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PRS35_MOUSE
ID   PRS35_MOUSE             Reviewed;         409 AA.
AC   Q8C0F9; Q8C0D6; Q8C0L5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Inactive serine protease 35;
DE   Flags: Precursor;
GN   Name=Prss35;
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RC   STRAIN=C57BL/6J; 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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: In ovary, it localizes to the theca cells of pre-
CC       antral follicles, the theca and granulosa cells of pre-ovulatory and
CC       ovulatory follicles, as well as to the developing corpus luteum.
CC       {ECO:0000269|PubMed:16870946}.
CC   -!- DEVELOPMENTAL STAGE: Increases around the time of ovulation and
CC       remained elevated in the developing corpus luteum.
CC       {ECO:0000269|PubMed:16870946}.
CC   -!- INDUCTION: Expression is progesterone-dependent regulation prior to
CC       follicle rupture. {ECO:0000269|PubMed:16870946}.
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; DQ223037; ABB46197.1; -; mRNA.
DR   EMBL; AK030671; BAC27073.1; -; mRNA.
DR   EMBL; AK031411; BAC27392.1; -; mRNA.
DR   EMBL; AK031644; BAC27491.1; -; mRNA.
DR   EMBL; BC075675; AAH75675.1; -; mRNA.
DR   CCDS; CCDS40714.1; -.
DR   RefSeq; NP_848853.2; NM_178738.3.
DR   RefSeq; XP_006511233.1; XM_006511170.3.
DR   RefSeq; XP_006511234.1; XM_006511171.3.
DR   RefSeq; XP_006511235.1; XM_006511172.3.
DR   AlphaFoldDB; Q8C0F9; -.
DR   STRING; 10090.ENSMUSP00000035271; -.
DR   MEROPS; S01.994; -.
DR   GlyGen; Q8C0F9; 1 site.
DR   PhosphoSitePlus; Q8C0F9; -.
DR   PaxDb; Q8C0F9; -.
DR   PRIDE; Q8C0F9; -.
DR   ProteomicsDB; 291902; -.
DR   Antibodypedia; 31685; 82 antibodies from 19 providers.
DR   DNASU; 244954; -.
DR   Ensembl; ENSMUST00000036426; ENSMUSP00000035271; ENSMUSG00000033491.
DR   Ensembl; ENSMUST00000179574; ENSMUSP00000137445; ENSMUSG00000033491.
DR   GeneID; 244954; -.
DR   KEGG; mmu:244954; -.
DR   UCSC; uc012gxu.1; mouse.
DR   CTD; 167681; -.
DR   MGI; MGI:2444800; Prss35.
DR   VEuPathDB; HostDB:ENSMUSG00000033491; -.
DR   eggNOG; ENOG502QV0K; Eukaryota.
DR   GeneTree; ENSGT00390000000155; -.
DR   HOGENOM; CLU_055829_0_0_1; -.
DR   InParanoid; Q8C0F9; -.
DR   OMA; MEQDFMW; -.
DR   OrthoDB; 1245017at2759; -.
DR   PhylomeDB; Q8C0F9; -.
DR   TreeFam; TF329011; -.
DR   BioGRID-ORCS; 244954; 2 hits in 73 CRISPR screens.
DR   PRO; PR:Q8C0F9; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8C0F9; protein.
DR   Bgee; ENSMUSG00000033491; Expressed in adrenal gland and 118 other tissues.
DR   Genevisible; Q8C0F9; MM.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   Gene3D; 2.40.10.10; -; 4.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..409
FT                   /note="Inactive serine protease 35"
FT                   /id="PRO_0000299360"
FT   DOMAIN          124..404
FT                   /note="Peptidase S1"
FT   REGION          188..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..205
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        154..170
FT                   /evidence="ECO:0000250"
FT   CONFLICT        169
FT                   /note="H -> N (in Ref. 2; BAC27491)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        266
FT                   /note="G -> S (in Ref. 2; BAC27073)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="R -> Q (in Ref. 2; BAC27491)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        383
FT                   /note="V -> E (in Ref. 2; BAC27073)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   409 AA;  45787 MW;  6E22D4A908E7EFE5 CRC64;
     MENTLLWLVI LIPGWALSDG SETELDFTWH LSRIPQVVSE NTIHLASPTF QADAGVVKAT
     VCGIECQEEL PAPSLSQLEE SLSYETIFEN GTRTLTRVKV QGLVLEPTRN SSVKGAHPRR
     RRQVYGTDSR FSILDKRFAT NFPFNTAVKL STGCSGTLVS PNHVLTAAHC VHDGKDYVKG
     SKKLRVGVLK MRNKGGRKKR RGSKRSRREA ESAGQSQAHL RESTTQRPGK KSRRGPRVTQ
     GRPSFQWTRV KSTHIPKGWV RGENGGLALD YDYALLELKR AHKQQHMELG VSPTITKLPG
     GRIHFSGFDN DRDEQLVYRF CSVSEESNDL LYQYCDAEAG STGSGIYLRL KEPGQKNWKR
     KIVAVYSGHQ WVDVHGVQKD YNVAVRITPL KYAQICLWIH GNAANCAYG
 
 
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