TSP50_HUMAN
ID TSP50_HUMAN Reviewed; 385 AA.
AC Q9UI38;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable threonine protease PRSS50;
DE EC=3.4.25.- {ECO:0000269|PubMed:17283160};
DE AltName: Full=Cancer/testis antigen 20;
DE AltName: Full=Serine protease 50;
DE AltName: Full=Testis-specific protease-like protein 50;
DE Flags: Precursor;
GN Name=PRSS50; Synonyms=CT20, TSP50;
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].
RC TISSUE=Mammary cancer;
RX PubMed=10397268;
RA Yuan L., Shan J., De Risi D., Broome J., Lovecchio J., Gal D.,
RA Vinciguerra V., Xu H.-P.;
RT "Isolation of a novel gene, TSP50, by a hypomethylated DNA fragment in
RT human breast cancer.";
RL Cancer Res. 59:3215-3221(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-310.
RX PubMed=17283160; DOI=10.1158/0008-5472.can-06-3688;
RA Xu H., Shan J., Jurukovski V., Yuan L., Li J., Tian K.;
RT "TSP50 encodes a testis-specific protease and is negatively regulated by
RT p53.";
RL Cancer Res. 67:1239-1245(2007).
CC -!- FUNCTION: May be involved in proteolysis through its threonine
CC endopeptidase activity. {ECO:0000269|PubMed:17283160}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000305|PubMed:17283160}. Note=May also localize to cytoplasmic
CC membranes.
CC -!- TISSUE SPECIFICITY: Testis specific. Differentially expressed in some
CC breast cancer tissues.
CC -!- MISCELLANEOUS: DNA hypomethylation is accompanied by the expression of
CC the gene in the testis.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Although related to peptidase S1 family, lacks the conserved
CC active Ser residue in position 310 which is replaced by a Thr.
CC {ECO:0000305}.
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DR EMBL; AF100707; AAF22500.1; -; mRNA.
DR EMBL; BC033016; AAH33016.1; -; mRNA.
DR EMBL; BC037775; AAH37775.1; -; mRNA.
DR CCDS; CCDS2745.1; -.
DR RefSeq; NP_037402.1; NM_013270.4.
DR AlphaFoldDB; Q9UI38; -.
DR SMR; Q9UI38; -.
DR BioGRID; 118887; 49.
DR IntAct; Q9UI38; 18.
DR MINT; Q9UI38; -.
DR STRING; 9606.ENSP00000418875; -.
DR MEROPS; S01.993; -.
DR GlyGen; Q9UI38; 2 sites.
DR iPTMnet; Q9UI38; -.
DR PhosphoSitePlus; Q9UI38; -.
DR BioMuta; PRSS50; -.
DR DMDM; 37089988; -.
DR MassIVE; Q9UI38; -.
DR PaxDb; Q9UI38; -.
DR PeptideAtlas; Q9UI38; -.
DR PRIDE; Q9UI38; -.
DR ProteomicsDB; 84468; -.
DR Antibodypedia; 78661; 55 antibodies from 9 providers.
DR DNASU; 29122; -.
DR Ensembl; ENST00000315170.13; ENSP00000326598.7; ENSG00000283706.2.
DR GeneID; 29122; -.
DR KEGG; hsa:29122; -.
DR MANE-Select; ENST00000315170.13; ENSP00000326598.7; NM_013270.5; NP_037402.1.
DR UCSC; uc003cqe.2; human.
DR CTD; 29122; -.
DR DisGeNET; 29122; -.
DR GeneCards; PRSS50; -.
DR HGNC; HGNC:17910; PRSS50.
DR HPA; ENSG00000283706; Group enriched (pituitary gland, testis, thyroid gland).
DR MIM; 607950; gene.
DR neXtProt; NX_Q9UI38; -.
DR OpenTargets; ENSG00000206549; -.
DR PharmGKB; PA165698443; -.
DR VEuPathDB; HostDB:ENSG00000206549; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162593; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q9UI38; -.
DR OMA; EQFCYEL; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9UI38; -.
DR TreeFam; TF351676; -.
DR PathwayCommons; Q9UI38; -.
DR SignaLink; Q9UI38; -.
DR BioGRID-ORCS; 29122; 41 hits in 1059 CRISPR screens.
DR GenomeRNAi; 29122; -.
DR Pharos; Q9UI38; Tbio.
DR PRO; PR:Q9UI38; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UI38; protein.
DR Bgee; ENSG00000283706; Expressed in right testis and 88 other tissues.
DR ExpressionAtlas; Q9UI38; baseline.
DR Genevisible; Q9UI38; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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 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.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Threonine protease.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..385
FT /note="Probable threonine protease PRSS50"
FT /id="PRO_0000028492"
FT DOMAIN 93..358
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 138..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 240..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 273..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 306..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 75
FT /note="Q -> P (in dbSNP:rs34788938)"
FT /id="VAR_051859"
FT VARIANT 98
FT /note="V -> I (in dbSNP:rs35866901)"
FT /id="VAR_051860"
FT MUTAGEN 310
FT /note="T->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17283160"
SQ SEQUENCE 385 AA; 43088 MW; F5B39D6E12798AE5 CRC64;
MGRWCQTVAR GQRPRTSAPS RAGALLLLLL LLRSAGCWGA GEAPGALSTA DPADQSVQCV
PKATCPSSRP RLLWQTPTTQ TLPSTTMETQ FPVSEGKVDP YRSCGFSYEQ DPTLRDPEAV
ARRWPWMVSV RANGTHICAG TIIASQWVLT VAHCLIWRDV IYSVRVGSPW IDQMTQTASD
VPVLQVIMHS RYRAQRFWSW VGQANDIGLL KLKQELKYSN YVRPICLPGT DYVLKDHSRC
TVTGWGLSKA DGMWPQFRTI QEKEVIILNN KECDNFYHNF TKIPTLVQII KSQMMCAEDT
HREKFCYELT GEPLVCSMEG TWYLVGLVSW GAGCQKSEAP PIYLQVSSYQ HWIWDCLNGQ
ALALPAPSRT LLLALPLPLS LLAAL