ID W5NVC7_SHEEP Unreviewed; 396 AA.
AC W5NVC7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000002123.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000002123.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000002123.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000002123.1}
RP IDENTIFICATION.
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 EMBL; AMGL01061553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NVC7; -.
DR Ensembl; ENSOART00000002173.1; ENSOARP00000002123.1; ENSOARG00000001993.1.
DR HOGENOM; CLU_013253_3_0_1; -.
DR Proteomes; UP000002356; Chromosome 21.
DR Bgee; ENSOARG00000001993; Expressed in placentome of cotyledonary placenta and 1 other cell type or tissue.
DR ExpressionAtlas; W5NVC7; baseline.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:SF49; PEPSIN A-5; 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:UP000002356}.
FT DOMAIN 87..393
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 286
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 118..123
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 277..281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 319..353
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 396 AA; 44690 MW; B25B401F72E5C0FD CRC64;
MLRTQTSLST WSQERSMKWL VLLGLVAFSE CIVKIPLRRV KTVRKTLSEK NMLNNFLKEH
AYRLSQISFH GSNLTIHPLR NIMDKLYVGN ITIGTPPQEF QVIFDTGSSD LWVSSVFCIS
PTCSTHIRFR HRQSSTFRLA NKTFGIMYGS GRMKGVVVHD TVRIGDLVST DQPFGLSVTE
YGFEGIPFDG VLGLNYPKLS FSGAIPIFDN LKNQGAISEP VFAFYLSKDK WEGSVVMFGG
VDHRYYKGEL NWVPFIQAGD WSVHMDRISM KRKIIACSGG CEAVVDTGTS LIEGPRRLVN
NIQKLIGAMP QGFEDYVSCF AVNTLPSIIF TINGINYPVP ARDYILKDSR GHCYTAFKEN
RVSPSRETWI LGDVFLRRYF SVFDRGNDRI GLARAV
//
