ACRO_RAT
ID ACRO_RAT Reviewed; 437 AA.
AC P29293; Q4QR89; Q9QWF2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 164.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=1932123; DOI=10.1016/0167-4781(91)90117-5;
RA Klemm U., Flake A., Engel W.;
RT "Rat sperm acrosin: cDNA sequence, derived primary structure and
RT phylogenetic origin.";
RL Biochim. Biophys. Acta 1090:270-272(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1802037; DOI=10.3109/10425179109008440;
RA Kremling H., Flake A., Adham I.M., Radtke J., Engel W.;
RT "Exon-intron structure and nucleotide sequence of the rat proacrosin
RT gene.";
RL DNA Seq. 2:57-60(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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 -!- 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}.
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DR EMBL; X59254; CAA41947.1; -; mRNA.
DR EMBL; X58550; CAA41441.2; -; Genomic_DNA.
DR EMBL; BC097345; AAH97345.1; -; mRNA.
DR PIR; S18407; S18407.
DR RefSeq; NP_036622.2; NM_012490.2.
DR AlphaFoldDB; P29293; -.
DR SMR; P29293; -.
DR STRING; 10116.ENSRNOP00000046900; -.
DR MEROPS; S01.223; -.
DR GlyGen; P29293; 2 sites.
DR PaxDb; P29293; -.
DR Ensembl; ENSRNOT00000045647; ENSRNOP00000046900; ENSRNOG00000029762.
DR GeneID; 24163; -.
DR KEGG; rno:24163; -.
DR CTD; 49; -.
DR RGD; 2024; Acr.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162430; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; P29293; -.
DR OMA; LMCRDNV; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P29293; -.
DR TreeFam; TF335943; -.
DR BRENDA; 3.4.21.10; 5301.
DR Reactome; R-RNO-1300645; Acrosome Reaction and Sperm:Oocyte Membrane Binding.
DR PRO; PR:P29293; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000029762; Expressed in testis and 6 other tissues.
DR ExpressionAtlas; P29293; baseline and differential.
DR Genevisible; P29293; RN.
DR GO; GO:0043159; C:acrosomal matrix; TAS:HGNC-UCL.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
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; ISO:RGD.
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; IMP:RGD.
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; ISO:RGD.
DR GO; GO:0007341; P:penetration of zona pellucida; IMP:RGD.
DR GO; GO:0030163; P:protein catabolic process; IMP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IDA:RGD.
DR GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 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 Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001141; Acrosin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 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; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..437
FT /note="Acrosin"
FT /id="PRO_0000027534"
FT CHAIN 20..42
FT /note="Acrosin light chain"
FT /id="PRO_0000027535"
FT CHAIN 43..345
FT /note="Acrosin heavy chain"
FT /id="PRO_0000027536"
FT PROPEP 346..437
FT /note="Pro-rich"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027537"
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 22..26
FT /note="Missing (in Ref. 2; CAA41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..52
FT /note="PG -> RW (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="K -> KR (in Ref. 2; CAA41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 250..253
FT /note="SVDS -> TRRQ (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..268
FT /note="FVIVGITSWGVGCA -> LCDRGDHELGGRLC (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 320..337
FT /note="IHPPWYFQHLSPRPPHLR -> TPPSLVLPTPVSSAALPT (in Ref. 1
FT and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 388..389
FT /note="RR -> SA (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 48623 MW; 882CF0F7896A927E CRC64;
MVEMLPTVVA LVLAVSVVAK DNTTCDGPCG LRFRQNPQAG IRIVGGQTSS PGAWPWMVSL
QIFTSHNSRR YHACGGSLLN SHWVLTAAHC FDNKKKVYDW RLVFGAHEIE YGRNKPVKEP
QQERYVQKIV IHEKYNAVTE GNDIALLKVT PPVTCGDFVG PGCLPHFKSG PPRIPHTCYV
TGWGYIKDNA PRPSPVLMEA RVDLIDLDLC NSTQWYNGRV TSTNVCAGYP EGKIDTCQGD
SGGPLMCRDS VDSPFVIVGI TSWGVGCARA KRPGVYTATW DYLDWIASKI GPTALHLIQP
ATPHPPTTQQ PVISFHPPSI HPPWYFQHLS PRPPHLRPPR PLLHQPSSVH TSSAPVIPLL
SLLTPVQPVS FTLAAYHTRH HTTLSFARRL QHLIEALKMR TYPIKYPSRY SGPVNYQHRF
STFEPLSNKP SEPLLHS
