GenomeNet

Database: UniProt
Entry: G3PFM2_GASAC
LinkDB: G3PFM2_GASAC
Original site: G3PFM2_GASAC 
ID   G3PFM2_GASAC            Unreviewed;       387 AA.
AC   G3PFM2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Gastricsin {ECO:0000256|ARBA:ARBA00023821};
DE            EC=3.4.23.3 {ECO:0000256|ARBA:ARBA00023796};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000016396.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000016396.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000016396.1}
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}.
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   AlphaFoldDB; G3PFM2; -.
DR   STRING; 69293.ENSGACP00000016396; -.
DR   Ensembl; ENSGACT00000016428.1; ENSGACP00000016396.1; ENSGACG00000012388.1.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000164965; -.
DR   InParanoid; G3PFM2; -.
DR   OMA; THATWDE; -.
DR   TreeFam; TF314990; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000012388; Expressed in liver.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 1.
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:UP000007635};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..387
FT                   /note="Gastricsin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003449556"
FT   DOMAIN          69..384
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        100..105
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   387 AA;  42093 MW;  B792A0B072A2A2AB CRC64;
     MKCLVAVLVC VVLAEGIVKI PLQKHKSMRE ALRDKGIELP YQDPALKYQA DEFAGSASMY
     INNYADTTYY GAISIGTPPQ SFQVLFDTGS ANLWVDSVYC NTQACNTHTK FNPQQSSTYS
     GKGQTFYLPY GAGSLYGTFG YDTVNVGGIV INNQEIGLST NEPGQNFVVA KFDGILGLSY
     PSISAGGETP VMDNMISQNL LSADMFAFYL SRGGQQGSVL SFGGVDNSLY QGQIYWTPVT
     SQTYWQIGVN GFQINGQETG WCSQGCQSIV DTGTSALTAP SQFLGSIMQA IGAQQNQYGQ
     YMVDCSQINN LPTFSFVISG VSLPLPPSAY ITQTNQNGYQ YCSVDISPTY LPSQDGQPLW
     IMGDVFLREY YSVYDRSNNR LGFAAAV
//
DBGET integrated database retrieval system