MCPT3_SHEEP
ID MCPT3_SHEEP Reviewed; 251 AA.
AC O46683;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Mast cell protease 3;
DE Short=sMCP-3;
DE EC=3.4.21.-;
DE Flags: Precursor;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RX PubMed=9677343; DOI=10.1042/bj3330801;
RA McAleese S.M., Pemberton A.D., McGrath M.E., Huntley J.F., Miller H.R.P.;
RT "Sheep mast-cell proteinases-1 and -3: cDNA cloning, primary structure and
RT molecular modelling of the enzymes and further studies on substrate
RT specificity.";
RL Biochem. J. 333:801-809(1998).
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Secretory
CC granules.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; Y13462; CAA73859.1; -; mRNA.
DR PIR; T10262; T10262.
DR RefSeq; NP_001009411.1; NM_001009411.2.
DR AlphaFoldDB; O46683; -.
DR SMR; O46683; -.
DR STRING; 9940.ENSOARP00000004938; -.
DR MEROPS; S01.142; -.
DR Ensembl; ENSOART00020038638; ENSOARP00020032007; ENSOARG00020024598.
DR GeneID; 443429; -.
DR KEGG; oas:443429; -.
DR CTD; 443429; -.
DR eggNOG; KOG3627; Eukaryota.
DR OrthoDB; 1076876at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..19
FT /note="Activation peptide"
FT /id="PRO_0000027471"
FT CHAIN 20..251
FT /note="Mast cell protease 3"
FT /id="PRO_0000027472"
FT DOMAIN 20..243
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 63
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 107
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 141..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 172..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 251 AA; 27511 MW; DF2F986114AAE909 CRC64;
MVLFLLLVAL LSPAGEAGKI IGGHEAKPHS RPYMAFLQFK ISGKSYICGG FLVREDFVLT
AAHCLGSSIN VTLGAHTITD QERTQQVIQV RRAIPHPDYN DETCANDIML LQLTRKAEMT
DAVSLINLPR SLEKVKPGMM CSVAGWGQLG VNMPSADKLQ EVDLEVQREE KCIARFKDYI
PVTQICAGDP SKRKDSFLGD SGGPLVCDGV AQGIVSYGKD DGTTPNVYTR ISSFLSWIQR
TMRQYKNQGS A