PEPC_MOUSE
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 03-AUG-2022, entry version 138.
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; Q9D7R7; -.
DR PRIDE; Q9D7R7; -.
DR ProteomicsDB; 287915; -.
DR Antibodypedia; 15914; 485 antibodies from 29 providers.
DR DNASU; 109820; -.
DR Ensembl; ENSMUST00000024782; ENSMUSP00000024782; ENSMUSG00000023987.
DR GeneID; 109820; -.
DR KEGG; mmu:109820; -.
DR UCSC; uc008cwb.1; mouse.
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; LSNNGYC; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; Q9D7R7; -.
DR TreeFam; TF314990; -.
DR BioGRID-ORCS; 109820; 2 hits in 74 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 34 other tissues.
DR ExpressionAtlas; Q9D7R7; baseline and differential.
DR Genevisible; Q9D7R7; MM.
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; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033735; Gastricsin.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR13683; PTHR13683; 1.
DR PANTHER; PTHR13683:SF292; PTHR13683:SF292; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
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
