ID   KLK3_MACMU              Reviewed;         261 AA.
AC   P33619;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Prostate-specific antigen;
DE            Short=PSA;
DE            EC=3.4.21.77;
DE   AltName: Full=Kallikrein-3;
DE   AltName: Full=Semenogelase;
DE   Flags: Precursor;
GN   Name=KLK3; Synonyms=APS;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7689340; DOI=10.1016/0167-4781(93)90118-w;
RA   Gauthier E.R., Chapdelaine P., Tremblay R.R., Dube J.Y.;
RT   "Characterization of rhesus monkey prostate specific antigen cDNA.";
RL   Biochim. Biophys. Acta 1174:207-210(1993).
CC   -!- FUNCTION: Hydrolyzes semenogelin-1 thus leading to the liquefaction of
CC       the seminal coagulum. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: -Tyr-|-Xaa-.; EC=3.4.21.77;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5. Activity is strongly
CC       inhibited by Zn2+, 100 times more abundant in semen than in serum. This
CC       inhibition is relieved by exposure to semenogelins, which are avid zinc
CC       binders (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a heterodimer with SERPINA5. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   EMBL; X73560; CAA51957.1; -; mRNA.
DR   PIR; S35711; S35711.
DR   RefSeq; NP_001036241.1; NM_001042776.1.
DR   AlphaFoldDB; P33619; -.
DR   SMR; P33619; -.
DR   STRING; 9544.ENSMMUP00000031500; -.
DR   MEROPS; S01.162; -.
DR   Ensembl; ENSMMUT00000038399; ENSMMUP00000031500; ENSMMUG00000012841.
DR   GeneID; 719444; -.
DR   KEGG; mcc:719444; -.
DR   CTD; 354; -.
DR   VEuPathDB; HostDB:ENSMMUG00000012841; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01020000230389; -.
DR   InParanoid; P33619; -.
DR   BRENDA; 3.4.21.77; 3126.
DR   Proteomes; UP000006718; Chromosome 19.
DR   Bgee; ENSMMUG00000012841; Expressed in testis and 4 other tissues.
DR   ExpressionAtlas; P33619; baseline.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR   GO; GO:0002803; P:positive regulation of antibacterial peptide production; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
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   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   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /note="Activation peptide"
FT                   /id="PRO_0000027935"
FT   CHAIN           25..261
FT                   /note="Prostate-specific antigen"
FT                   /id="PRO_0000027936"
FT   DOMAIN          25..258
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        120
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        152..219
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        184..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        209..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   261 AA;  28816 MW;  8525B14B15967E5C CRC64;
     MWVLVVFLTL SVTWIGAAPL ILSRIVGGWE CEKHSQPWQV LVASRGRAVC GGVLVHPQWV
     LTAAHCIRSN SVILLGRHNP YYPEDTGQVF QVSHSFPHPL YNMSLLKNRY LGPGDDSSHD
     LMLLRLSEPA EITDAVQVLD LPTWEPELGT TCYASGWGSI EPEEHLTPKK LQCVDLHIIS
     NDVCAQVHSQ KVTKFMLCAG SWMGGKSTCS GDSGGPLVCD GVLQGITSWG SQPCALPRRP
     SLYTKVVRYR KWIQDTIMAN P