ID G3PP46_GASAC Unreviewed; 405 AA.
AC G3PP46;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Nothepsin {ECO:0000313|Ensembl:ENSGACP00000019379.1};
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:ENSGACP00000019379.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000019379.1, 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:ENSGACP00000019379.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR AlphaFoldDB; G3PP46; -.
DR STRING; 69293.ENSGACP00000019379; -.
DR Ensembl; ENSGACT00000019417.1; ENSGACP00000019379.1; ENSGACG00000014665.1.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000164590; -.
DR InParanoid; G3PP46; -.
DR OMA; CRVHQKF; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000014665; Expressed in mesonephros and 1 other cell type or tissue.
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:SF37; CATHEPSINE-A-LIKE PROTEIN; 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:UP000007635};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..405
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003449931"
FT DOMAIN 83..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 101
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 114..119
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 278..282
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 321..358
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 405 AA; 44799 MW; BFB06D01829E2858 CRC64;
LLWTWTWTSS ALLRLSIIIR VPLKRVRSVR SQLRVEGLLE EFLKEHRPDM FNRRYAQCFP
PGTPSLRLGR SSEKIYNFMD AQYYGEITLG TPGQNFSVVF DTGSSDLWVP STYCVSQACA
SHRRFKAFES SSFFHDGRTF GVHYGSGHLL GVMARETLKI GSLTTINQEF GESVYEPGSA
FVRAKFDGVL GLGYPALAEI LGNPVFDNLL AQKAVEEPVF SFFLSRRTSS GSPEGELLLG
GKDEALYSGP INWLPVTAKG YWQIKMESVS VQGAISLCPR GCQAIVDTGT SLIAGPTADI
ISLHQLIGAT PTNIGEFLID CARMSSLPHV TFVLGGTEYT LTPEQYVRKD TLADKEFCFS
GFQAVDIFSP QGPLWILGDV FLTEFYSIFD RGLDRVGFAF AKHPA
//
