ID A0A0N4VDM8_ENTVE Unreviewed; 676 AA.
AC A0A0N4VDM8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Membrane-bound transcription factor site-2 protease {ECO:0000256|ARBA:ARBA00014400};
DE EC=3.4.24.85 {ECO:0000256|ARBA:ARBA00012347};
DE AltName: Full=Endopeptidase S2P {ECO:0000256|ARBA:ARBA00032658};
GN ORFNames=EVEC_LOCUS8203 {ECO:0000313|EMBL:VDD93452.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000871901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000871901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD93452.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves several transcription factors that are type-2
CC transmembrane proteins within membrane-spanning domains. Known
CC substrates include sterol regulatory element-binding protein (SREBP)
CC -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2
CC is cleaved at the site 477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The
CC residues Asn-Pro, 11 residues distal to the site of cleavage in the
CC membrane-spanning domain, are important for cleavage by S2P
CC endopeptidase. Replacement of either of these residues does not
CC prevent cleavage, but there is no cleavage if both of these residues
CC are replaced.; EC=3.4.24.85;
CC Evidence={ECO:0000256|ARBA:ARBA00001350};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; UXUI01009313; VDD93452.1; -; Genomic_DNA.
DR STRING; 51028.A0A0N4VDM8; -.
DR WBParaSite; EVEC_0000871901-mRNA-1; EVEC_0000871901-mRNA-1; EVEC_0000871901.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR001193; MBTPS2.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR13325:SF3; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-2 PROTEASE; 1.
DR PANTHER; PTHR13325; PROTEASE M50 MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE 2 PROTEASE; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR PRINTS; PR01000; SREBPS2PTASE.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000274131};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 221..371
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 676 AA; 75899 MW; 5459A21DEDEC311B CRC64;
MLLTTALSCF LAFWSLLFLT DFYLRANAVH WYINFADHIG LSVSFFQVCS LYLGPFSSIF
PFRQPYTFYP LGILRIIVKK PDEKLGCRFS ELSGMEGAEI RFYTNRFHQS LLYQPLAASS
PSKYSLISRA VSVWFTVGAT VSLICFFGVT IFLTKLLWDV FAPWWPSYPY PEEQLVPPVF
HLNQVKDHGF ISHTQRQTES EVGLTPIVPG VNIPWEHVPL FLLVLTIVGV VHELGHAMAA
VDANVPVSGF GIFLIAVYPG AFTEMQTDAL GRSSSAQKMR IFGAGIWHNL VLAFFGYLLY
LVVPYVLAPL YLRGNGVYIR VRLLLQDVDL RSGLSGMAGL RKNDVVYNIN GCATKSTADW
YKCLAEIKGT KVGFCVPNEK ILPGLAKKVE TFGGEMHCCD EFQDVSLSHI CFYFKNVSAA
VKKKKFLFDF PLSRGVTLAP NLAESLGFKA ARKRDIKALE RKSNFILNRN ARKVEQGSKN
FDAFAFLSKP TAIKKTQDEK YACLPARLVT DYETCKTPLD CAGYPNGPQC AFPALFNGTL
LLRINVGNTS RPILFIGTTD ELVYFVKLSD YIPLYFFAFP WLPYASELVS KYLVTFSLAG
LQLAKYFFAA VALLNAVPCY GLDGQFISET VIESVFAQFS TRRRLILHKF LVYYGVAILS
GNLLVGFVRF LRPYLT
//
