ID D7FPT0_ECTSI Unreviewed; 442 AA.
AC D7FPT0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Vacuolar Processing Enzyme {ECO:0000313|EMBL:CBJ30537.1};
GN Name=VPE {ECO:0000313|EMBL:CBJ30537.1};
GN ORFNames=Esi_0199_0018 {ECO:0000313|EMBL:CBJ30537.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ30537.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ30537.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
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DR EMBL; FN648374; CBJ30537.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FPT0; -.
DR STRING; 2880.D7FPT0; -.
DR EnsemblProtists; CBJ30537; CBJ30537; Esi_0199_0018.
DR eggNOG; KOG1348; Eukaryota.
DR InParanoid; D7FPT0; -.
DR OMA; LMMYDDV; -.
DR OrthoDB; 2951493at2759; -.
DR Proteomes; UP000002630; Chromosome LG13.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd21115; legumain_C; 1.
DR Gene3D; 1.10.132.130; -; 1.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR048501; Legum_prodom.
DR InterPro; IPR046427; Legumain_prodom_sf.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR12000; HEMOGLOBINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR12000:SF42; LEGUMAIN; 1.
DR Pfam; PF20985; Legum_prodom; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..442
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003095380"
FT DOMAIN 385..438
FT /note="Legumain prodomain"
FT /evidence="ECO:0000259|Pfam:PF20985"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 185
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 442 AA; 47747 MW; 4132CAC54B13F8C6 CRC64;
MIALWRIVFW LGLVATSAGE SNWAVIIAGS RGFINYRHQA DVCHAYHVVR RNGIPAENVI
LMTYGDAVDS VDNPFPGQLF NKPTPDGVAG YDVNRACSPS YTGEDVTADN FLAVLKGDNK
TTEGKPVLRS TKEDRVFVYF ADHGGVGLVA MPAGDPVYAQ DLIDALRHMS TNGMYKELVF
YMEACESGSM FEGLLPEDAN IYATTAANSQ ESSYGTYCGM ESSVNGTLIG SCLGDLYSVN
FLENSDEPSM FHTETLDSQF ALVKNETSKS HAQKFGTLSM GTDHIEWFLG AVGFPSVEGG
EFGDQAAAVA RIPTPKNGVN SRDIKLHDLR YQRSQLAGTG RTREADNLDR QIAEEMAMRF
HSAKVFGEIS TRTSGGAPVP PLTGVFTEHS CLKAASTAVI ASCGPWNDFS LTYVRSLATL
CQAGYPALQI QAAAEAVCRV DV
//
