ID G3NZM7_GASAC Unreviewed; 395 AA.
AC G3NZM7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
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:ENSGACP00000010800.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000010800.1, 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:ENSGACP00000010800.1}
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; G3NZM7; -.
DR MEROPS; A01.009; -.
DR Ensembl; ENSGACT00000010822.1; ENSGACP00000010800.1; ENSGACG00000008090.1.
DR GeneTree; ENSGT00940000155733; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000008090; Expressed in heart and 13 other cell types or tissues.
DR GO; GO:0005764; C:lysosome; IEA:InterPro.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05490; Cathepsin_D2; 1.
DR Gene3D; 2.60.40.1960; -; 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; IPR033144; Cathepsin_D.
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:SF94; NAPSIN-A; 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}.
FT DOMAIN 75..392
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 93
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 280
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT DISULFID 106..113
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 271..275
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 314..351
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 395 AA; 43151 MW; 6A937B5D8B012D8D CRC64;
YVYFNLVVFM VSLWKGFLIC RVPLHKTRSL RRVMSDNGMS LEELRALASS YAPPDGSPSP
DVPVERLTNF MDAQYYGVIS IGTPPQDFTV LFDTGSSNLW VPSIHCSFFD LACWLHRRYN
SKKSSTFVKN GTEFSIRYGR GSLSGYISGD TVSVAGLPVP GQQFGEAVKQ PGITFAVARF
DGVLGMAYPS ISVANVTPVF DTAMAAKLLP QDVFSFYISR DPTAAVGGEL MLGGTDPKYY
TGDLHYVNVT RKAYWQMKLS GVDVGNQLTL CKAGCQAIVD TGTSLIVGPV EEIRALHKAI
GALPLLMGEY WINCEKIPSL PVVSFIIGGK MYNLTGEDYV MKETQMGSSI CLSGFMAMDI
PPPAGPLWIL GDVFIGKYYT VFDRAADRLG FAPAK
//
