ID   PRS35_RAT               Reviewed;         406 AA.
AC   Q5R212;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Inactive serine protease 35;
DE   Flags: Precursor;
GN   Name=Prss35;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yoshino M., Mizutani T., Yamada K., Yazawa T., Ogata H., Sekiguchi T.,
RA   Kajitani T., Miyamoto K.;
RT   "Rat novel serine protease.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 339 which is replaced by a Thr,
CC       suggesting that it has no protease activity. {ECO:0000305}.
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DR   EMBL; AB180912; BAD74162.1; -; mRNA.
DR   RefSeq; NP_001008560.1; NM_001008560.1.
DR   AlphaFoldDB; Q5R212; -.
DR   STRING; 10116.ENSRNOP00000036136; -.
DR   GlyGen; Q5R212; 1 site.
DR   iPTMnet; Q5R212; -.
DR   PhosphoSitePlus; Q5R212; -.
DR   PaxDb; Q5R212; -.
DR   GeneID; 315866; -.
DR   KEGG; rno:315866; -.
DR   UCSC; RGD:1311282; rat.
DR   CTD; 167681; -.
DR   RGD; 1311282; Prss35.
DR   eggNOG; ENOG502QV0K; Eukaryota.
DR   InParanoid; Q5R212; -.
DR   PhylomeDB; Q5R212; -.
DR   PRO; PR:Q5R212; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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..406
FT                   /note="Inactive serine protease 35"
FT                   /id="PRO_0000299361"
FT   DOMAIN          121..401
FT                   /note="Peptidase S1"
FT   REGION          186..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..202
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        151..167
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   406 AA;  45496 MW;  61F9C9A0E896EEB2 CRC64;
     MLLWLIIFVS GWTLSLGSET EPDFTWHLSR IPQVVSEKTI HLASPTFQAD AAAVKATVCG
     IECQEELPAP SLSQLEDFLS YETVFENGTR TLTRVKVQGL VLEPTQNSSI KGARPRRRRQ
     VYGTDSRFSI LDKRFLTNFP FNTAVKLSTG CSGALVSPNH VLTAAHCVHD GKDYVKGSKK
     LRVGVLKMRN KGGRKKRRGS RRSRREAESG GQSPEHPQES TTQRPGKKSR RGPRVAQGRP
     SFQWTRVKST HIPKGWARGE NGDPALDFDY ALLELKRAQK QQYMELGVSP TISKLPGGRI
     HFSGFDNDRD DQLVYRFCSV SEESNDLLYQ YCDAEAGSTG SGIYLRLKEP GQKNWKRKII
     AVYSGHQWVD VHGVQKDYNV AVRITPLKYA QICLWIHGNA ANCAYG