PRS53_MOUSE
ID PRS53_MOUSE Reviewed; 552 AA.
AC Q571E5; Q8CFX9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-552.
RC STRAIN=FVB/N; TISSUE=Liver;
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: In vitro can degrade the fibrinogen alpha chain of as well as
CC pro-urokinase-type plasminogen activator. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39632.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD90169.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK220244; BAD90169.1; ALT_INIT; mRNA.
DR EMBL; BC039632; AAH39632.1; ALT_INIT; mRNA.
DR CCDS; CCDS52409.1; -.
DR RefSeq; NP_001074737.1; NM_001081268.1.
DR RefSeq; XP_017177807.1; XM_017322318.1.
DR AlphaFoldDB; Q571E5; -.
DR SMR; Q571E5; -.
DR STRING; 10090.ENSMUSP00000112972; -.
DR MEROPS; S01.374; -.
DR PaxDb; Q571E5; -.
DR PRIDE; Q571E5; -.
DR ProteomicsDB; 291680; -.
DR Antibodypedia; 50883; 30 antibodies from 9 providers.
DR DNASU; 330657; -.
DR Ensembl; ENSMUST00000121394; ENSMUSP00000112972; ENSMUSG00000044139.
DR GeneID; 330657; -.
DR KEGG; mmu:330657; -.
DR UCSC; uc009jxd.1; mouse.
DR CTD; 339105; -.
DR MGI; MGI:2652890; Prss53.
DR VEuPathDB; HostDB:ENSMUSG00000044139; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162122; -.
DR HOGENOM; CLU_004497_4_0_1; -.
DR InParanoid; Q571E5; -.
DR OMA; KWCWGPV; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q571E5; -.
DR TreeFam; TF321170; -.
DR BioGRID-ORCS; 330657; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Prss53; mouse.
DR PRO; PR:Q571E5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q571E5; protein.
DR Bgee; ENSMUSG00000044139; Expressed in islet of Langerhans and 57 other tissues.
DR ExpressionAtlas; Q571E5; baseline and differential.
DR Genevisible; Q571E5; MM.
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 2: Evidence at transcript 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..552
FT /note="Serine protease 53"
FT /id="PRO_0000316764"
FT DOMAIN 24..273
FT /note="Peptidase S1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 294..525
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 477
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 443..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 473..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 552 AA; 58974 MW; 4E605F7BA1AB8A91 CRC64;
MRQSWRPELL IVGAVVVIEG LQAAQRACGQ RGPGPPEPQE GNTLPGEWPW QASVRRQGVH
ICSGSLVADT WVLTAAHCFE KMATAELSSW SVVLGSLKQE GQSPGAEEVG VAALQLPKAY
NHYSQGSDLA LLQLTHPTVQ TTLCLPQPTY HFPFGASCWA TGWDQNTSDV SRTLRNLRLR
LISRPTCNCL YNRLHQRLLS NPARPGMLCG GAQPGEQGPC QGDSGGPVMC REPDGHWVQV
GIISFTSKCA QEDTPVLLTD MAVHSSWLQA HVHEAAFLVQ APGVVKMSDE NSCVACGSLR
SAGPQAGALS QWPWDARLKH HGKLACGGAL VSEVVVLTAA HCFIGRQTLE EWSVGLGAGP
EEWGLKQLIL HGAYTHPEGG YDVAFLLLAQ PVTLGPGLRP LCLPYADHHL PDGEHGWVLG
LTQKAGINYP QTVPVTVLGP MACSRQHAAP GGTGIPILPG MVCTTVVGEP PHCEGLSGAP
LVHEIRGTWF LVGLHSFGDT CQSSAKPAVF AALSAYEDWI SNLDWQVYFA EEPEPEAETG
SCLVNSSQPA SC
