ACRO_SHEEP
ID ACRO_SHEEP Reviewed; 329 AA.
AC Q9GL10;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 97.
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; Fragment;
GN Name=ACR;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF
RP 18-329.
RC TISSUE=Testis;
RX PubMed=11080640; DOI=10.1016/s0969-2126(00)00523-2;
RA Tranter R., Read J.A., Jones R., Brady R.L.;
RT "Effector sites in the three dimensional structure of mammalian sperm beta-
RT acrosin.";
RL Structure 8:1179-1188(2000).
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; AJ278742; CAC15386.1; -; mRNA.
DR PDB; 1FIW; X-ray; 2.10 A; A=40-329, L=18-39.
DR PDBsum; 1FIW; -.
DR AlphaFoldDB; Q9GL10; -.
DR SMR; Q9GL10; -.
DR STRING; 9940.ENSOARP00000021514; -.
DR MEROPS; S01.223; -.
DR eggNOG; KOG3627; Eukaryota.
DR BRENDA; 3.4.21.10; 2668.
DR EvolutionaryTrace; Q9GL10; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:InterPro.
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:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0007340; P:acrosome reaction; ISS:UniProtKB.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..17
FT CHAIN 18..329
FT /note="Acrosin"
FT /id="PRO_0000027538"
FT CHAIN 18..39
FT /note="Acrosin light chain"
FT /id="PRO_0000027539"
FT CHAIN 40..>329
FT /note="Acrosin heavy chain"
FT /id="PRO_0000027540"
FT DOMAIN 40..288
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 86
FT /note="Charge relay system"
FT ACT_SITE 140
FT /note="Charge relay system"
FT ACT_SITE 238
FT /note="Charge relay system"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 22..152
FT /note="Interchain (between light and heavy chains)"
FT DISULFID 26..160
FT /note="Interchain (between light and heavy chains)"
FT DISULFID 71..87
FT DISULFID 175..244
FT DISULFID 207..223
FT DISULFID 234..264
FT NON_TER 329
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:1FIW"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1FIW"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1FIW"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:1FIW"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:1FIW"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:1FIW"
FT TURN 210..215
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1FIW"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1FIW"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1FIW"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:1FIW"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:1FIW"
SQ SEQUENCE 329 AA; 36119 MW; B934C569D83E21E0 CRC64;
MLPTAVLLVL AVSVVARDNT TCDGPCGVRF RQNRQGGVRI IGGQDAAHGA WPWMVSLQIF
TYHNNRRYHV CGGSLLNSQW LLTAAHCFRI KKKVTDWRLI FGAKEVEWGT NKPVKPPLQE
RYVEKIIIHE KYSASSEAND IALMKITPPV TCGHFIGPGC LPQFRAGPPR VPQTCWVAGW
GFLQENARRT SPMLQEARVD LIDLGLCNST RWYNGRIRST NVCAGYPEGK IDTCQGDSGG
PLMCKDSAEN SYVVVGITSW GVGCARAKRP GVYTSTWSYL NWIASKIGST AVHMIQLPTA
SPASTPGAQA SSGSVQPSVR PPWFFQQIT
