ID   PEPC_MOUSE              Reviewed;         392 AA.
AC   Q9D7R7; Q9D7T2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Gastricsin;
DE            EC=3.4.23.3;
DE   AltName: Full=Pepsinogen C;
DE   Flags: Precursor;
GN   Name=Pgc; Synonyms=Upg1;
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; TISSUE=Stomach;
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=Placenta;
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   -!- FUNCTION: Hydrolyzes a variety of proteins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=More restricted specificity than pepsin A, but shows
CC         preferential cleavage at Tyr-|-Xaa bonds. High activity on
CC         hemoglobin.; EC=3.4.23.3;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB25952.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK008959; BAB25990.1; -; mRNA.
DR   EMBL; AK008886; BAB25952.1; ALT_FRAME; mRNA.
DR   EMBL; BC099409; AAH99409.1; -; mRNA.
DR   CCDS; CCDS28855.1; -.
DR   RefSeq; NP_080249.2; NM_025973.3.
DR   AlphaFoldDB; Q9D7R7; -.
DR   SMR; Q9D7R7; -.
DR   STRING; 10090.ENSMUSP00000024782; -.
DR   MEROPS; A01.003; -.
DR   PhosphoSitePlus; Q9D7R7; -.
DR   PaxDb; 10090-ENSMUSP00000024782; -.
DR   ProteomicsDB; 287915; -.
DR   Antibodypedia; 15914; 535 antibodies from 29 providers.
DR   DNASU; 109820; -.
DR   Ensembl; ENSMUST00000024782.12; ENSMUSP00000024782.6; ENSMUSG00000023987.15.
DR   GeneID; 109820; -.
DR   KEGG; mmu:109820; -.
DR   UCSC; uc008cwb.1; mouse.
DR   AGR; MGI:98909; -.
DR   CTD; 5225; -.
DR   MGI; MGI:98909; Pgc.
DR   VEuPathDB; HostDB:ENSMUSG00000023987; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000160626; -.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   InParanoid; Q9D7R7; -.
DR   OMA; KWMVLAL; -.
DR   OrthoDB; 1120702at2759; -.
DR   PhylomeDB; Q9D7R7; -.
DR   TreeFam; TF314990; -.
DR   BioGRID-ORCS; 109820; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Pgc; mouse.
DR   PRO; PR:Q9D7R7; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9D7R7; Protein.
DR   Bgee; ENSMUSG00000023987; Expressed in pyloric antrum and 35 other cell types or tissues.
DR   ExpressionAtlas; Q9D7R7; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; ISO:MGI.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0002803; P:positive regulation of antibacterial peptide production; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   Gene3D; 6.10.140.60; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF72; GASTRICSIN; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
DR   Genevisible; Q9D7R7; MM.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; Digestion; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..62
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026063"
FT   CHAIN           63..392
FT                   /note="Gastricsin"
FT                   /id="PRO_0000026064"
FT   DOMAIN          76..389
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        107..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..275
FT                   /evidence="ECO:0000250"
FT   DISULFID        314..347
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   392 AA;  42849 MW;  0D19D87E4683C848 CRC64;
     MKWMVVALLC LPLLEAALIR VPLKKMKSIR ETMKEQGVLK DFLKNHKYDP GQKYHFGKFG
     DYSVLYEPMA YMDASYYGEI SIGTPPQNFL VLFDTGSSNL WVSSVYCQSE ACTTHTRYNP
     SKSSTYYTQG QTFSLQYGTG SLTGFFGYDT LRVQSIQVPN QEFGLSENEP GTNFVYAQFD
     GIMGLAYPGL SSGGATTALQ GMLGEGALSQ PLFGVYLGSQ QGSNGGQIVF GGVDENLYTG
     ELTWIPVTQE LYWQITIDDF LIGNQASGWC SSSGCQGIVD TGTSLLVMPA QYLNELLQTI
     GAQEGEYGQY FVSCDSVSSL PTLTFVLNGV QFPLSPSSYI IQEEGSCMVG LESLSLNAES
     GQPLWILGDV FLRSYYAVFD MGNNRVGLAP SV
//