KLK3_HUMAN
ID KLK3_HUMAN Reviewed; 261 AA.
AC P07288; C9JXH3; G3V0H4; G3XAE3; Q15096; Q16272; Q86TG8; Q8IXI4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Prostate-specific antigen;
DE Short=PSA;
DE EC=3.4.21.77;
DE AltName: Full=Gamma-seminoprotein;
DE Short=Seminin;
DE AltName: Full=Kallikrein-3;
DE AltName: Full=P-30 antigen;
DE AltName: Full=Semenogelase;
DE Flags: Precursor;
GN Name=KLK3; Synonyms=APS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 4-238
RP (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Prostate;
RX PubMed=2436946; DOI=10.1016/0014-5793(87)80078-9;
RA Lundwall A., Lilja H.;
RT "Molecular cloning of human prostate specific antigen cDNA.";
RL FEBS Lett. 214:317-322(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Prostate;
RX PubMed=2467258; DOI=10.1093/nar/17.5.2137;
RA Digby M.R., Zhang X.Y., Richard R.I.;
RT "Human prostate specific antigen (PSA) gene: structure and linkage to the
RT kallikrein-like gene, hGK-1.";
RL Nucleic Acids Res. 17:2137-2137(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2471958; DOI=10.1093/nar/17.10.3981;
RA Klobeck H.-G., Combriato G., Schulz P., Arbusow V., Fittler F.;
RT "Genomic sequence of human prostate specific antigen (PSA).";
RL Nucleic Acids Res. 17:3981-3981(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leukocyte;
RX PubMed=2472789; DOI=10.1016/0006-291x(89)91362-4;
RA Lundwall A.;
RT "Characterization of the gene for prostate-specific antigen, a human
RT glandular kallikrein.";
RL Biochem. Biophys. Res. Commun. 161:1151-1159(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=2470373; DOI=10.1016/0006-291x(89)92520-5;
RA Henttu P., Vihko P.;
RT "cDNA coding for the entire human prostate specific antigen shows high
RT homologies to the human tissue kallikrein genes.";
RL Biochem. Biophys. Res. Commun. 160:903-910(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Prostate;
RX PubMed=2466464; DOI=10.1016/0006-291x(89)92409-1;
RA Riegman P.H.J., Vlietstra R.J., van der Korput J.A.G.M., Romijn J.C.,
RA Trapman J.;
RT "Characterization of the prostate-specific antigen gene: a novel human
RT kallikrein-like gene.";
RL Biochem. Biophys. Res. Commun. 159:95-102(1989).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=8677566; DOI=10.1016/s0090-4295(96)00060-x;
RA Baffa R., Moreno J.G., Monne M., Veronese M.L., Gomella L.G.;
RT "A comparative analysis of prostate-specific antigen gene sequence in
RT benign and malignant prostate tissue.";
RL Urology 47:795-800(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11054574; DOI=10.1016/s0378-1119(00)00382-6;
RA Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J., Moss P.,
RA Paeper B., Wang K.;
RT "Sequencing and expression analysis of the serine protease gene cluster
RT located in chromosome 19q13 region.";
RL Gene 257:119-130(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND ALTERNATIVE SPLICING.
RC TISSUE=Prostate;
RA Heuze-Vourc'h N., Courty Y.;
RT "Complex alternative splicing of the hKLK3 gene coding for the tumour
RT marker PSA (prostate-specific-antigen).";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=PNS, Prostate, and Sciatic nerve;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-176 (ISOFORM 1).
RX PubMed=7527295;
RA Monne M., Croce C.M., Yu H., Diamandis E.P.;
RT "Molecular characterization of prostate-specific antigen messenger RNA
RT expressed in breast tumors.";
RL Cancer Res. 54:6344-6347(1994).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-261 (ISOFORM 1).
RX PubMed=2456523; DOI=10.1093/nar/16.13.6226;
RA Schulz P., Stucka R., Feldmann H., Combriato G., Klobeck H.-G., Fittler F.;
RT "Sequence of a cDNA clone encompassing the complete mature human prostate
RT specific antigen (PSA) and an unspliced leader sequence.";
RL Nucleic Acids Res. 16:6226-6226(1988).
RN [16]
RP PROTEIN SEQUENCE OF 25-261.
RX PubMed=2422647; DOI=10.1073/pnas.83.10.3166;
RA Watt K.W.K., Lee P.J., M'Timkulu T., Chan W.P., Loor R.;
RT "Human prostate-specific antigen: structural and functional similarity with
RT serine proteases.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3166-3170(1986).
RN [17]
RP PROTEIN SEQUENCE OF 25-261.
RX PubMed=3691515; DOI=10.1111/j.1432-1033.1987.tb13674.x;
RA Schaller J., Akiyama K., Tsuda R., Hara M., Marti T., Rickli E.E.;
RT "Isolation, characterization and amino-acid sequence of gamma-
RT seminoprotein, a glycoprotein from human seminal plasma.";
RL Eur. J. Biochem. 170:111-120(1987).
RN [18]
RP PROTEIN SEQUENCE OF 18-32.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [19]
RP PROTEIN SEQUENCE OF 126-138, AND VARIANT ILE-132.
RX PubMed=23842001; DOI=10.1074/mcp.m113.028365;
RA Vegvari A., Sjodin K., Rezeli M., Malm J., Lilja H., Laurell T.,
RA Marko-Varga G.;
RT "Identification of a novel proteoform of prostate specific antigen (SNP-
RT L132I) in clinical samples by multiple reaction monitoring.";
RL Mol. Cell. Proteomics 12:2761-2773(2013).
RN [20]
RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
RX PubMed=1725227; DOI=10.1016/0049-3848(91)90002-e;
RA Espana F., Gilabert J., Estelles A., Romeu A., Aznar J., Cabo A.;
RT "Functionally active protein C inhibitor/plasminogen activator inhibitor-3
RT (PCI/PAI-3) is secreted in seminal vesicles, occurs at high concentrations
RT in human seminal plasma and complexes with prostate-specific antigen.";
RL Thromb. Res. 64:309-320(1991).
RN [21]
RP 3D-STRUCTURE MODELING.
RX PubMed=7535613; DOI=10.1002/pro.5560031116;
RA Villoutreix B.O., Getzoff E.D., Griffin J.H.;
RT "A structural model for the prostate disease marker, human prostate-
RT specific antigen.";
RL Protein Sci. 3:2033-2044(1994).
RN [22]
RP 3D-STRUCTURE MODELING.
RX PubMed=9751643; DOI=10.1016/s1074-5521(98)90004-7;
RA Coombs G.S., Bergstrom R.C., Pellequer J.L., Baker S.I., Navre M.,
RA Smith M.M., Tainer J.A., Madison E.L., Corey D.R.;
RT "Substrate specificity of prostate-specific antigen (PSA).";
RL Chem. Biol. 5:475-488(1998).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 25-261 IN COMPLEX WITH SUBSTRATE
RP AND ACTIVATING ANTIBODY, ACTIVITY REGULATION, ACTIVE SITE, AND DISULFIDE
RP BONDS.
RX PubMed=18187150; DOI=10.1016/j.jmb.2007.11.052;
RA Menez R., Michel S., Muller B.H., Bossus M., Ducancel F.,
RA Jolivet-Reynaud C., Stura E.A.;
RT "Crystal structure of a ternary complex between human prostate-specific
RT antigen, its substrate acyl intermediate and an activating antibody.";
RL J. Mol. Biol. 376:1021-1033(2008).
CC -!- FUNCTION: Hydrolyzes semenogelin-1 thus leading to the liquefaction of
CC the seminal coagulum.
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. {ECO:0000269|PubMed:1725227, ECO:0000269|PubMed:18187150}.
CC -!- SUBUNIT: Forms a heterodimer with SERPINA5.
CC {ECO:0000269|PubMed:18187150}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P07288-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07288-2; Sequence=VSP_045786;
CC Name=3;
CC IsoId=P07288-3; Sequence=VSP_046169, VSP_046171;
CC Name=4;
CC IsoId=P07288-4; Sequence=VSP_046169, VSP_046170;
CC Name=5;
CC IsoId=P07288-5; Sequence=VSP_047643;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD14185.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA32124.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Prostate-specific antigen entry;
CC URL="https://en.wikipedia.org/wiki/Prostate_specific_antigen";
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; M21896; AAA59996.1; -; mRNA.
DR EMBL; X05332; CAA28947.1; -; mRNA.
DR EMBL; X13940; CAA32123.1; -; Genomic_DNA.
DR EMBL; X13941; CAA32124.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X13942; CAB46487.1; -; Genomic_DNA.
DR EMBL; X13943; CAA32126.1; -; Genomic_DNA.
DR EMBL; X13944; CAA32127.1; -; Genomic_DNA.
DR EMBL; X14810; CAA32915.1; -; Genomic_DNA.
DR EMBL; M27274; AAA60192.1; -; Genomic_DNA.
DR EMBL; M26663; AAA58802.1; -; mRNA.
DR EMBL; M24543; AAA60193.1; -; Genomic_DNA.
DR EMBL; U17040; AAA56764.1; -; mRNA.
DR EMBL; AF243527; AAG33355.1; -; Genomic_DNA.
DR EMBL; AJ512346; CAD54617.1; -; mRNA.
DR EMBL; BT019862; AAV38665.1; -; mRNA.
DR EMBL; AC011523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW71929.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW71930.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW71936.1; -; Genomic_DNA.
DR EMBL; BC005307; AAH05307.1; -; mRNA.
DR EMBL; BC050595; AAH50595.2; -; mRNA.
DR EMBL; BC056665; AAH56665.1; -; mRNA.
DR EMBL; BF679511; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BQ932072; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S75755; AAD14185.1; ALT_INIT; mRNA.
DR EMBL; X07730; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS12807.1; -. [P07288-1]
DR CCDS; CCDS33083.1; -. [P07288-2]
DR CCDS; CCDS46155.1; -. [P07288-3]
DR PIR; A32297; A32297.
DR RefSeq; NP_001025218.1; NM_001030047.1. [P07288-2]
DR RefSeq; NP_001025219.1; NM_001030048.1. [P07288-3]
DR RefSeq; NP_001639.1; NM_001648.2. [P07288-1]
DR PDB; 2ZCH; X-ray; 2.83 A; P=25-261.
DR PDB; 2ZCK; X-ray; 3.10 A; P=25-261.
DR PDB; 2ZCL; X-ray; 3.25 A; P=25-261.
DR PDB; 3QUM; X-ray; 3.20 A; P/Q=25-261.
DR PDBsum; 2ZCH; -.
DR PDBsum; 2ZCK; -.
DR PDBsum; 2ZCL; -.
DR PDBsum; 3QUM; -.
DR AlphaFoldDB; P07288; -.
DR SMR; P07288; -.
DR BioGRID; 106850; 61.
DR CORUM; P07288; -.
DR IntAct; P07288; 10.
DR MINT; P07288; -.
DR STRING; 9606.ENSP00000314151; -.
DR BindingDB; P07288; -.
DR ChEMBL; CHEMBL2099; -.
DR DrugBank; DB04839; Cyproterone acetate.
DR DrugBank; DB16019; Gallium Ga-68 gozetotide.
DR DrugBank; DB00834; Mifepristone.
DR GuidetoPHARMACOLOGY; 2373; -.
DR Allergome; 2836; Hom s PSA.
DR MEROPS; S01.162; -.
DR GlyConnect; 666; 57 N-Linked glycans (1 site).
DR GlyConnect; 790; 167 N-Linked glycans (1 site).
DR GlyGen; P07288; 1 site, 173 N-linked glycans (1 site).
DR iPTMnet; P07288; -.
DR PhosphoSitePlus; P07288; -.
DR SwissPalm; P07288; -.
DR BioMuta; KLK3; -.
DR DMDM; 130989; -.
DR CPTAC; CPTAC-1296; -.
DR CPTAC; CPTAC-1476; -.
DR jPOST; P07288; -.
DR MassIVE; P07288; -.
DR MaxQB; P07288; -.
DR PaxDb; P07288; -.
DR PeptideAtlas; P07288; -.
DR PRIDE; P07288; -.
DR ProteomicsDB; 12120; -.
DR ProteomicsDB; 32197; -.
DR ProteomicsDB; 33725; -.
DR ProteomicsDB; 51977; -. [P07288-1]
DR ABCD; P07288; 9 sequenced antibodies.
DR Antibodypedia; 743; 2492 antibodies from 51 providers.
DR DNASU; 354; -.
DR Ensembl; ENST00000326003.7; ENSP00000314151.1; ENSG00000142515.16. [P07288-1]
DR Ensembl; ENST00000360617.7; ENSP00000353829.2; ENSG00000142515.16. [P07288-2]
DR Ensembl; ENST00000593997.5; ENSP00000472907.1; ENSG00000142515.16. [P07288-5]
DR Ensembl; ENST00000595952.5; ENSP00000471155.1; ENSG00000142515.16. [P07288-3]
DR GeneID; 354; -.
DR KEGG; hsa:354; -.
DR MANE-Select; ENST00000326003.7; ENSP00000314151.1; NM_001648.2; NP_001639.1.
DR UCSC; uc002ptr.2; human. [P07288-1]
DR CTD; 354; -.
DR DisGeNET; 354; -.
DR GeneCards; KLK3; -.
DR HGNC; HGNC:6364; KLK3.
DR HPA; ENSG00000142515; Tissue enriched (prostate).
DR MIM; 176820; gene.
DR neXtProt; NX_P07288; -.
DR OpenTargets; ENSG00000142515; -.
DR PharmGKB; PA164741810; -.
DR VEuPathDB; HostDB:ENSG00000142515; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P07288; -.
DR OMA; WIQDTIM; -.
DR PhylomeDB; P07288; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.77; 2681.
DR PathwayCommons; P07288; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR SignaLink; P07288; -.
DR SIGNOR; P07288; -.
DR BioGRID-ORCS; 354; 8 hits in 1071 CRISPR screens.
DR ChiTaRS; KLK3; human.
DR EvolutionaryTrace; P07288; -.
DR GeneWiki; Prostate-specific_antigen; -.
DR GenomeRNAi; 354; -.
DR Pharos; P07288; Tclin.
DR PRO; PR:P07288; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P07288; protein.
DR Bgee; ENSG00000142515; Expressed in prostate gland and 122 other tissues.
DR ExpressionAtlas; P07288; baseline and differential.
DR Genevisible; P07288; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IMP:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0016525; P:negative regulation of angiogenesis; NAS:UniProtKB.
DR GO; GO:0002803; P:positive regulation of antibacterial peptide production; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:15340161"
FT PROPEP 18..24
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2422647,
FT ECO:0000269|PubMed:3691515"
FT /id="PRO_0000027931"
FT CHAIN 25..261
FT /note="Prostate-specific antigen"
FT /id="PRO_0000027932"
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:0000269|PubMed:18187150"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:18187150"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:18187150"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 31..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:18187150"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:18187150"
FT DISULFID 152..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:18187150"
FT DISULFID 184..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:18187150"
FT DISULFID 209..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:18187150"
FT VAR_SEQ 69
FT /note="N -> K (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046169"
FT VAR_SEQ 70..261
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046170"
FT VAR_SEQ 70..112
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046171"
FT VAR_SEQ 211..261
FT /note="GDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVANP
FT -> WVILITELTMPALPMVLHGSLVPWRGGV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2436946"
FT /id="VSP_045786"
FT VAR_SEQ 211..260
FT /note="GDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVAN
FT -> VSHPYSQDLEGKGEWG (in isoform 5)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_047643"
FT VARIANT 32
FT /note="E -> K (in dbSNP:rs2271092)"
FT /id="VAR_021941"
FT VARIANT 132
FT /note="L -> I (in dbSNP:rs2003783)"
FT /evidence="ECO:0000269|PubMed:23842001"
FT /id="VAR_021942"
FT VARIANT 179
FT /note="I -> T (in dbSNP:rs17632542)"
FT /id="VAR_051852"
FT CONFLICT 64
FT /note="A -> T (in Ref. 15)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="N -> KC (in Ref. 6; AAA60193)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="H -> T (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="V -> M (in Ref. 15)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..168
FT /note="FLTP -> HLLYDQM (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="D -> Q (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 39..56
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2ZCH"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:2ZCH"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2ZCK"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:2ZCH"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 216..229
FT /evidence="ECO:0007829|PDB:2ZCH"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2ZCL"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2ZCH"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:2ZCH"
FT HELIX 250..258
FT /evidence="ECO:0007829|PDB:2ZCH"
SQ SEQUENCE 261 AA; 28741 MW; AE9E732AF872141A CRC64;
MWVPVVFLTL SVTWIGAAPL ILSRIVGGWE CEKHSQPWQV LVASRGRAVC GGVLVHPQWV
LTAAHCIRNK SVILLGRHSL FHPEDTGQVF QVSHSFPHPL YDMSLLKNRF LRPGDDSSHD
LMLLRLSEPA ELTDAVKVMD LPTQEPALGT TCYASGWGSI EPEEFLTPKK LQCVDLHVIS
NDVCAQVHPQ KVTKFMLCAG RWTGGKSTCS GDSGGPLVCN GVLQGITSWG SEPCALPERP
SLYTKVVHYR KWIKDTIVAN P
