ID L5LV94_MYODS Unreviewed; 163 AA.
AC L5LV94;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Sperm acrosome membrane-associated protein 3 {ECO:0000256|ARBA:ARBA00016370};
GN ORFNames=MDA_GLEAN10014399 {ECO:0000313|EMBL:ELK29986.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK29986.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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. {ECO:0000256|ARBA:ARBA00024656}.
CC -!- SUBUNIT: Interacts with ASTL. {ECO:0000256|ARBA:ARBA00011780}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000256|RuleBase:RU004440}.
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DR EMBL; KB107558; ELK29986.1; -; Genomic_DNA.
DR RefSeq; XP_006764121.1; XM_006764058.1.
DR AlphaFoldDB; L5LV94; -.
DR GeneID; 102759668; -.
DR KEGG; myd:102759668; -.
DR CTD; 124912; -.
DR eggNOG; ENOG502S1F5; Eukaryota.
DR OrthoDB; 5344399at2759; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
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; IPR019799; Glyco_hydro_22_CS.
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; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..163
FT /note="Sperm acrosome membrane-associated protein 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003970650"
FT DOMAIN 110..128
FT /note="Glycosyl hydrolases family 22 (GH22)"
FT /evidence="ECO:0000259|PROSITE:PS00128"
SQ SEQUENCE 163 AA; 18252 MW; BE865C4A86796222 CRC64;
MEARGWAPRR QLCPPGILLL AVASLLSCLL TCSQAKVYSR CELFRVLQDF GLEGYRGHSL
ADWLCLAYYT SGFDSAAVDH EADGSTNNGI FQINSRKWCK TLREYSTKGC NMYCTELLDP
DLKNAVICAM KISQQPQGLG SWEAWKHHCL GKDLSDWVDG CTF
//