ERVC_TABDI
ID ERVC_TABDI Reviewed; 208 AA.
AC P83654;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 02-JUN-2021, entry version 64.
DE RecName: Full=Ervatamin-C;
DE Short=ERV-C;
DE EC=3.4.22.-;
OS Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae;
OC Tabernaemontaneae; Tabernaemontaninae; Tabernaemontana.
OX NCBI_TaxID=52861 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MASS SPECTROMETRY,
RP AND DISULFIDE BONDS.
RX PubMed=14769029; DOI=10.1021/bi0357659;
RA Guha Thakurta P., Biswas S., Chakrabarti C., Sundd M., Jagannadham M.V.,
RA Dattagupta J.K.;
RT "Structural basis of the unusual stability and substrate specificity of
RT ervatamin C, a plant cysteine protease from Ervatamia coronaria.";
RL Biochemistry 43:1532-1540(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Latex {ECO:0000305};
RA Guha Thakurta P., Biswas S., Chakrabarti C., Dattagupta J.K.;
RL Submitted (AUG-2003) to UniProtKB.
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-21, FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Latex {ECO:0000269|PubMed:9836431};
RX PubMed=9836431; DOI=10.1271/bbb.62.1947;
RA Sundd M., Kundu S., Pal G.P., Medicherla J.V.;
RT "Purification and characterization of a highly stable cysteine protease
RT from the latex of Ervatamia coronaria.";
RL Biosci. Biotechnol. Biochem. 62:1947-1955(1998).
RN [4] {ECO:0000305}
RP STABILITY.
RC TISSUE=Latex {ECO:0000269|PubMed:10543984};
RX PubMed=10543984; DOI=10.1006/bbrc.1999.1550;
RA Kundu S., Sundd M., Jagannadham M.V.;
RT "Structural characterization of a highly stable cysteine protease ervatamin
RT C.";
RL Biochem. Biophys. Res. Commun. 264:635-642(1999).
CC -!- FUNCTION: Cysteine proteinase. Hydrolyzes denatured natural substrates
CC such as casein, hemoglobin, azoalbumin and azocasein with a high
CC specific activity. Has little or no activity against synthetic
CC substrates. {ECO:0000269|PubMed:9836431}.
CC -!- ACTIVITY REGULATION: Activated by thio-specific activators such as
CC cysteine, beta-mercaptoethanol, DTT and glutathione. Inhibited by the
CC thiol-specific inhibitors leupeptin, iodoacetamide, PCMB, NEM, mercuric
CC chloride and sodium tetrathionate. {ECO:0000269|PubMed:9836431}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.09 uM for azoalbumin;
CC pH dependence:
CC Optimum pH is 7.5-8.0 with azoalbumin or hemoglobin as substrate.
CC Active and stable from pH 2.0 to 12.0.;
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius with azoalbumin as
CC substrate. Thermostable up to 70 degrees Celsius.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.2, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Laticifer. {ECO:0000269|Ref.2, ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=23000; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:14769029};
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR PDB; 1O0E; X-ray; 1.90 A; A/B=1-208.
DR PDB; 2PNS; X-ray; 1.90 A; A/B=1-208.
DR PDBsum; 1O0E; -.
DR PDBsum; 2PNS; -.
DR SMR; P83654; -.
DR MEROPS; C01.116; -.
DR BRENDA; 3.4.22.B50; 6200.
DR SABIO-RK; P83654; -.
DR EvolutionaryTrace; P83654; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Protease; Secreted; Thiol protease.
FT CHAIN 1..208
FT /note="Ervatamin-C"
FT /id="PRO_0000050559"
FT ACT_SITE 25
FT /evidence="ECO:0000250|UniProtKB:P00785"
FT ACT_SITE 157
FT /evidence="ECO:0000250|UniProtKB:P00785"
FT ACT_SITE 173
FT /evidence="ECO:0000250|UniProtKB:P00785"
FT DISULFID 22..63
FT /evidence="ECO:0000269|PubMed:14769029"
FT DISULFID 56..96
FT /evidence="ECO:0000269|PubMed:14769029"
FT DISULFID 114..193
FT /evidence="ECO:0000269|PubMed:14769029"
FT DISULFID 151..196
FT /evidence="ECO:0000269|PubMed:14769029"
FT CONFLICT 17
FT /note="K -> W (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="S -> W (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:1O0E"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1O0E"
FT HELIX 25..42
FT /evidence="ECO:0007829|PDB:1O0E"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:1O0E"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:1O0E"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1O0E"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1O0E"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:1O0E"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1O0E"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1O0E"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1O0E"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:1O0E"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:1O0E"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1O0E"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1O0E"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1O0E"
SQ SEQUENCE 208 AA; 22523 MW; 13CD944089802C12 CRC64;
LPEQIDWRKK GAVTPVKNQG SCGSCWAFST VSTVESINQI RTGNLISLSE QELVDCDKKN
HGCLGGAFVF AYQYIINNGG IDTQANYPYK AVQGPCQAAS KVVSIDGYNG VPFCNEXALK
QAVAVQPSTV AIDASSAQFQ QYSSGIFSGP CGTKLNHGVT IVGYQANYWI VRNSWGRYWG
EKGYIRMLRV GGCGLCGIAR LPYYPTKA
