ID G3QJP9_GORGO Unreviewed; 388 AA.
AC G3QJP9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 79.
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:ENSGGOP00000002651.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000002651.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000002651.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000002651.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000002651.3}
RP IDENTIFICATION.
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}.
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DR EMBL; CABD030044643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004044046.2; XM_004043998.2.
DR AlphaFoldDB; G3QJP9; -.
DR STRING; 9593.ENSGGOP00000002651; -.
DR MEROPS; A01.003; -.
DR Ensembl; ENSGGOT00000002705.3; ENSGGOP00000002651.3; ENSGGOG00000002688.3.
DR GeneID; 101129549; -.
DR KEGG; ggo:101129549; -.
DR CTD; 5225; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000160626; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; G3QJP9; -.
DR OMA; KWMVLAL; -.
DR OrthoDB; 1120702at2759; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000001519; Chromosome 6.
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:UP000001519};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..388
FT /note="Gastricsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030171774"
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; 42420 MW; 1E4679939586C7D8 CRC64;
MKWMVMVLVC LQLLEAAVVK VPLKKFKSIR ETMKEKGLLG EFLRTHKYDP AWKYHFGDLS
VTYEPMAYMD AAYFGEISIG TPPQNFLVLF DTGSSNLWVP SVYCQSQACT SHSRFNPSES
STYSTNGQTF SLQYGSGSLT GFFGYDTLTV QSIQVPNQEF GLSENEPGTN FVCAQFDGIM
GLAYPALSVD EATTAMQGMV QEGALTSPVF SVYLSNQQGS SGGAVVFGGV DNSLYTGQIY
WAPVTQELYW QIGIEEFLIG GQASGWCSEG CQAIVDTGTS LLTVPQQYMS ALLQATGAQE
DEYGQFLVNC NSIQNLPTLT FIINGVEFPL PPSSYILSNN GYCTVGVEPT YLSSQNGQPL
WILGDVFLRS YYSVYDLGNN RVGFATAA
//
