K., Han L., Villa A.,
RA de Sanctis D., Jovine L.;
RT "Structural basis of egg coat-sperm recognition at fertilization.";
RL Cell 169:1315-1326(2017).
CC -!- FUNCTION: Creates a 3 um hole in the egg vitelline layer through which
CC the sperm passes (PubMed:7106382). Does not have enzyme activity
CC (PubMed:7106382). Species-specific interaction between the sperm
CC protein lysin and the egg protein VERL exposes a basic surface on lysin
CC that may dissociate the egg vitelline layer via electrostatic repulsion
CC (PubMed:7106382, PubMed:28622512). Plays a role in ensuring species-
CC specific fertilization (PubMed:2377618, PubMed:9192632,
CC PubMed:28622512). {ECO:0000269|PubMed:2377618,
CC ECO:0000269|PubMed:28622512, ECO:0000269|PubMed:7106382,
CC ECO:0000269|PubMed:9192632}.
CC -!- SUBUNIT: Monomer (PubMed:7657696, PubMed:10666624). Homodimer
CC (PubMed:7657696, PubMed:10666624). Molecules associate into dimers and
CC then rapidly dissociate again (PubMed:7657696, PubMed:10666624).
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
CC (PubMed:9192632, PubMed:28622512). {ECO:0000269|PubMed:10666624,
CC ECO:0000269|PubMed:28622512, ECO:0000269|PubMed:7657696,
CC ECO:0000269|PubMed:9192632}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC lumen {ECO:0000269|PubMed:7106382}.
CC -!- TISSUE SPECIFICITY: Sperm (at protein level).
CC {ECO:0000269|PubMed:2377618, ECO:0000269|PubMed:3894351,
CC ECO:0000269|PubMed:7106382, ECO:0000269|PubMed:9192632}.
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DR EMBL; M34388; AAA29196.1; -; mRNA.
DR PIR; A35960; EYNKHR.
DR PDB; 1LIS; X-ray; 1.90 A; A=19-154.
DR PDB; 1LYN; X-ray; 2.75 A; A/B=19-154.
DR PDB; 2LIS; X-ray; 1.35 A; A=19-154.
DR PDB; 2LYN; X-ray; 2.07 A; A/B/C/D=19-154.
DR PDB; 5II7; X-ray; 1.66 A; A=19-154.
DR PDB; 5II8; X-ray; 0.99 A; A=19-154.
DR PDB; 5II9; X-ray; 2.11 A; A/B/C/D/E/F=19-154.
DR PDB; 5IIA; X-ray; 1.70 A; A/C/E/G=19-154.
DR PDB; 5IIB; X-ray; 1.64 A; A=19-154.
DR PDB; 5MR3; X-ray; 1.80 A; A/C/E/G=19-154.
DR PDB; 5UTG; NMR; -; A=19-152.
DR PDBsum; 1LIS; -.
DR PDBsum; 1LYN; -.
DR PDBsum; 2LIS; -.
DR PDBsum; 2LYN; -.
DR PDBsum; 5II7; -.
DR PDBsum; 5II8; -.
DR PDBsum; 5II9; -.
DR PDBsum; 5IIA; -.
DR PDBsum; 5IIB; -.
DR PDBsum; 5MR3; -.
DR PDBsum; 5UTG; -.
DR AlphaFoldDB; P04552; -.
DR BMRB; P04552; -.
DR SMR; P04552; -.
DR EvolutionaryTrace; P04552; -.
DR GO; GO:0043160; C:acrosomal lumen; IDA:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IDA: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; Direct protein sequencing;
KW Fertilization; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:3894351"
FT CHAIN 19..154
FT /note="Egg-lysin"
FT /id="PRO_0000021170"
FT MUTAGEN 78..79
FT /note="TH->AA: Nearly abolishes VERL binding."
FT /evidence="ECO:0000269|PubMed:28622512"
FT MUTAGEN 119
FT /note="F->S: Impaired VERL binding."
FT /evidence="ECO:0000269|PubMed:28622512"
FT MUTAGEN 150
FT /note="K->A: No effect on VERL binding. Impairs VERL
FT binding; when associated with N-151."
FT /evidence="ECO:0000269|PubMed:28622512"
FT MUTAGEN 151
FT /note="Y->N: Impairs VERL binding; when associated with A-
FT 150."
FT /evidence="ECO:0000269|PubMed:28622512"
FT CONFLICT 39..41
FT /note="VQI -> KQF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="L -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="E -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 31..56
FT /evidence="ECO:0007829|PDB:5II8"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5II8"
FT HELIX 62..92
FT /evidence="ECO:0007829|PDB:5II8"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2LIS"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:5II8"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:5II8"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:5II8"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5II8"
SQ SEQUENCE 154 AA; 18237 MW; 5E0E0D2BC4E8A32A CRC64;
MKLLVLCIFA MMATLAMSRS WHYVEPKFLN KAFEVALKVQ IIAGFDRGLV KWLRVHGRTL
STVQKKALYF VNRRYMQTHW ANYMLWINKK IDALGRTPVV GDYTRLGAEI GRRIDMAYFY
DFLKDKNMIP KYLPYMEEIN RMRPADVPVK YMGK
