ID Q5H728_MACMU Unreviewed; 247 AA. AC Q5H728; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=trypsin {ECO:0000256|ARBA:ARBA00038868}; DE EC=3.4.21.4 {ECO:0000256|ARBA:ARBA00038868}; GN Name=try16 {ECO:0000313|EMBL:AAW69367.1}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AAW69367.1}; RN [1] {ECO:0000313|EMBL:AAW69367.1} RP NUCLEOTIDE SEQUENCE. RA Rowen L., Geraghty D., Daza R., Bloom S., Hood L.; RT "Sequence of the beta T-cell receptor locus from rhesus macaque."; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; CC Evidence={ECO:0000256|ARBA:ARBA00036320}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC149201; AAW69367.1; -; Genomic_DNA. DR RefSeq; NP_001040585.1; NM_001047120.1. DR RefSeq; XP_014990580.1; XM_015135094.1. DR AlphaFoldDB; Q5H728; -. DR MEROPS; S01.258; -. DR GeneID; 698352; -. DR KEGG; mcc:698352; -. DR CTD; 5645; -. DR eggNOG; KOG3627; Eukaryota. DR OrthoDB; 4629979at2759; -. 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; 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; PTHR24264:SF57; TRYPSIN-2; 1. DR PANTHER; PTHR24264; TRYPSIN-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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..15 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 16..247 FT /note="trypsin" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5015097894" FT DOMAIN 24..244 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" SQ SEQUENCE 247 AA; 26496 MW; 9688EFEA21439F0D CRC64; MNPLLILAFV GVAVAAPFDD DDKIVGGYTC EENSVPYQVS LNSGYHFCGG SLINEQWVVS AAHCYKTRIQ VRLGEHNIEV LEGTEQFINA AKIIRHPDYD RKTLNNDILL IKLSSPAVIN ARVSTISLPT APPAAGAEAL ISGWGNTLSS GADYPDELQC LEAPVLSQAE CEASYPGKIT SNMFCVGFLE GGKDSCQGDS GGPVVSNGQL QGIVSWGYGC AQKNRPGVYT KVYNYVDWIR DTIAANS //