ID Q3ZB05_MOUSE Unreviewed; 380 AA.
AC Q3ZB05;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 22-FEB-2023, entry version 101.
DE RecName: Full=Acrosin {ECO:0000256|ARBA:ARBA00017161, ECO:0000256|PIRNR:PIRNR001141};
DE EC=3.4.21.10 {ECO:0000256|ARBA:ARBA00012050, ECO:0000256|PIRNR:PIRNR001141};
GN Name=Acr {ECO:0000313|EMBL:AAI03580.1, ECO:0000313|MGI:MGI:87884};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAI03580.1};
RN [1] {ECO:0000313|EMBL:AAI03580.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PCR rescued clones {ECO:0000313|EMBL:AAI03580.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acrosin is the major protease of mammalian spermatozoa. It is
CC a serine protease of trypsin-like cleavage specificity, it is
CC synthesized in a zymogen form, proacrosin and stored in the acrosome.
CC {ECO:0000256|ARBA:ARBA00003042, ECO:0000256|PIRNR:PIRNR001141}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.10;
CC Evidence={ECO:0000256|ARBA:ARBA00001656,
CC ECO:0000256|PIRNR:PIRNR001141};
CC -!- SUBUNIT: Heavy chain (catalytic) and a light chain linked by two
CC disulfide bonds. Forms a heterodimer with SERPINA5.
CC {ECO:0000256|ARBA:ARBA00025832}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|PIRNR:PIRNR001141}.
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DR EMBL; BC103579; AAI03580.1; -; mRNA.
DR RefSeq; NP_001264174.1; NM_001277245.1.
DR RefSeq; NP_001264175.1; NM_001277246.1.
DR AlphaFoldDB; Q3ZB05; -.
DR MEROPS; S01.223; -.
DR DNASU; 11434; -.
DR GeneID; 11434; -.
DR UCSC; uc033gwi.1; mouse.
DR AGR; MGI:87884; -.
DR CTD; 49; -.
DR MGI; MGI:87884; Acr.
DR OrthoDB; 4629979at2759; -.
DR BRENDA; 3.4.21.10; 3474.
DR BioGRID-ORCS; 11434; 2 hits in 78 CRISPR screens.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR012267; Pept_S1A_acrosin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001141; Acrosin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001141, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|PIRNR:PIRNR001141, ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|PIRNR:PIRNR001141,
KW ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 1..235
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 33
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-1"
FT ACT_SITE 87
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-1"
FT ACT_SITE 185
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-1"
SQ SEQUENCE 380 AA; 43016 MW; 90D58E433BADEB76 CRC64;
MVSLQIFTSH NSRRYHACGG SLLNSHWVLT AAHCFDNKKK VYDWRLVFGA QEIEYGRNKP
VKEPQQERYV QKIVIHEKYN VVTEGNDIAL LKITPPVTCG NFIGPCCLPH FKAGPPQIPH
TCYVTGWGYI KEKAPRPSPV LMEARVDLID LDLCNSTQWY NGRVTSTNVC AGYPEGKIDT
CQGDSGGPLM CRDNVDSPFV VVGITSWGVG CARAKRPGVY TATWDYLDWI ASKIGPNALH
LIQPATPHPP TTRHPMVSFH PPSLRPPWYF QHLPSRPLYL RPLRPLLHRP SSTQTSSSLM
PLLSPPTPAQ PASFTIATQH MRHRTTLSFA RRLQRLIEAL KMRTYPMKHP SQYSGPRNYH
YRFSTFEPLS NKPSEPFLHS
//
