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PRS38_MOUSE
ID   PRS38_MOUSE             Reviewed;         322 AA.
AC   Q3UKY7; B9EJM8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Serine protease 38;
DE            EC=3.4.21.-;
DE   AltName: Full=Marapsin-2;
DE   Flags: Precursor;
GN   Name=Prss38; Synonyms=Gm249, Mpn2;
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   STRAIN=C57BL/6J;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AK145810; BAE26664.1; -; mRNA.
DR   EMBL; BC147400; AAI47401.1; -; mRNA.
DR   EMBL; BC147401; AAI47402.1; -; mRNA.
DR   CCDS; CCDS36170.1; -.
DR   RefSeq; NP_001038986.1; NM_001045521.1.
DR   AlphaFoldDB; Q3UKY7; -.
DR   SMR; Q3UKY7; -.
DR   STRING; 10090.ENSMUSP00000052010; -.
DR   MEROPS; S01.324; -.
DR   GlyGen; Q3UKY7; 3 sites.
DR   PhosphoSitePlus; Q3UKY7; -.
DR   PaxDb; Q3UKY7; -.
DR   PRIDE; Q3UKY7; -.
DR   ProteomicsDB; 291903; -.
DR   Antibodypedia; 20773; 30 antibodies from 11 providers.
DR   DNASU; 216797; -.
DR   Ensembl; ENSMUST00000061481; ENSMUSP00000052010; ENSMUSG00000049291.
DR   GeneID; 216797; -.
DR   KEGG; mmu:216797; -.
DR   UCSC; uc007jdr.1; mouse.
DR   CTD; 339501; -.
DR   MGI; MGI:2685095; Prss38.
DR   VEuPathDB; HostDB:ENSMUSG00000049291; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000154494; -.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; Q3UKY7; -.
DR   OMA; TACEGDS; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q3UKY7; -.
DR   TreeFam; TF351676; -.
DR   BioGRID-ORCS; 216797; 0 hits in 72 CRISPR screens.
DR   PRO; PR:Q3UKY7; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q3UKY7; protein.
DR   Bgee; ENSMUSG00000049291; Expressed in spermatocyte and 9 other tissues.
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; IBA:GO_Central.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
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; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..55
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000328822"
FT   CHAIN           56..322
FT                   /note="Serine protease 38"
FT                   /id="PRO_0000328823"
FT   DOMAIN          56..289
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        96
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        146
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        241
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        81..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        179..247
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        210..226
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        237..265
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   322 AA;  35698 MW;  0073C08E70FFF674 CRC64;
     MAALTSGLGV LGYLLFPLLL ASPTWVTSVS RRHPKSQANS LSGDVACGQP VLQGKLLGGE
     FARDRKWPWQ VSLHYSGFHI CGGSILSAYW VLSAAHCFDR GKKLETYDIY VGITNLEKAN
     RHTQWFEIYQ VIIHPTFQMY HPIGGDVALV QLKSAIVFSD FVLPICLPPS DLYLINLSCW
     TTGWGMISPQ GETGNELLEA QLPLIPRFQC QLLYGLSSYL LPEMLCAADI KTMKNVCEGD
     SGSPLVCKQN QTWLQIGIVS WGRGCAQPLY PGVFANVSYF LSWIRYHLQI IPNPPQILPS
     LSSSPKNTLI IFVTIMGHLL VL
 
 
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