PRS53_HUMAN
ID PRS53_HUMAN Reviewed; 553 AA.
AC Q2L4Q9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Serine protease 53;
DE EC=3.4.21.-;
DE AltName: Full=Polyserine protease 3;
DE Short=Polyserase-3;
DE Flags: Precursor;
GN Name=PRSS53;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal liver;
RX PubMed=16566820; DOI=10.1186/1471-2091-7-9;
RA Cal S., Peinado J.R., Llamazares M., Quesada V., Moncada-Pazos A.,
RA Garabaya C., Lopez-Otin C.;
RT "Identification and characterization of human polyserase-3, a novel protein
RT with tandem serine-protease domains in the same polypeptide chain.";
RL BMC Biochem. 7:9-9(2006).
CC -!- FUNCTION: In vitro can degrade the fibrinogen alpha chain of as well as
CC pro-urokinase-type plasminogen activator.
CC {ECO:0000269|PubMed:16566820}.
CC -!- INTERACTION:
CC Q2L4Q9; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-18393698, EBI-2514383;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16566820}.
CC -!- TISSUE SPECIFICITY: Predominantly detected in testis, liver, heart and
CC ovary, as well as in several tumor cell lines.
CC {ECO:0000269|PubMed:16566820}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AJ627035; CAF25304.1; -; mRNA.
DR CCDS; CCDS42153.1; -.
DR RefSeq; NP_001034592.1; NM_001039503.2.
DR AlphaFoldDB; Q2L4Q9; -.
DR SMR; Q2L4Q9; -.
DR BioGRID; 396747; 133.
DR IntAct; Q2L4Q9; 1.
DR STRING; 9606.ENSP00000280606; -.
DR MEROPS; S01.375; -.
DR BioMuta; PRSS53; -.
DR DMDM; 121941263; -.
DR EPD; Q2L4Q9; -.
DR MassIVE; Q2L4Q9; -.
DR PaxDb; Q2L4Q9; -.
DR PeptideAtlas; Q2L4Q9; -.
DR PRIDE; Q2L4Q9; -.
DR ProteomicsDB; 61328; -.
DR Antibodypedia; 50883; 30 antibodies from 9 providers.
DR DNASU; 339105; -.
DR Ensembl; ENST00000280606.6; ENSP00000280606.6; ENSG00000151006.7.
DR GeneID; 339105; -.
DR KEGG; hsa:339105; -.
DR MANE-Select; ENST00000280606.7; ENSP00000280606.6; NM_001039503.3; NP_001034592.1.
DR UCSC; uc002eaq.4; human.
DR CTD; 339105; -.
DR DisGeNET; 339105; -.
DR GeneCards; PRSS53; -.
DR HGNC; HGNC:34407; PRSS53.
DR HPA; ENSG00000151006; Tissue enhanced (brain, liver).
DR MIM; 610561; gene.
DR neXtProt; NX_Q2L4Q9; -.
DR OpenTargets; ENSG00000151006; -.
DR PharmGKB; PA165450635; -.
DR VEuPathDB; HostDB:ENSG00000151006; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162122; -.
DR HOGENOM; CLU_004497_4_0_1; -.
DR InParanoid; Q2L4Q9; -.
DR OMA; KWCWGPV; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q2L4Q9; -.
DR TreeFam; TF321170; -.
DR PathwayCommons; Q2L4Q9; -.
DR SignaLink; Q2L4Q9; -.
DR BioGRID-ORCS; 339105; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; PRSS53; human.
DR GenomeRNAi; 339105; -.
DR Pharos; Q2L4Q9; Tdark.
DR PRO; PR:Q2L4Q9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q2L4Q9; protein.
DR Bgee; ENSG00000151006; Expressed in right lobe of liver and 90 other tissues.
DR Genevisible; Q2L4Q9; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 2.
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; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 2.
DR SUPFAM; SSF50494; SSF50494; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Hydrolase; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..553
FT /note="Serine protease 53"
FT /id="PRO_0000316763"
FT DOMAIN 24..273
FT /note="Peptidase S1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 294..526
FT /note="Peptidase S1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 27..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 77
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 341
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 382
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 478
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 62..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 158..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 187..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 220..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 326..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 444..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 474..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 553 AA; 58410 MW; 8464159A3E65AFA7 CRC64;
MKWCWGPVLL IAGATVLMEG LQAAQRACGQ RGPGPPKPQE GNTVPGEWPW QASVRRQGAH
ICSGSLVADT WVLTAAHCFE KAAATELNSW SVVLGSLQRE GLSPGAEEVG VAALQLPRAY
NHYSQGSDLA LLQLAHPTTH TPLCLPQPAH RFPFGASCWA TGWDQDTSDA PGTLRNLRLR
LISRPTCNCI YNQLHQRHLS NPARPGMLCG GPQPGVQGPC QGDSGGPVLC LEPDGHWVQA
GIISFASSCA QEDAPVLLTN TAAHSSWLQA RVQGAAFLAQ SPETPEMSDE DSCVACGSLR
TAGPQAGAPS PWPWEARLMH QGQLACGGAL VSEEAVLTAA HCFIGRQAPE EWSVGLGTRP
EEWGLKQLIL HGAYTHPEGG YDMALLLLAQ PVTLGASLRP LCLPYPDHHL PDGERGWVLG
RARPGAGISS LQTVPVTLLG PRACSRLHAA PGGDGSPILP GMVCTSAVGE LPSCEGLSGA
PLVHEVRGTW FLAGLHSFGD ACQGPARPAV FTALPAYEDW VSSLDWQVYF AEEPEPEAEP
GSCLANISQP TSC
