ID G3U980_LOXAF Unreviewed; 374 AA.
AC G3U980;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 08-NOV-2023, entry version 58.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000024388.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000024388.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000024388.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000024388.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000024388.1};
RG Ensembl;
RL Submitted (JUL-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; G3U980; -.
DR STRING; 9785.ENSLAFP00000024388; -.
DR MEROPS; A01.006; -.
DR Ensembl; ENSLAFT00000034170.1; ENSLAFP00000024388.1; ENSLAFG00000031820.1.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000162710; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; G3U980; -.
DR OMA; QNHHRFN; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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:SF13; CHYMOSIN; 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:UP000007646}.
FT DOMAIN 67..371
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 85
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 267
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 98..103
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 258..262
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 301..334
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 374 AA; 41558 MW; E9CAC0E0A6EF74C5 CRC64;
RCPTLTLILP HLLRVHLHKG KSMRQALKES GLLDDFLRKH QYAIGRKYSN SGMVAREPLI
NYLDSQYFGK IYIGTPSQEF TVVFDTGSSD FWVPSVYCNS DACQNHHCFN LFKSSTFQNM
GQPLTIQYGT GSMQGFLGYD TVTVSDIVDP QQTVGLSTQE PGNVFTYAEF DGILGLAYPS
LASEYLVPVF DNMMYRHLVP HDLFSVYMSR NDQGSVLTLG AIDSSYYTGS LHWVPVTLQE
YWQFTVDSIT VDGVLVACDG GCQAILDTGT SLLAGPNNDI LNIQKVIGAT RGQYGQFNID
CGRLSSMPVV VFEIQGRRYP LPPSAYTNQD QGSCTSGFQS NSDPQQWILG DVFIREYYSV
FDRANNCVGL AKAI
//