ID   KLK3_MACFA              Reviewed;         261 AA.
AC   Q6DT45;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
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 fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16430490; DOI=10.1111/j.1600-0684.2005.00134.x;
RA   Marshall D.J., Rudnick K.A., Lu J., Snyder L.A.;
RT   "Cloning and sequencing of the cynomolgus monkey prostate specific antigen
RT   cDNA.";
RL   J. Med. Primatol. 35:12-17(2006).
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}.
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DR   EMBL; AY647976; AAT68459.1; -; mRNA.
DR   AlphaFoldDB; Q6DT45; -.
DR   SMR; Q6DT45; -.
DR   STRING; 9541.XP_005590103.1; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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_0000027933"
FT   CHAIN           25..261
FT                   /note="Prostate-specific antigen"
FT                   /id="PRO_0000027934"
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;  28820 MW;  8EC937876F98CBBE CRC64;
     MWVLVVFLTL SVTWIGAAPL ILSRIVGGWE CEKHSQPWQV LVASHGRAVC GGVLVHPQWV
     LTAAHCIRSH SVILLGRHNP YYPEDTGQVF QVSHSFPHPL YNMSLLKNRY LGPGDDSSHD
     LMLLRLSEPA EITDAVQVLD LPTWEPELGT TCYASGWGSI EPEEHLTPKK LQCVDLHIIS
     NDVCAQVHSQ KVTKFMLCAG SWMGGKSTCS GDSGGPLVCD GVLQGITSWG SQPCALPRRP
     SLYTKVVRYR KWIQDTIMAN P