ID SACA3_PONPY Reviewed; 167 AA.
AC B6VH77;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 22-FEB-2023, entry version 36.
DE RecName: Full=Sperm acrosome membrane-associated protein 3;
DE AltName: Full=Sperm protein reactive with antisperm antibodies;
DE Short=Sperm protein reactive with ASA;
DE Contains:
DE RecName: Full=Sperm acrosome membrane-associated protein 3, membrane form;
DE Contains:
DE RecName: Full=Sperm acrosome membrane-associated protein 3, processed form;
DE Flags: Fragment;
GN Name=SPACA3; Synonyms=SPRASA;
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Prendergast D., Woad K.J., Chamley L.W., Shelling A.N.;
RT "Evolutionary conservation of SPRASA in various animal species.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sperm surface membrane protein that may be involved in sperm-
CC egg plasma membrane adhesion and fusion during fertilization. It could
CC be a potential receptor for the egg oligosaccharide residue N-
CC acetylglucosamine, which is present in the extracellular matrix over
CC the egg plasma membrane. The processed form has no detectable
CC bacteriolytic activity in vitro (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ASTL. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC membrane {ECO:0000250}; Single-pass type II membrane protein
CC {ECO:0000250}. Note=Anterior acrosome in non-capacitated spermatozoa
CC and retained in the equatorial segment and in the luminal face of both
CC the inner and outer acrosomal membranes following capacitation and the
CC acrosome reaction. {ECO:0000250}.
CC -!- PTM: The processed form derives from the membrane form by proteolytic
CC processing. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 22 family, Thr-
CC 122 and Asn-139 are present instead of the conserved Glu and Asp which
CC are active site residues. It is therefore expected that this protein
CC lacks hydrolase activity. {ECO:0000305}.
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DR EMBL; FJ396444; ACJ06638.1; -; Genomic_DNA.
DR AlphaFoldDB; B6VH77; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR CDD; cd16897; LYZ_C; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR000974; Glyco_hydro_22_lys.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR11407; LYSOZYME C; 1.
DR PANTHER; PTHR11407:SF25; SPERM ACROSOME MEMBRANE-ASSOCIATED PROTEIN 3; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00137; LYSOZYME.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle; Disulfide bond; Membrane; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..>167
FT /note="Sperm acrosome membrane-associated protein 3,
FT membrane form"
FT /id="PRO_0000375084"
FT CHAIN 88..>167
FT /note="Sperm acrosome membrane-associated protein 3,
FT processed form"
FT /id="PRO_0000375085"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..>167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 88..>167
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT SITE 87..88
FT /note="Cleavage; to produce processed form"
FT /evidence="ECO:0000250"
FT DISULFID 151..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT NON_TER 167
SQ SEQUENCE 167 AA; 17899 MW; D83B8A5596E974BE CRC64;
MVSALREAPL IRVHSSPVSS PSVSGSRRPV SCLSSQSSAL SQSGGGSTSA AGIEARSRAL
RRRWCPAGII LLALISLLSC LLPASEAKVY GRCELARVLH DFGLDGYRGY SLADWVCLAY
FTSGFNTAAV DHEADGSTNN GIFQINSRRW CRNLTPNVPN VCQMYCS
//
