ID   SACA3_PAPHA             Reviewed;         166 AA.
AC   B6VH79;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 31.
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   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
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; FJ396445; ACJ06640.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6VH79; -.
DR   SMR; B6VH79; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
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:0003796; F:lysozyme activity; IEA:InterPro.
DR   GO; GO:0009566; P:fertilization; IEA:InterPro.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR030058; LYZL3.
DR   PANTHER; PTHR11407; PTHR11407; 1.
DR   PANTHER; PTHR11407:SF25; PTHR11407:SF25; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; SSF53955; 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..>166
FT                   /note="Sperm acrosome membrane-associated protein 3,
FT                   membrane form"
FT                   /id="PRO_0000375082"
FT   CHAIN           87..>166
FT                   /note="Sperm acrosome membrane-associated protein 3,
FT                   processed form"
FT                   /id="PRO_0000375083"
FT   TOPO_DOM        1..62
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..>166
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          87..>166
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   REGION          16..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            86..87
FT                   /note="Cleavage; to produce processed form"
FT                   /evidence="ECO:0000250"
FT   DISULFID        150..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   NON_TER         166
SQ   SEQUENCE   166 AA;  17714 MW;  C69F0D75899CDA7E CRC64;
     MISALWGALL IRVHSSPVSS PSVSGPPRLV SCGSSQSSAL SQSGGSTSTT GTEARSRALG
     RRWCPAAIML LALVSLLSCL LPSSEAKVYS RCELARVLQD FGLDGYRGYS LADWVCLAYF
     TSGFNAAALD YEADGSTNNG IFQINSRRWC SNLTPNVPNV CRMYCS