CARDB_CYNCA
ID CARDB_CYNCA Reviewed; 506 AA.
AC Q9XFX4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Procardosin-B {ECO:0000303|PubMed:8654427};
DE EC=3.4.23.-;
DE Contains:
DE RecName: Full=Cardosin-B heavy chain {ECO:0000303|PubMed:8654427};
DE AltName: Full=Cardosin-B 34 kDa subunit {ECO:0000303|PubMed:8654427};
DE Contains:
DE RecName: Full=Cardosin-B light chain {ECO:0000303|PubMed:8654427};
DE AltName: Full=Cardosin-B 14 kDa subunit {ECO:0000303|PubMed:8654427};
DE Flags: Precursor;
GN Name=cardB {ECO:0000312|EMBL:CAB40349.1};
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB40349.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Flower bud {ECO:0000269|PubMed:11414612};
RX PubMed=11414612; DOI=10.1023/a:1010675015318;
RA Vieira M., Pissarr J., Verissimo P., Castanheira P., Costa Y., Pires E.,
RA Faro C.;
RT "Molecular cloning and characterization of cDNA encoding cardosin B, an
RT aspartic proteinase accumulating extracellularly in the transmitting tissue
RT of Cynara cardunculus L.";
RL Plant Mol. Biol. 45:529-539(2001).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 71-113; 199-229; 239-260; 268-276; 418-442; 445-448 AND
RP 486-502, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC TISSUE=Stigma {ECO:0000269|PubMed:8654427};
RX PubMed=8654427; DOI=10.1111/j.1432-1033.1996.00762.x;
RA Verissimo P., Faro C., Moir A.J., Lin Y., Tang J., Pires E.;
RT "Purification, characterization and partial amino acid sequencing of two
RT new aspartic proteinases from fresh flowers of Cynara cardunculus L.";
RL Eur. J. Biochem. 235:762-768(1996).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=16428617; DOI=10.3168/jds.s0022-0302(06)72111-7;
RA Barros R.M., Malcata F.X.;
RT "Molecular characterization of peptides released from beta-lactoglobulin
RT and alpha-lactalbumin via cardosins A and B.";
RL J. Dairy Sci. 89:483-494(2006).
RN [4] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=18767217; DOI=10.1007/s00709-008-0288-9;
RA Pereira C.S., da Costa D.S., Pereira S., Nogueira Fde M., Albuquerque P.M.,
RA Teixeira J., Faro C., Pissarra J.;
RT "Cardosins in postembryonic development of cardoon: towards an elucidation
RT of the biological function of plant aspartic proteinases.";
RL Protoplasma 232:203-213(2008).
CC -!- FUNCTION: Aspartic protease. Cleaves alpha-lactalbumin but not beta-
CC lactoglobulin. {ECO:0000269|PubMed:16428617,
CC ECO:0000269|PubMed:8654427}.
CC -!- ACTIVITY REGULATION: Inhibited by the specific aspartic proteinase
CC inhibitors diazoacetyl-noleucine methyl ester and pepstatin.
CC {ECO:0000269|PubMed:8654427}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.081 mM for Leu-Ser-Phe(NO2)-Ahx-Ala-Leu
CC {ECO:0000269|PubMed:8654427};
CC KM=0.11 mM for Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu
CC {ECO:0000269|PubMed:8654427};
CC pH dependence:
CC Optimum pH is 5.0. Active from pH 2.0-7.0.
CC {ECO:0000269|PubMed:8654427};
CC Temperature dependence:
CC Stable at temperatures of up to 60 degrees Celsius.
CC {ECO:0000269|PubMed:8654427};
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, ECO:0000269|PubMed:8654427}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q9XFX3}. Protein storage vacuole
CC {ECO:0000250|UniProtKB:Q9XFX3}. Secreted, cell wall
CC {ECO:0000269|PubMed:11414612}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000269|PubMed:11414612}. Note=Procardosin-B
CC is associated with the microsomal membranes, the mature form is
CC secreted. {ECO:0000250|UniProtKB:Q9XFX3, ECO:0000269|PubMed:11414612}.
CC -!- TISSUE SPECIFICITY: Detected in pistils, but not in seeds, bracts,
CC midribs, roots, leaves or stamen extracts (PubMed:11414612). Detected
CC in seeds (PubMed:18767217). In stigmas and styles, detected in the
CC transmitting tissue and in contiguous subepidermal layers at the
CC longitudenal grooves of the stigma (at protein level).
CC {ECO:0000269|PubMed:11414612, ECO:0000269|PubMed:18767217}.
CC -!- DEVELOPMENTAL STAGE: In flowers, highest levels of mRNA are found in
CC closed capitula and amount decreases during floral development,
CC detected at protein level in both closed and open flowers. At the mRNA
CC level, virtually undetectable in seeds at all stages. At protein level,
CC detected in the embryo during the first stages after seed hydration,
CC levels gradually decrease and it becomes almost undetectable after 72-
CC 84 hours. {ECO:0000269|PubMed:11414612, ECO:0000269|PubMed:18767217}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255}.
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DR EMBL; AJ237674; CAB40349.1; -; mRNA.
DR PDB; 5NFG; X-ray; 2.38 A; A/B=25-314, A/B=418-506.
DR PDBsum; 5NFG; -.
DR AlphaFoldDB; Q9XFX4; -.
DR SMR; Q9XFX4; -.
DR MEROPS; A01.020; -.
DR BRENDA; 3.4.23.40; 1789.
DR SABIO-RK; Q9XFX4; -.
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: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; -; 2.
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; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF47862; SSF47862; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS50015; SAP_B; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Cell wall; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Extracellular matrix; Glycoprotein;
KW Hydrolase; Membrane; Microsome; Protease; Secreted; Signal; Vacuole;
KW Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..506
FT /note="Procardosin-B"
FT /evidence="ECO:0000255"
FT /id="PRO_5000065111"
FT PROPEP 25..70
FT /evidence="ECO:0000269|PubMed:8654427"
FT /id="PRO_0000394448"
FT CHAIN 71..?
FT /note="Cardosin-B heavy chain"
FT /evidence="ECO:0000269|PubMed:8654427"
FT /id="PRO_5000065112"
FT CHAIN 418..506
FT /note="Cardosin-B light chain"
FT /evidence="ECO:0000269|PubMed:8654427"
FT /id="PRO_5000065113"
FT DOMAIN 85..503
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT DOMAIN 315..417
FT /note="Saposin B-type"
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU00415"
FT ACT_SITE 103
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 290
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 116..122
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 281..285
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 320..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 345..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 351..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 425..462
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU00415"
FT CONFLICT 84..86
FT /note="AYY -> DYF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..92
FT /note="GIG -> PTQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..254
FT /note="NHT -> GHY (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="I -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 440..442
FT /note="SKL -> GKK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="V -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="G -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5NFG"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:5NFG"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:5NFG"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:5NFG"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 137..147
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 150..163
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 166..179
FT /evidence="ECO:0007829|PDB:5NFG"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:5NFG"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:5NFG"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:5NFG"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:5NFG"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:5NFG"
FT TURN 280..284
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:5NFG"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:5NFG"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:5NFG"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 462..468
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:5NFG"
FT HELIX 483..486
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:5NFG"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:5NFG"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:5NFG"
SQ SEQUENCE 506 AA; 54951 MW; 14A74CC5A93F1C4D CRC64;
MGTPIKASLL ALFLFFLLSP TAFSVSNGGL LRVGLKKRKV DRLDQLRAHG VHMLGNARKD
FGFRRTLSDS GSGIVALTND RDTAYYGEIG IGTPPQNFAV IFDTGSSDLW VPSTKCDTSL
ACVIHPRYDS GDSSTYKGNG TTASIQYGTG AIVGFYSQDS VEVGDLVVEH QDFIETTEED
DTVFLKSEFD GILGLGFQEI SAGKAVPVWY NMVNQGLVEE AVFSFWLNRN VDEEEGGELV
FGGVDPNHFR GNHTYVPVTR KGYWQFEMGD VLIGDKSSGF CAGGCAAIAD SGTSFFAGPT
AIITQINQAI GAKGVLNQQC KTLVGQYGKN MIQMLTSEVQ PDKICSHMKL CTFDGAHDVR
SMIESVVDKN NDKSSGGEIC TFCEMALVRM QNEIKRNETE DNIINHVNEV CDQLPTSSAE
SIVDCNGISS MPNIAFTIGS KLFEVTPEQY IYKVGEGEAA TCISGFTALD IMSPQGPIWI
LGDMFMGPYH TVFDYGKLRV GFAEAV
