ID A0A287AFN9_PIG Unreviewed; 414 AA.
AC A0A287AFN9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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|Ensembl:ENSSSCP00000042835.1,
GN ECO:0000313|VGNC:VGNC:103212};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000042835.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000042835.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000042835.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000042835.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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 AlphaFoldDB; A0A287AFN9; -.
DR SMR; A0A287AFN9; -.
DR Ensembl; ENSSSCT00000060173.1; ENSSSCP00000042835.1; ENSSSCG00000021265.3.
DR VGNC; VGNC:103212; ACR.
DR GeneTree; ENSGT00940000162430; -.
DR InParanoid; A0A287AFN9; -.
DR Reactome; R-SSC-1300645; Acrosome Reaction and Sperm:Oocyte Membrane Binding.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000021265; Expressed in testis and 3 other cell types or tissues.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005537; F:mannose binding; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007340; P:acrosome reaction; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0007341; P:penetration of zona pellucida; IEA:Ensembl.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Serine protease {ECO:0000256|PIRNR:PIRNR001141,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..414
FT /note="Acrosin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013080910"
FT DOMAIN 40..288
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 296..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-1"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-1"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-1"
FT DISULFID 22..152
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-2"
FT DISULFID 26..160
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-2"
FT DISULFID 71..87
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-2"
FT DISULFID 175..244
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-2"
FT DISULFID 207..223
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-2"
FT DISULFID 234..264
FT /evidence="ECO:0000256|PIRSR:PIRSR001141-2"
SQ SEQUENCE 414 AA; 45408 MW; A3E763E02B4F32F1 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 PPAPPLPRPP RPPTPTASTT
PTPPPQQVSA KPPQALSFAK RLQQLIEALK GTAFSSGRSY YETETTDLQE LPAS
//