GenomeNet

Database: UniProt
Entry: G7MPA3_MACMU
LinkDB: G7MPA3_MACMU
Original site: G7MPA3_MACMU 
ID   G7MPA3_MACMU            Unreviewed;       388 AA.
AC   G7MPA3; A0A1D5Q3Y2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Gastricsin {ECO:0000256|ARBA:ARBA00023821};
DE            EC=3.4.23.3 {ECO:0000256|ARBA:ARBA00023796};
DE   AltName: Full=Pepsinogen C {ECO:0000256|ARBA:ARBA00033248};
GN   Name=PGC {ECO:0000313|Ensembl:ENSMMUP00000042745.1,
GN   ECO:0000313|VGNC:VGNC:83442};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000042745.1, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000042745.1}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000042745.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Hydrolyzes a variety of proteins.
CC       {ECO:0000256|ARBA:ARBA00023749}.
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; Evidence={ECO:0000256|ARBA:ARBA00023733};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_014991818.1; XM_015136332.1.
DR   AlphaFoldDB; G7MPA3; -.
DR   SMR; G7MPA3; -.
DR   STRING; 9544.ENSMMUP00000042745; -.
DR   MEROPS; A01.003; -.
DR   PaxDb; 9544-ENSMMUP00000028042; -.
DR   Ensembl; ENSMMUT00000056162.2; ENSMMUP00000042745.1; ENSMMUG00000048466.2.
DR   GeneID; 695713; -.
DR   KEGG; mcc:695713; -.
DR   CTD; 5225; -.
DR   VEuPathDB; HostDB:ENSMMUG00000048466; -.
DR   VGNC; VGNC:83442; PGC.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000160626; -.
DR   InParanoid; G7MPA3; -.
DR   OMA; KWMVLAL; -.
DR   OrthoDB; 1120702at2759; -.
DR   Proteomes; UP000006718; Chromosome 4.
DR   Bgee; ENSMMUG00000048466; Expressed in lung and 2 other cell types or tissues.
DR   ExpressionAtlas; G7MPA3; baseline.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0002803; P:positive regulation of antibacterial peptide production; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd05477; gastricsin; 1.
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.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          73..385
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        104..109
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        310..343
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   388 AA;  42447 MW;  924CA6A38FDC72D0 CRC64;
     MKWLVVVLLC LQLLEAAVVK VPLKKFKSIR ETMKEKGLLG EFLRTHKYDP AWKYHFGDLS
     VSYEPMAYMD AAYFGEISIG TPPQNFLVLF DTGSSNLWVP SVYCQSQACT SHSRFNPSES
     STYSTNGQTF SLQYGSGSLT GFFGYDTLTV QSIQVPNQEF GLSENEPGTN FVYAQFDGIM
     GLAYPTLSVD GATTAMQGMV QEGALTSPIF SVYLSDQQGS SGGAVVFGGV DSSLYTGQIY
     WAPVTQELYW QIGIEEFLIG GQASGWCSEG CQAIVDTGTS LLTVPQQYMS ALLQATGAQE
     DEYGQFLVNC NSIQNLPTLT FIINGVEFPL PPSSYILNNN GYCTVGVEPT YLSAQNSQPL
     WILGDVFLRS YYSVYDLSNN RVGFATAA
//
DBGET integrated database retrieval system