ID ACRO_MOUSE Reviewed; 436 AA.
AC P23578;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 24-JAN-2024, entry version 188.
DE RecName: Full=Acrosin;
DE EC=3.4.21.10;
DE Contains:
DE RecName: Full=Acrosin light chain;
DE Contains:
DE RecName: Full=Acrosin heavy chain;
DE Flags: Precursor;
GN Name=Acr;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2127931; DOI=10.1093/oxfordjournals.jbchem.a123281;
RA Kashiwabara S., Baba T., Takada M., Watanabe K., Yano Y., Arai Y.;
RT "Primary structure of mouse proacrosin deduced from the cDNA sequence and
RT its gene expression during spermatogenesis.";
RL J. Biochem. 108:785-791(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1939002; DOI=10.1093/oxfordjournals.jbchem.a123466;
RA Watanabe K., Baba T., Kashiwabara S., Okamoto A., Arai Y.;
RT "Structure and organization of the mouse acrosin gene.";
RL J. Biochem. 109:828-833(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2111255; DOI=10.1111/j.1432-0436.1990.tb00757.x;
RA Klemm U., Maier W.-M., Tsaousidou S., Adham I.M., Willison K., Engel W.;
RT "Mouse preproacrosin: cDNA sequence, primary structure and postmeiotic
RT expression in spermatogenesis.";
RL Differentiation 42:160-166(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1783391; DOI=10.1016/0888-7543(91)90005-y;
RA Kremling H., Keime S., Wilhelm K., Adham I.M., Hameister H., Engel W.;
RT "Mouse proacrosin gene: nucleotide sequence, diploid expression, and
RT chromosomal localization.";
RL Genomics 11:828-834(1991).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.10;
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC -!- SUBUNIT: Heavy chain (catalytic) and a light chain linked by two
CC disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40124.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA00651.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA36704.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D00754; BAA00651.1; ALT_INIT; mRNA.
DR EMBL; S66245; AAB20293.1; -; Genomic_DNA.
DR EMBL; S64500; AAB20293.1; JOINED; Genomic_DNA.
DR EMBL; S66243; AAB20293.1; JOINED; Genomic_DNA.
DR EMBL; X52466; CAA36704.1; ALT_INIT; mRNA.
DR EMBL; M85170; AAA40124.1; ALT_INIT; mRNA.
DR EMBL; M96430; AAA37163.1; -; Genomic_DNA.
DR EMBL; M96426; AAA37163.1; JOINED; Genomic_DNA.
DR EMBL; M96427; AAA37163.1; JOINED; Genomic_DNA.
DR EMBL; M96428; AAA37163.1; JOINED; Genomic_DNA.
DR CCDS; CCDS27755.1; -.
DR PIR; A37344; A37344.
DR PIR; JX0172; JX0172.
DR RefSeq; NP_038483.1; NM_013455.3.
DR AlphaFoldDB; P23578; -.
DR SMR; P23578; -.
DR BioGRID; 197930; 1.
DR STRING; 10090.ENSMUSP00000023295; -.
DR MEROPS; S01.223; -.
DR GlyCosmos; P23578; 2 sites, No reported glycans.
DR GlyGen; P23578; 2 sites.
DR SwissPalm; P23578; -.
DR PaxDb; 10090-ENSMUSP00000023295; -.
DR ProteomicsDB; 285845; -.
DR Antibodypedia; 53952; 256 antibodies from 27 providers.
DR DNASU; 11434; -.
DR Ensembl; ENSMUST00000023295.3; ENSMUSP00000023295.3; ENSMUSG00000022622.6.
DR GeneID; 11434; -.
DR KEGG; mmu:11434; -.
DR UCSC; uc007xhc.2; mouse.
DR AGR; MGI:87884; -.
DR CTD; 49; -.
DR MGI; MGI:87884; Acr.
DR VEuPathDB; HostDB:ENSMUSG00000022622; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162430; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; P23578; -.
DR OMA; LMCRDNV; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; P23578; -.
DR TreeFam; TF335943; -.
DR Reactome; R-MMU-1300645; Acrosome Reaction and Sperm:Oocyte Membrane Binding.
DR BioGRID-ORCS; 11434; 2 hits in 78 CRISPR screens.
DR PRO; PR:P23578; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P23578; Protein.
DR Bgee; ENSMUSG00000022622; Expressed in seminiferous tubule of testis and 48 other cell types or tissues.
DR ExpressionAtlas; P23578; baseline and differential.
DR Genevisible; P23578; MM.
DR GO; GO:0043159; C:acrosomal matrix; TAS:HGNC-UCL.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004040; F:amidase activity; ISS:UniProtKB.
DR GO; GO:0042806; F:fucose binding; ISS:UniProtKB.
DR GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IMP:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0002077; P:acrosome matrix dispersal; ISO:MGI.
DR GO; GO:0007340; P:acrosome reaction; ISS:UniProtKB.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IGI:MGI.
DR GO; GO:0007341; P:penetration of zona pellucida; IMP:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0048545; P:response to steroid hormone; ISO:MGI.
DR GO; GO:0007338; P:single fertilization; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT CHAIN 20..436
FT /note="Acrosin"
FT /id="PRO_0000027522"
FT CHAIN 20..42
FT /note="Acrosin light chain"
FT /id="PRO_0000027523"
FT CHAIN 43..345
FT /note="Acrosin heavy chain"
FT /id="PRO_0000027524"
FT PROPEP 346..436
FT /note="Pro-rich"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027525"
FT DOMAIN 43..291
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 89
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 25..155
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 29..163
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 74..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 178..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 210..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 237..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 8
FT /note="Missing (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 10..14
FT /note="VLVLA -> FWSVK (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 17..18
FT /note="VV -> AG (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="T -> A (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="D -> F (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="F -> T (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..51
FT /note="QL -> HV (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="Q -> E (in Ref. 3; CAA36704/AAA40124 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="I -> V (in Ref. 3; CAA36704/AAA40124 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..174
FT /note="QI -> RNT (in Ref. 3; AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="Q -> RK (in Ref. 3; CAA36704)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..183
FT /note="TCYVTGW -> LLRDWV (in Ref. 3; AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 185..186
FT /note="YI -> IH (in Ref. 3; AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..189
FT /note="EK -> RE (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 251..253
FT /note="VDS -> ARQ (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..268
FT /note="FVVVGITSWGVGCA -> LCGRGDHELGGRLC (in Ref. 3;
FT AAA40124 and 4; AAA37163)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..300
FT /note="QP -> PA (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="L -> F (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="H -> Y (in Ref. 3; CAA36704/AAA40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 407..436
FT /note="SQYSGPRNYHYRFSTFEPLSNKPSEPFLHS -> PSTVDKELPLPLLHV
FT (in Ref. 3; CAA36704/AAA40124 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 48929 MW; 4CC6EAD56CB51F54 CRC64;
MVEMLPTVAV LVLAVSVVAK DNTTCDGPCG LRFRQNSQAG TRIVSGQSAQ LGAWPWMVSL
QIFTSHNSRR YHACGGSLLN SHWVLTAAHC FDNKKKVYDW RLVFGAQEIE YGRNKPVKEP
QQERYVQKIV IHEKYNVVTE GNDIALLKIT PPVTCGNFIG PCCLPHFKAG PPQIPHTCYV
TGWGYIKEKA PRPSPVLMEA RVDLIDLDLC NSTQWYNGRV TSTNVCAGYP EGKIDTCQGD
SGGPLMCRDN VDSPFVVVGI TSWGVGCARA KRPGVYTATW DYLDWIASKI GPNALHLIQP
ATPHPPTTRH PMVSFHPPSL RPPWYFQHLP SRPLYLRPLR PLLHRPSSTQ TSSSLMPLLS
PPTPAQPASF TIATQHMRHR TTLSFARRLQ RLIEALKMRT YPMKHPSQYS GPRNYHYRFS
TFEPLSNKPS EPFLHS
//
