ID   TEST_HUMAN              Reviewed;         314 AA.
AC   Q9Y6M0; Q9NS34; Q9P2V6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Testisin;
DE            EC=3.4.21.-;
DE   AltName: Full=Eosinophil serine protease 1;
DE            Short=ESP-1;
DE   AltName: Full=Serine protease 21;
DE   Flags: Precursor;
GN   Name=PRSS21; Synonyms=ESP1, TEST1; ORFNames=UNQ266/PRO303;
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 (ISOFORM 1).
RC   TISSUE=Eosinophil;
RX   PubMed=9826525; DOI=10.1006/bbrc.1998.9645;
RA   Inoue M., Kanbe N., Kurosawa M., Kido H.;
RT   "Cloning and tissue distribution of a novel serine protease esp-1 from
RT   human eosinophils.";
RL   Biochem. Biophys. Res. Commun. 252:307-312(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX   PubMed=10600542; DOI=10.1006/bbrc.1999.1870;
RA   Inoue M., Isobe M., Itoyama T., Kido H.;
RT   "Structural analysis of esp-1 gene (PRSS 21).";
RL   Biochem. Biophys. Res. Commun. 266:564-568(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RC   TISSUE=Cervix carcinoma;
RX   PubMed=10397266;
RA   Hooper J.D., Nicol D.L., Dickinson J.L., Eyre H.J., Scarman A.L.,
RA   Normyle J.F., Stuttgen M.A., Douglas M.L., Loveland K.A., Sutherland G.R.,
RA   Antalis T.M.;
RT   "Testisin, a new human serine proteinase expressed by premeiotic testicular
RT   germ cells and lost in testicular germ cell tumors.";
RL   Cancer Res. 59:3199-3205(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11004480; DOI=10.1016/s0167-4781(00)00071-3;
RA   Hooper J.D., Bowen N., Marshall H., Cullen L.M., Sood R., Daniels R.,
RA   Stuttgen M.A., Normyle J.F., Higgs D.R., Kastner D.L., Ogbourne S.M.,
RA   Pera M.F., Jazwinska E.C., Antalis T.M.;
RT   "Localization, expression and genomic structure of the gene encoding the
RT   human serine protease testisin.";
RL   Biochim. Biophys. Acta 1492:63-71(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
CC   -!- FUNCTION: Could regulate proteolytic events associated with testicular
CC       germ cell maturation.
CC   -!- INTERACTION:
CC       Q9Y6M0; P36952: SERPINB5; NbExp=7; IntAct=EBI-7054564, EBI-2371394;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=L;
CC         IsoId=Q9Y6M0-1; Sequence=Displayed;
CC       Name=2; Synonyms=S;
CC         IsoId=Q9Y6M0-2; Sequence=VSP_005389;
CC       Name=3;
CC         IsoId=Q9Y6M0-3; Sequence=VSP_005390;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in premeiotic testicular
CC       germ cells, mostly late pachytene and diplotene spermatocytes.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AF058300; AAD41588.1; -; mRNA.
DR   EMBL; AB031329; BAA83520.1; -; mRNA.
DR   EMBL; AB031330; BAA83521.1; -; mRNA.
DR   EMBL; AB031331; BAA89532.1; -; mRNA.
DR   EMBL; AF058301; AAF79019.1; -; Genomic_DNA.
DR   EMBL; AF058301; AAF79020.1; -; Genomic_DNA.
DR   EMBL; AY359034; AAQ89393.1; -; mRNA.
DR   EMBL; BC074999; AAH74999.1; -; mRNA.
DR   EMBL; BC075000; AAH75000.1; -; mRNA.
DR   CCDS; CCDS10478.1; -. [Q9Y6M0-1]
DR   CCDS; CCDS45388.1; -. [Q9Y6M0-3]
DR   RefSeq; NP_001257381.1; NM_001270452.1.
DR   RefSeq; NP_006790.1; NM_006799.3. [Q9Y6M0-1]
DR   RefSeq; NP_659205.1; NM_144956.2. [Q9Y6M0-2]
DR   RefSeq; NP_659206.1; NM_144957.2. [Q9Y6M0-3]
DR   AlphaFoldDB; Q9Y6M0; -.
DR   SMR; Q9Y6M0; -.
DR   BioGRID; 116142; 65.
DR   IntAct; Q9Y6M0; 15.
DR   MINT; Q9Y6M0; -.
DR   STRING; 9606.ENSP00000005995; -.
DR   MEROPS; S01.011; -.
DR   GlyCosmos; Q9Y6M0; 3 sites, No reported glycans.
DR   GlyGen; Q9Y6M0; 4 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y6M0; -.
DR   PhosphoSitePlus; Q9Y6M0; -.
DR   BioMuta; PRSS21; -.
DR   DMDM; 13633973; -.
DR   EPD; Q9Y6M0; -.
DR   jPOST; Q9Y6M0; -.
DR   MassIVE; Q9Y6M0; -.
DR   MaxQB; Q9Y6M0; -.
DR   PaxDb; 9606-ENSP00000005995; -.
DR   PeptideAtlas; Q9Y6M0; -.
DR   ProteomicsDB; 86721; -. [Q9Y6M0-1]
DR   ProteomicsDB; 86722; -. [Q9Y6M0-2]
DR   ProteomicsDB; 86723; -. [Q9Y6M0-3]
DR   Pumba; Q9Y6M0; -.
DR   Antibodypedia; 1701; 74 antibodies from 17 providers.
DR   DNASU; 10942; -.
DR   Ensembl; ENST00000005995.8; ENSP00000005995.3; ENSG00000007038.11. [Q9Y6M0-1]
DR   Ensembl; ENST00000450020.7; ENSP00000407741.3; ENSG00000007038.11. [Q9Y6M0-3]
DR   GeneID; 10942; -.
DR   KEGG; hsa:10942; -.
DR   MANE-Select; ENST00000005995.8; ENSP00000005995.3; NM_006799.4; NP_006790.1.
DR   UCSC; uc002crr.5; human. [Q9Y6M0-1]
DR   AGR; HGNC:9485; -.
DR   CTD; 10942; -.
DR   DisGeNET; 10942; -.
DR   GeneCards; PRSS21; -.
DR   HGNC; HGNC:9485; PRSS21.
DR   HPA; ENSG00000007038; Tissue enriched (testis).
DR   MIM; 608159; gene.
DR   neXtProt; NX_Q9Y6M0; -.
DR   OpenTargets; ENSG00000007038; -.
DR   PharmGKB; PA33834; -.
DR   VEuPathDB; HostDB:ENSG00000007038; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000155138; -.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; Q9Y6M0; -.
DR   OMA; SGWTIQF; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; Q9Y6M0; -.
DR   TreeFam; TF351676; -.
DR   PathwayCommons; Q9Y6M0; -.
DR   Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   SignaLink; Q9Y6M0; -.
DR   SIGNOR; Q9Y6M0; -.
DR   BioGRID-ORCS; 10942; 22 hits in 1152 CRISPR screens.
DR   ChiTaRS; PRSS21; human.
DR   GenomeRNAi; 10942; -.
DR   Pharos; Q9Y6M0; Tbio.
DR   PRO; PR:Q9Y6M0; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9Y6M0; Protein.
DR   Bgee; ENSG00000007038; Expressed in right testis and 88 other cell types or tissues.
DR   ExpressionAtlas; Q9Y6M0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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   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.
DR   Genevisible; Q9Y6M0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..41
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027849"
FT   CHAIN           42..288
FT                   /note="Testisin"
FT                   /id="PRO_0000027850"
FT   PROPEP          289..314
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027851"
FT   DOMAIN          42..286
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        82
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        137
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        238
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   LIPID           288
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        67..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        171..244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        204..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        234..262
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   VAR_SEQ         87..88
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005389"
FT   VAR_SEQ         222..235
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10600542"
FT                   /id="VSP_005390"
FT   VARIANT         264
FT                   /note="R -> Q (in dbSNP:rs2072273)"
FT                   /id="VAR_051840"
SQ   SEQUENCE   314 AA;  34884 MW;  E738CF73F6B56E98 CRC64;
     MGARGALLLA LLLARAGLRK PESQEAAPLS GPCGRRVITS RIVGGEDAEL GRWPWQGSLR
     LWDSHVCGVS LLSHRWALTA AHCFETYSDL SDPSGWMVQF GQLTSMPSFW SLQAYYTRYF
     VSNIYLSPRY LGNSPYDIAL VKLSAPVTYT KHIQPICLQA STFEFENRTD CWVTGWGYIK
     EDEALPSPHT LQEVQVAIIN NSMCNHLFLK YSFRKDIFGD MVCAGNAQGG KDACFGDSGG
     PLACNKNGLW YQIGVVSWGV GCGRPNRPGV YTNISHHFEW IQKLMAQSGM SQPDPSWPLL
     FFPLLWALPL LGPV
//