ID A0A0N5D6M0_THECL Unreviewed; 477 AA.
AC A0A0N5D6M0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=TCLT_LOCUS8675 {ECO:0000313|EMBL:VDN06253.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000868601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000868601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN06253.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-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}.
CC -!- SIMILARITY: Belongs to the peptidase M50A family.
CC {ECO:0000256|ARBA:ARBA00009989}.
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DR EMBL; UYYF01004668; VDN06253.1; -; Genomic_DNA.
DR STRING; 103827.A0A0N5D6M0; -.
DR WBParaSite; TCLT_0000868601-mRNA-1; TCLT_0000868601-mRNA-1; TCLT_0000868601.
DR OMA; FYSWGRW; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; 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; IPR036034; PDZ_sf.
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.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..462
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 477 AA; 54113 MW; 67E6CC892350EDDA CRC64;
MVFQIRFVLF QSPSKAFKML PQNSLSLYLL NIWFITGVIT AICFSFSIIF YLSRTSIMEL
SLWWVEFFGS FAVDSSVTYV RRQEVTTASK RFVEFDGSLE FVIPGWNIPW TQVPLYIVVL
FLAALTHEFG HMLAALNTNV PVLNMGFVFL AIYIVAYVEI DTTALRRLSL FQKLKISCAG
IWHNLVLAVF AYALYKASPF FLLPLYVSDA GVYVSDIQKG SPLSGPAGLQ KGIVINGVSG
CSVSSVDNWN DCLMKLRSTD LGFCVSNTVI ADNIAKEMQL VENELDCCYN ATKNHSTSYM
CFYVREWINT TQSRGNQELL KYFSAKECTC LPSRYVAELL LCSSNEDCIK LNDTLEKSSE
SCVYPALLGN MSLMRISIND TSRVVLYVGY IEELECHVEV SNYVPRLSFV PALIPYVIEL
MAKYLFTFSF AFAVINAVPC IYLDGQYMWS NFVDIIFSRL GPRFLIFVLF FRLMNLI
//
