ID M0QVZ7_BOVIN Unreviewed; 323 AA.
AC M0QVZ7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=LOC520130 {ECO:0000313|Ensembl:ENSBTAP00000009701.6};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000009701.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000009701.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000009701.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000009701.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000009701.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR AlphaFoldDB; M0QVZ7; -.
DR SMR; M0QVZ7; -.
DR PaxDb; 9913-ENSBTAP00000009701; -.
DR Ensembl; ENSBTAT00000009701.6; ENSBTAP00000009701.6; ENSBTAG00000038506.3.
DR VEuPathDB; HostDB:ENSBTAG00000038506; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000153747; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; M0QVZ7; -.
DR OMA; LEWPKPG; -.
DR Proteomes; UP000009136; Chromosome 29.
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; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF49; PEPSIN A-5; 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|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..323
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018664823"
FT DOMAIN 60..323
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 91..96
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 248..252
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 323 AA; 36017 MW; A7F9DAAEAE6E482D CRC64;
MKWLVLLGLV AFSNCRVVTN CKAIVNNRAE EFNFHRCKNH SSKKLLNLYS VLRDRQRMLY
MGNITIGTPP QEFQVIFDTG SSDLWVPSFF CPSPACSTQV RFRHYKSSTF RPTQNTFSIA
YGSGSMKGFL TYNIVWIGDL VSTDQLFGLS VVEYRCEGTP FDGILGLKYP NISVFGAISI
FDNLKNQGAI SEPVFAFYLS KAKGSVVMFG GVYKSYYQGV LNWVPLIHTG DWSVHMECIS
MKRKVIACSG GCEPFVDTET SLILGPRRLV NNIQKLISAM PGGSEHYISC FAVNTLPSII
FTINGINYPV PAQAYIFKVR GGS
//
