TEST_HUMAN
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 03-AUG-2022, entry version 181.
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; 62.
DR IntAct; Q9Y6M0; 15.
DR MINT; Q9Y6M0; -.
DR STRING; 9606.ENSP00000005995; -.
DR MEROPS; S01.011; -.
DR GlyGen; Q9Y6M0; 3 sites.
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; Q9Y6M0; -.
DR PeptideAtlas; Q9Y6M0; -.
DR PRIDE; Q9Y6M0; -.
DR ProteomicsDB; 86721; -. [Q9Y6M0-1]
DR ProteomicsDB; 86722; -. [Q9Y6M0-2]
DR ProteomicsDB; 86723; -. [Q9Y6M0-3]
DR Antibodypedia; 1701; 60 antibodies from 16 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 Ensembl; ENST00000634351.2; ENSP00000489315.1; ENSG00000282838.2. [Q9Y6M0-1]
DR Ensembl; ENST00000634454.1; ENSP00000489081.1; ENSG00000282838.2. [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 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; GPCGHRT; -.
DR OrthoDB; 1314811at2759; -.
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; 20 hits in 1074 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 86 other tissues.
DR ExpressionAtlas; Q9Y6M0; baseline and differential.
DR Genevisible; Q9Y6M0; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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: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; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR034380; Testisin.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24256:SF173; PTHR24256:SF173; 1.
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 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
