CARDE_CYNCA
ID CARDE_CYNCA Reviewed; 224 AA.
AC P85136;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Cardosin-E {ECO:0000303|PubMed:19488781};
DE EC=3.4.23.-;
DE Contains:
DE RecName: Full=Cardosin-E heavy chain {ECO:0000303|PubMed:19488781};
DE Contains:
DE RecName: Full=Cardosin-E light chain {ECO:0000303|PubMed:19488781};
DE Flags: Fragments;
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;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, GLYCOSYLATION, AND MASS
RP SPECTROMETRY.
RC STRAIN=cv. Sylvestris {ECO:0000269|PubMed:19488781};
RC TISSUE=Stigma {ECO:0000269|PubMed:19488781};
RX PubMed=19488781; DOI=10.1007/s00425-009-0948-9;
RA Sarmento A.C., Lopes H., Oliveira C.S., Vitorino R., Samyn B., Sergeant K.,
RA Debyser G., Van Beeumen J., Domingues P., Amado F., Pires E.,
RA Domingues M.R., Barros M.T.;
RT "Multiplicity of aspartic proteinases from Cynara cardunculus L.";
RL Planta 230:429-439(2009).
CC -!- FUNCTION: Aspartic protease with a high preference for bonds between
CC hydrophobic residues. {ECO:0000269|PubMed:19488781}.
CC -!- ACTIVITY REGULATION: Inhibited by pepstatin.
CC {ECO:0000269|PubMed:19488781}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.64 mM for Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu
CC {ECO:0000269|PubMed:19488781};
CC pH dependence:
CC Optimim pH is 4.3. Active from pH 3 to 6.5.
CC {ECO:0000269|PubMed:19488781};
CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain. An
CC intermediate form is produced first, and undergoes proteolytic
CC processing to remove the internal plant-specific insert (PSI) and the
CC propeptide. {ECO:0000250|UniProtKB:Q9XFX3,
CC ECO:0000269|PubMed:19488781}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q9XFX3}. Protein storage vacuole
CC {ECO:0000250|UniProtKB:Q9XFX3}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:Q9XFX3}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250|UniProtKB:Q9XFX3}. Note=Procardosin-E
CC is associated with the microsomal membranes, the mature form is
CC secreted. {ECO:0000250|UniProtKB:Q9XFX3}.
CC -!- TISSUE SPECIFICITY: Pistils. {ECO:0000269|PubMed:19488781}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19488781}.
CC -!- MASS SPECTROMETRY: [Cardosin-E heavy chain]: Mass=27669;
CC Method=Electrospray; Note=Heavy chain.;
CC Evidence={ECO:0000269|PubMed:19488781};
CC -!- MASS SPECTROMETRY: Mass=10691; Method=Electrospray; Note=Light chain.
CC The measured range is unknown.; Evidence={ECO:0000269|PubMed:19488781};
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255}.
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DR AlphaFoldDB; P85136; -.
DR SMR; P85136; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000326; C:protein storage vacuole; 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; 2.40.70.10; -; 3.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 3.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cell wall; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Hydrolase;
KW Membrane; Microsome; Protease; Secreted; Vacuole; Zymogen.
FT CHAIN 1..?
FT /note="Cardosin-E heavy chain"
FT /evidence="ECO:0000269|PubMed:19488781"
FT /id="PRO_0000286869"
FT CHAIN ?..>224
FT /note="Cardosin-E light chain"
FT /evidence="ECO:0000269|PubMed:19488781"
FT /id="PRO_0000394452"
FT DOMAIN 1..221
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 35
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 134
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU10094"
FT DISULFID 125..129
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID ?..181
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU00415"
FT NON_CONS 47..48
FT /evidence="ECO:0000303|PubMed:19488781"
FT NON_CONS 65..66
FT /evidence="ECO:0000303|PubMed:19488781"
FT NON_CONS 157..158
FT /evidence="ECO:0000303|PubMed:19488781"
FT NON_CONS 163..164
FT /evidence="ECO:0000303|PubMed:19488781"
FT NON_CONS 175..176
FT /evidence="ECO:0000303|PubMed:19488781"
FT NON_TER 224
FT /evidence="ECO:0000303|PubMed:19488781"
SQ SEQUENCE 224 AA; 24507 MW; 2A72113B52B60DFA CRC64;
DSGSAIVALT NDRDTSYFGE IGIGTPPQKY TVIYDTGSSV LWVPSSKEQD FIEATDETDN
VFLHRRFSFW LNRNVDEEEG GELVFGGLDP NHFRGDHTYV PVTYQYYWQF GIGDVLIGDK
STGFCAPGCQ AFADSGTSLL SGPTAIVTQI NHAIGANSEE LNVKFGLTPE QYILKGEATQ
CISGFTAMDA TLLGPLWILG DVFMRPYHTV FDYGNLLVGF AEAA
