ID A0A2K6U1M6_SAIBB Unreviewed; 507 AA.
AC A0A2K6U1M6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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 Name=MBTPS2 {ECO:0000313|Ensembl:ENSSBOP00000025805.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000025805.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000025805.1}
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 RefSeq; XP_003924148.1; XM_003924099.2.
DR AlphaFoldDB; A0A2K6U1M6; -.
DR STRING; 39432.ENSSBOP00000025805; -.
DR Ensembl; ENSSBOT00000042674.1; ENSSBOP00000025805.1; ENSSBOG00000029363.1.
DR GeneID; 101045752; -.
DR KEGG; sbq:101045752; -.
DR CTD; 51360; -.
DR GeneTree; ENSGT00510000048066; -.
DR OMA; FYSWGRW; -.
DR OrthoDB; 5181at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:Ensembl.
DR GO; GO:0140537; F:transcription regulator activator activity; IEA:Ensembl.
DR GO; GO:0070977; P:bone maturation; IEA:Ensembl.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IEA:Ensembl.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0051604; P:protein maturation; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR CDD; cd06162; S2P-M50_PDZ_SREBP; 1.
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:UP000233220};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..486
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 507 AA; 56389 MW; 3E3E89E0F1CA98FE CRC64;
MIPVSLVVVV VGGWTVVYLT DLVLKSSVYF KHSYEDWLEN NGLSISPFHI RWQTAVFNRA
FYSWGRRKAR MLYQWFNFGM VFGVIAMFSS FFLLGKTLMQ TLAQMMADSP SSYSSSSSSS
SSSSLHNEQV LQVVVPGINL PVNQLTYFFA AVLVSGVVHE IGHGIAAIRE QVRFNGFGIF
LFIIYPGAFV DLFTTHLQLI SPVQQLRIFC AGIWHNFVLA LLGILALVLL PVILLPFYYT
GVGVLITEVA EDSPAIGPRG LFVGDLVTHL QDCPVTNVQD WNECLDTIAY EPQIGYCISA
STLQQLSFPV RAYKRLDGST ECCNNHSLTD VCFSYRNNFN KRLHTCLPAR KAVEATQVCR
TNKDCEKSSS SNFCIIPSLE TDTRLIKVKH PPQIDMLYVG HPLHLHYTVS ITSFIPRFNF
LSIDLPVVVE TFVKYLISLS GALAIVNAVP CFALDGQWIL NSFLDATLTS VIGDNDVRDL
IGFFILLGGS VLLAANVTLG LWMVTAR
//
