ID W5N4U3_LEPOC Unreviewed; 388 AA.
AC W5N4U3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Gastricsin {ECO:0000256|ARBA:ARBA00023821};
DE EC=3.4.23.3 {ECO:0000256|ARBA:ARBA00023796};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000015652.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000015652.1}
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}.
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DR EMBL; AHAT01016571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015198218.1; XM_015342732.1.
DR AlphaFoldDB; W5N4U3; -.
DR STRING; 7918.ENSLOCP00000015652; -.
DR Ensembl; ENSLOCT00000015681.1; ENSLOCP00000015652.1; ENSLOCG00000012718.1.
DR GeneID; 102693407; -.
DR KEGG; loc:102693407; -.
DR CTD; 5225; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000164965; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; W5N4U3; -.
DR OMA; CLHLCEG; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000012718; Expressed in embryo and 11 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
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; 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:UP000018468};
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..388
FT /note="Gastricsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004869279"
FT DOMAIN 70..385
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 88
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 272
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 101..106
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 388 AA; 43130 MW; 5DA6DC3B52E72863 CRC64;
MKWLIVALAC LTLSEGLVRI PLKRFKSIRE QMRESGKYLP YSDPGLKYQH YYSYATSANE
PLANYADMSY YGAISIGTPP QSFYVLFDTG SSNLWVASVY CNSQACTNHP TFDPSKSSTY
SSTGQTFSLQ YGTGSLTGVF GYDTVYIQDI AITNQEVGLS TNEPGTNFVY AQFDGILGLA
YPQLSAGGET PVMDTMMQEH LLQYNLFAFY LSRDEQQGSE VTFGGVDSSR YSGQIYWAPV
TQDLYWQIAI DGFQINNQET GWCSQGCQAI VDTGTSLLTC PQQYLGYLQQ YIGAQANQNG
EYIINCNNLS NMPTISFTIN GVNFALPPSA YTIVRNQNGY QYCTSGIMGT YLPSQNGQPL
WILGDVFLRE YYSVYDRQNN RVGFAAAA
//
