ID   PRS23_MACMU             Reviewed;         383 AA.
AC   Q1WK23;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Serine protease 23;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=PRSS23;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=16870946; DOI=10.1095/biolreprod.106.052290;
RA   Miyakoshi K., Murphy M.J., Yeoman R.R., Mitra S., Dubay C.J.,
RA   Hennebold J.D.;
RT   "The identification of novel ovarian proteases through the use of genomic
RT   and bioinformatic methodologies.";
RL   Biol. Reprod. 75:823-835(2006).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; DQ223039; ABB46199.1; -; mRNA.
DR   RefSeq; NP_001038202.1; NM_001044737.1.
DR   RefSeq; XP_014970783.1; XM_015115297.1.
DR   AlphaFoldDB; Q1WK23; -.
DR   STRING; 9544.ENSMMUP00000004958; -.
DR   GeneID; 704537; -.
DR   KEGG; mcc:704537; -.
DR   CTD; 11098; -.
DR   eggNOG; ENOG502QTW6; Eukaryota.
DR   HOGENOM; CLU_055829_0_0_1; -.
DR   InParanoid; Q1WK23; -.
DR   OMA; RQQQKWE; -.
DR   OrthoDB; 1245017at2759; -.
DR   TreeFam; TF329011; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   Pfam; PF00089; Trypsin; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Phosphoprotein; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..383
FT                   /note="Serine protease 23"
FT                   /id="PRO_0000299362"
FT   REGION          108..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        175
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10078"
FT   ACT_SITE        240
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10078"
FT   ACT_SITE        316
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10078"
FT   MOD_RES         109
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000250|UniProtKB:O95084"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        160..176
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   383 AA;  42882 MW;  30A1799D6C6E9791 CRC64;
     MAGIPGLLFL LFLLLCAVGQ VSPYSAPWKP TWPAYRLPVV LPQSTLSLAK PDFGAEAKLE
     VSSSCGPQCH KGTPLPTYEE AKQYLSYETL YANGSRTETQ VGIYILSSSG GGAQHRDSGS
     SGKSRRKRQI YGYDSRFSIF GKDFLLNYPF STSVKLSTGC TGTLVAEKHV LTAAHCIHDG
     KTYVKGTQKL RVGFLKPKFK DGGRGANDST SAMPEKMKFQ WIRVKRTHVP KGWIKGNAND
     IGMDYDYALL ELKKPHKRKF MKIGVSPPAK QLPGGRIHFS GYDNDRPGNL VYRFCDVKDE
     TYDLLYQQCD AQPGASGSGV YVRMWKRQQQ KWERKIIGIF SGHQWVDMNG SPQDFNVAVR
     ITPLKYAQIC YWIKGNYLDC REG