ID A0A3B3I1E2_ORYLA Unreviewed; 1155 AA.
AC A0A3B3I1E2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSORLP00000037909.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000037909.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000037909.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000037909.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000037909.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000037909.1};
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; A0A3B3I1E2; -.
DR STRING; 8090.ENSORLP00000037909; -.
DR Ensembl; ENSORLT00000034931.1; ENSORLP00000037909.1; ENSORLG00000014065.2.
DR GeneTree; ENSGT00510000048066; -.
DR InParanoid; A0A3B3I1E2; -.
DR Proteomes; UP000001038; Chromosome 20.
DR Bgee; ENSORLG00000014065; Expressed in heart and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IBA:GO_Central.
DR GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 485..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 509..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 537..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 646..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 735..753
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..804
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 816..835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 855..877
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1128..1152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 789..1135
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 1155 AA; 125499 MW; 92CA3F4DE2614FCF CRC64;
MFTSMVPAVH LVVPAVHLVV PAVLLVVAAV HLVCSSCSPG LFQLFTWLFQ LFYWFVPAVH
LVCSSCSPGC SSCSPGCSSC CPGCSSFSIG LFQLFPWLFQ LFPWLFQLFP WLIQLLSWLF
QLLSWLFQMF SRFVPAVHLV VPAVLLVCSS CSPGGSSCFP GCSSCSPGCC SCSSGLFQLF
TWLFQLFSWL FQLFTWLFQL FTWLFQLFMW WFQLVMWWFQ LFFWWFQMFS WWFQLFTWLF
QLLSWLFQLF MWLFQLFFWR FPAVLLVVPA VFLVVPDVYL VVPDVLPVCS RCSPGLVPAV
FLVVPAVLLE VSSCSSGCSS CCPGCSSCCP GCSSFSIGLF QLFTQFVPAV LLVCSSCSPG
CSSCSPGCSS CSPGCSSCSC GGSSCSPGGS SCFSGGSRCS PGGSSCSPGC SSCCPGCSSC
CPGCSSCCPG CSSCSCGCSS CSSGGFQLFF WWFQLFSWLF QLFIWLFQMF IWLFQMFSRF
VPDVLPVWFQ LFSWLFQLLF WRFPAVHLVV PAVVLVVPAV VLVVPAVVLV VPAVHVVVPA
VHLVVPAVFL VVPDVLLVCS SCSPGCSSCS PGCSSCSPGC SSCSCGGSSC SPGCSSCFSG
GSRCSPGGSS CSPGCSSCCP GCSSCCPGCS SCSCGCSSCS SGGFQLFFWW FQLFSWWFQM
FIWLFQMFSR FGSSCSPGCS RCSPGLFQMF TSWFPAVHLY LQKSLSILSQ TPPQVFPAVA
ETSCMLCVCR FSSGLMFGVG AMLGSVVLLI RTLQQTYAQM TSDNPRIGAQ QALQVVVPGV
NLPTSQLVYF FTALLLSGVV HELGHAVAAL REQVRVNGFG IFLFVLYPGA FVDLFTTHLN
LISPAQQLRI FCAGVWHNFV LCLAALAFIF LMPVFLFPLY STGGGALVTE VVQGSAADGP
RGLSVGDIVT ALEDCPVRGV EDWTGCLSRL SRLPQMGYCV PVASLQPSWA HGRAFKRLDG
TTDCCSNSSL TDLCFSYSRA ASSREYACIP VRKMVTGTRV CRSDRDCAAR SSAARSSAAS
VCVTPSLENQ TRFIRVTHPP NTHMLFVGYP PHLQHAVTLT NFIPRFSFLH LHVPVFLETF
CKYVVSLSGA LAVVNSVPCF ALDGQWMLNA LLEATLVTVV TDRQKRELVG FFLLLAGSAL
LAANVALGLW MVTAR
//
