ID Q39476_CYNCA Unreviewed; 509 AA. AC Q39476; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 117. DE SubName: Full=Cyprosin {ECO:0000313|EMBL:CAA57510.1}; OS Cynara cardunculus (Cardoon). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae; OC Carduinae; Cynara. OX NCBI_TaxID=4265 {ECO:0000313|EMBL:CAA57510.1}; RN [1] {ECO:0000313|EMBL:CAA57510.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Flower {ECO:0000313|EMBL:CAA57510.1}; RA Pietrzak M., Brodelius P., Pais M.S.; RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the peptidase A1 family. CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}. 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; X81984; CAA57510.1; -; mRNA. DR PIR; S49349; S49349. DR AlphaFoldDB; Q39476; -. DR SMR; Q39476; -. DR MEROPS; A01.A02; -. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd06098; phytepsin; 1. DR Gene3D; 2.40.70.10; Acid Proteases; 2. DR Gene3D; 1.10.225.10; Saposin-like; 1. 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 InterPro; IPR033869; Phytepsin. DR InterPro; IPR007856; SapB_1. DR InterPro; IPR008138; SapB_2. DR InterPro; IPR011001; Saposin-like. DR InterPro; IPR008139; SaposinB_dom. DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1. DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1. DR Pfam; PF00026; Asp; 1. DR Pfam; PF05184; SapB_1; 1. DR Pfam; PF03489; SapB_2; 1. DR PRINTS; PR00792; PEPSIN. DR SMART; SM00741; SapB; 2. DR SUPFAM; SSF50630; Acid proteases; 1. DR SUPFAM; SSF47862; Saposin; 1. DR PROSITE; PS00141; ASP_PROTEASE; 2. DR PROSITE; PS51767; PEPTIDASE_A1; 1. DR PROSITE; PS50015; SAP_B; 2. PE 2: Evidence at transcript level; KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750, KW ECO:0000256|RuleBase:RU000454}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR601461-2}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454}; KW Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..509 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004222214" FT DOMAIN 85..506 FT /note="Peptidase A1" FT /evidence="ECO:0000259|PROSITE:PS51767" FT DOMAIN 315..355 FT /note="Saposin B-type" FT /evidence="ECO:0000259|PROSITE:PS50015" FT DOMAIN 379..420 FT /note="Saposin B-type" FT /evidence="ECO:0000259|PROSITE:PS50015" FT ACT_SITE 103 FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1" FT ACT_SITE 290 FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1" FT DISULFID 116..122 FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2" SQ SEQUENCE 509 AA; 55177 MW; 4E287C423F827A44 CRC64; MGTAIKASVL ALFLFFLLSP TAFSVSNGGL LRVGLKKRKV DQINQLSGHG VSMEAKARKD FGFGGALRDS GSDIIALKNY MDAQYYGEIG IGSPPQKFTV IFDTGSSNLW VPSAKCYFSV ACLFHSKYKS SHSSTYKKNG TSAAIQYGTG SISGFVSQDS VKLGDLVVKE QDFIEATKEP GITFLAAKFD GILGLGFQEI SVGKSVPLWY NMVNQGLVQE PVFSFWFNRN ADEEEGGELV FGGVDPNHFK GKHTYVPVTE KGYWQFDMGD VLIEDKTTGF CSDGCAAIAD SGTSLLAGPT AIITEINHAI GAKGVMSQQC KTLVSQYGKT MIEMLLSEAQ PDKICSQMKL CTFDGARDAS SIIESVVDEN NGKSSSGVHD EMCTFCEMAV VWMQNQIKRN ETEDNIINYV NELCDRLPSP MGESAVDCNS LSSMPNIAFT IGGKVFELCP EQYILKIGEG EAAQCISGFT AMDVAPPRGP LWILGDVFMG RYHTVFDYGK LRVGFAEAA //