ID A0A2U9CY36_SCOMX Unreviewed; 497 AA.
AC A0A2U9CY36;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Name=mbtps2 {ECO:0000313|Ensembl:ENSSMAP00000011384.1};
GN ORFNames=SMAX5B_001780 {ECO:0000313|EMBL:AWP21063.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP21063.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP21063.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSMAP00000011384.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; CP026263; AWP21063.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000011384; -.
DR Ensembl; ENSSMAT00000011533.2; ENSSMAP00000011384.1; ENSSMAG00000007005.2.
DR GeneTree; ENSGT00510000048066; -.
DR OMA; FYSWGRW; -.
DR OrthoDB; 5181at2759; -.
DR Proteomes; UP000246464; Chromosome 21.
DR Proteomes; UP000694558; Chromosome 21.
DR Bgee; ENSSMAG00000007005; Expressed in head kidney and 6 other cell types or tissues.
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:UniProtKB-KW.
DR CDD; cd06162; S2P-M50_PDZ_SREBP; 1.
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 Hydrolase {ECO:0000313|EMBL:AWP21063.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:AWP21063.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..497
FT /note="Membrane-bound transcription factor site-2 protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040585529"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..477
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 497 AA; 54328 MW; C9B6E33F4DC88031 CRC64;
MIPVPLLVCV MAAWCAVYLA DTLLRSSASH RVRYESWLAS RGLMLSPFHL RWQTTMFNRL
FAFCARINPR ALHVWFNSGL VFGVVAMVGS VVLLTKTLQQ TLAQMTSDNP RMGGQQALQV
VVPGVNLPTN QLAYFFTALL LSGVIHELGH AVAALREQVR VNGFGMFVFV VYPGAFVDLF
TTHLNLVSPT QQLRIFCAGV WHNFVLCVAA LAFLFLLPIF LFPVYSTGAG ALVIEVIQGS
AADGPRGLSV GDIVTGLEDC PVSGVEDWSS CLSRLSHSPQ TGYCVPVTSL QPSWAHGRAF
KRLDGTMDCC SNNSLTDLCF SYVQPQGRSR EKEFACMPVR KMVSGTRVCR ADGDCAAAHV
ASVCVTPSLE NQTRFIRVTH PPNTHMLFVG YPPHLQYAVS LTNFVPRFGF LHLDLPVFLE
TFCKYVVSLS GALAVVNSVP CFALDGQWML NALLEATLAA VVTDRQKREL IGFFLLLAGS
ALLAANVALG LWMVTAR
//
