ID A0A1U7RPV5_ALLSI Unreviewed; 147 AA.
AC A0A1U7RPV5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Sperm acrosome membrane-associated protein 3 {ECO:0000256|ARBA:ARBA00016370};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
GN Name=LOC102387181 {ECO:0000313|RefSeq:XP_006023845.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006023845.1};
RN [1] {ECO:0000313|RefSeq:XP_006023845.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000256|ARBA:ARBA00000632};
CC -!- SUBUNIT: Interacts with ASTL. {ECO:0000256|ARBA:ARBA00011780}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000256|RuleBase:RU004440}.
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DR RefSeq; XP_006023845.1; XM_006023783.2.
DR AlphaFoldDB; A0A1U7RPV5; -.
DR STRING; 38654.A0A1U7RPV5; -.
DR GeneID; 102387181; -.
DR KEGG; asn:102387181; -.
DR eggNOG; ENOG502S1F5; Eukaryota.
DR InParanoid; A0A1U7RPV5; -.
DR OrthoDB; 5344399at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..147
FT /note="Sperm acrosome membrane-associated protein 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010528048"
FT DOMAIN 94..112
FT /note="Glycosyl hydrolases family 22 (GH22)"
FT /evidence="ECO:0000259|PROSITE:PS00128"
SQ SEQUENCE 147 AA; 16567 MW; A34A040CFC4A6A3D CRC64;
MKALALLPLF GCLIMSNEAK VFSRCELAYK LQEAGMDGYE GYSLANWICM AFFESGFNTA
AEDDNADGST DYGIFQINSR VWCNNHRSPT ENLCYMPCTD LLSSDITDDI ICAKRIVKDP
KGMDAWEDWT MHCKGRDLSE WVDGCDL
//
