ACRO_PIG
ID ACRO_PIG Reviewed; 415 AA.
AC P08001; P08000; Q29015;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 5.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Acrosin;
DE EC=3.4.21.10;
DE AltName: Full=53 kDa fucose-binding protein;
DE Contains:
DE RecName: Full=Acrosin light chain;
DE Contains:
DE RecName: Full=Acrosin heavy chain;
DE Flags: Precursor;
GN Name=ACR;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2745422; DOI=10.1016/s0021-9258(18)80154-5;
RA Baba T., Kashiwabara S., Watanabe K., Itoh H., Michikawa Y., Kimura K.,
RA Takada M., Fukamizu A., Arai Y.;
RT "Activation and maturation mechanisms of boar acrosin zymogen based on the
RT deduced primary structure.";
RL J. Biol. Chem. 264:11920-11927(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=2502391; DOI=10.1111/j.1432-1033.1989.tb14864.x;
RA Adham I.M., Maier W.-M., Hoyer-Fender S., Tsaousidou S., Engel W.,
RA Klemm U.;
RT "Molecular cloning of preproacrosin and analysis of its expression pattern
RT in spermatogenesis.";
RL Eur. J. Biochem. 182:563-568(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8737992;
RA Adham I.M., Kremling H., Nieter S., Zimmermann S., Hummel M., Schroeter U.,
RA Engel W.;
RT "The structures of the bovine and porcine proacrosin genes and their
RT conservation during mammals.";
RL Biol. Chem. Hoppe-Seyler 377:261-265(1996).
RN [4]
RP PROTEIN SEQUENCE OF 17-39.
RC TISSUE=Sperm;
RX PubMed=6378631; DOI=10.1111/j.1432-1033.1984.tb08211.x;
RA Fock-Nuezel R., Lottspeich F., Henschen A., Mueller-Esterl W.;
RT "Boar acrosin is a two-chain molecule. Isolation and primary structure of
RT the light chain; homology with the pro-part of other serine proteinases.";
RL Eur. J. Biochem. 141:441-446(1984).
RN [5]
RP PROTEIN SEQUENCE OF 25-91.
RC TISSUE=Sperm;
RX PubMed=7007202; DOI=10.1515/bchm2.1980.361.2.1823;
RA Fock-Nuezel R., Lottspeich F., Henschen A., Mueller-Esterl W., Fritz H.;
RT "N-terminal amino acid sequence of boar sperm acrosin. Homology with other
RT serine proteinases.";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:1823-1828(1980).
RN [6]
RP PROTEIN SEQUENCE OF 17-32 AND 40-53.
RC TISSUE=Sperm;
RX PubMed=3480243; DOI=10.1016/0014-5793(87)80546-x;
RA Toepfer-Petersen E., Henschen A.;
RT "Acrosin shows zona and fucose binding, novel properties for a serine
RT proteinase.";
RL FEBS Lett. 226:38-42(1987).
RN [7]
RP PROTEIN SEQUENCE OF 17-40.
RX PubMed=2111146; DOI=10.1515/bchm3.1990.371.1.317;
RA Cechova D., Toepfer-Petersen E., Zucker A., Jonakova V.;
RT "Is sperminogen a modified proacrosin? Isolation, purification, and partial
RT characterization of low-molecular-mass boar proacrosin.";
RL Biol. Chem. Hoppe-Seyler 371:317-323(1990).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-19 AND
RP ASN-208.
RC TISSUE=Sperm;
RX PubMed=2261983; DOI=10.1016/0014-5793(90)81458-z;
RA Toepfer-Petersen E., Calvete J.J., Schaefer W., Henschen A.;
RT "Complete localization of the disulfide bridges and glycosylation sites in
RT boar sperm acrosin.";
RL FEBS Lett. 275:139-142(1990).
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; J04950; AAA31131.1; -; mRNA.
DR EMBL; X14844; CAA32948.1; -; mRNA.
DR EMBL; X58549; CAA41440.1; -; Genomic_DNA.
DR PIR; A34170; A34170.
DR RefSeq; NP_999198.1; NM_214033.1.
DR PDB; 1FIZ; X-ray; 2.90 A; A=40-302, L=17-39.
DR PDBsum; 1FIZ; -.
DR AlphaFoldDB; P08001; -.
DR SMR; P08001; -.
DR STRING; 9823.ENSSSCP00000021991; -.
DR BindingDB; P08001; -.
DR ChEMBL; CHEMBL3243910; -.
DR DrugCentral; P08001; -.
DR MEROPS; S01.223; -.
DR iPTMnet; P08001; -.
DR PaxDb; P08001; -.
DR PeptideAtlas; P08001; -.
DR GeneID; 397098; -.
DR KEGG; ssc:397098; -.
DR CTD; 49; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P08001; -.
DR OrthoDB; 1314811at2759; -.
DR BRENDA; 3.4.21.10; 6170.
DR EvolutionaryTrace; P08001; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0043159; C:acrosomal matrix; NAS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0004040; F:amidase activity; IMP:UniProtKB.
DR GO; GO:0042806; F:fucose binding; IDA: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; IMP: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; IMP: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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:2111146,
FT ECO:0000269|PubMed:3480243, ECO:0000269|PubMed:6378631"
FT CHAIN 17..415
FT /note="Acrosin"
FT /id="PRO_0000027526"
FT CHAIN 17..39
FT /note="Acrosin light chain"
FT /id="PRO_0000027527"
FT CHAIN 40..338
FT /note="Acrosin heavy chain"
FT /id="PRO_0000027528"
FT PROPEP 339..415
FT /note="Pro-rich"
FT /id="PRO_0000027529"
FT DOMAIN 40..288
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 296..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2261983"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2261983"
FT DISULFID 22..152
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:2261983"
FT DISULFID 26..160
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:2261983"
FT DISULFID 71..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:2261983"
FT DISULFID 175..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:2261983"
FT DISULFID 207..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:2261983"
FT DISULFID 234..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:2261983"
FT CONFLICT 8
FT /note="Missing (in Ref. 2; CAA32948)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="R -> Q (in Ref. 2; CAA32948)"
FT /evidence="ECO:0000305"
FT CONFLICT 217..218
FT /note="IR -> VT (in Ref. 2; CAA32948)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="A -> P (in Ref. 1; AAA31131)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="Missing (in Ref. 2; CAA32948)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..402
FT /note="RSYY -> KELL (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..415
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:1FIZ"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1FIZ"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:1FIZ"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:1FIZ"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:1FIZ"
FT TURN 210..215
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1FIZ"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1FIZ"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1FIZ"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:1FIZ"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:1FIZ"
SQ SEQUENCE 415 AA; 45362 MW; BAC41900AD43E768 CRC64;
MLPTAVLLVL AVSVAARDNA TCDGPCGLRF RQKLESGMRV VGGMSAEPGA WPWMVSLQIF
MYHNNRRYHT CGGILLNSHW VLTAAHCFKN KKKVTDWRLI FGANEVVWGS NKPVKPPLQE
RFVEEIIIHE KYVSGLEIND IALIKITPPV PCGPFIGPGC LPQFKAGPPR APQTCWVTGW
GYLKEKGPRT SPTLQEARVA LIDLELCNST RWYNGRIRST NVCAGYPRGK IDTCQGDSGG
PLMCRDRAEN TFVVVGITSW GVGCARAKRP GVYTSTWPYL NWIASKIGSN ALQMVQLGTP
PRPSTPAPPV RPPSVQTPVR PPWYFQRPPG PSQQPGSRPR PPAPPPAPPP PPPPPPPPPP
PPPPPPQQVS AKPPQALSFA KRLQQLIEAL KGTAFSSGRS YYETETTDLQ ELPAS
