GenomeNet

Database: UniProt
Entry: A0A287AFN9_PIG
LinkDB: A0A287AFN9_PIG
Original site: A0A287AFN9_PIG 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system