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Database: UniProt
Entry: A0A2K5XV97_MANLE
LinkDB: A0A2K5XV97_MANLE
Original site: A0A2K5XV97_MANLE 
ID   A0A2K5XV97_MANLE        Unreviewed;       252 AA.
AC   A0A2K5XV97;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Chymase 1 {ECO:0000313|Ensembl:ENSMLEP00000007244.1};
GN   Name=CMA1 {ECO:0000313|Ensembl:ENSMLEP00000007244.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000007244.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000007244.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K5XV97; -.
DR   STRING; 9568.ENSMLEP00000007244; -.
DR   Ensembl; ENSMLET00000030545.1; ENSMLEP00000007244.1; ENSMLEG00000027616.1.
DR   GeneTree; ENSGT01030000234551; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR   GO; GO:0034769; P:basement membrane disassembly; IEA:Ensembl.
DR   GO; GO:0140447; P:cytokine precursor processing; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24271:SF24; CHYMASE; 1.
DR   PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..252
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014444792"
FT   DOMAIN          22..250
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   252 AA;  27932 MW;  56BAF88AB1DABDB0 CRC64;
     MLLLPLPLLL FFLCSRAEAG EIIGGTECKP HSRPYMAYLE IVTSNGPSKS CGGFLIRRNF
     VLTAAHCAGR SITVTLGAHN ITEKEDTWQK LEVIKQFRHP KYNTSTLHHD IMLLKLLLQV
     LIEKASLTLA VGTLPFPSQF NFVPPGRMCR VAGWGRTGVL KPGSETLQEV KLRLMHPQAC
     SHFRYFDHNL QLCVGNPRKT KSAFKGDSGG PLLCAGVAQG IVSYGQLDAK PPAVFTRISH
     YRPWINKILQ AN
//
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