ID   PRS35_MACMU             Reviewed;         409 AA.
AC   Q1WK24;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Inactive serine protease 35;
DE   Flags: Precursor;
GN   Name=PRSS35;
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}.
CC   -!- CAUTION: Although related to peptidase S1 family, lacks the conserved
CC       active Ser residue in position 342 which is replaced by a Thr,
CC       suggesting that it has no protease activity. {ECO:0000305}.
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DR   EMBL; DQ223038; ABB46198.1; -; mRNA.
DR   RefSeq; NP_001041709.1; NM_001048244.1.
DR   AlphaFoldDB; Q1WK24; -.
DR   STRING; 9544.ENSMMUP00000021956; -.
DR   MEROPS; S01.994; -.
DR   GeneID; 695095; -.
DR   KEGG; mcc:695095; -.
DR   CTD; 167681; -.
DR   eggNOG; ENOG502QV0K; Eukaryota.
DR   InParanoid; Q1WK24; -.
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   Gene3D; 2.40.10.10; -; 1.
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; Reference proteome; Secreted;
KW   Serine protease homolog; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..409
FT                   /note="Inactive serine protease 35"
FT                   /id="PRO_0000299359"
FT   DOMAIN          120..404
FT                   /note="Peptidase S1"
FT   REGION          188..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..202
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        150..166
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  46512 MW;  7A7F138C2AEB1E20 CRC64;
     MLLWLIFFTP GWTLIDGSEM QRDFTWHLRK VPRIVSERTF HLTSPTFEAD AKMMVNTVCG
     IECQKELPTP SLSELEDYLS YETVFENGTR TLTRVKVQDL VFEPTQNTTK GASVRRKRQV
     YGTDSRFSIL DKRFLTNFPF STAVKLSTGC SGILISPQHV LTAAHCVHDG KDYVKGSKKL
     RVGLLKMRNK SGGKKRRGSK RSRRETSGGD QREGPREHLQ DRVKAGRRRK QSGGGQRVSE
     GRPSFRWTRV KNTHIPKGWA RGGMGDAALD YDYALLELKR AHKKKYMELG ISPTIKKMPG
     GMIHFSGFDN DRADQLVYRF CSVSDESNDL LYQYCDAESG STGSGVYLRL KDPDKKNWKR
     KIIAVYSGHQ WVDVHGVQKD YNVAVRITPL KYAQICLWIH GNDANCAYG