Mbtps1
entrez
56453
canonical
uniprot
Q9WTZ2
canonical
ensembl
ENSMUSG00000031835
resolver
ensp
ENSMUSP00000080117
resolver
ensp
ENSMUSP00000095965
resolver
ensp
ENSMUSP00000203793
resolver
ensp
ENSMUSP00000203795
resolver
ensp
ENSMUSP00000203796
resolver
ensp
ENSMUSP00000203821
resolver
ensp
ENSMUSP00000203822
resolver
enst
ENSMUST00000081381
resolver
enst
ENSMUST00000098362
resolver
genesymbol
Mbtps1
resolver
genesymbol_syn
S1p
resolver
genesymbol_syn
Ski1
resolver
uniprot
Q6PG67
resolver
uniprot_entry
MBTP1_MOUSE
resolver
uniprot_sec
Q6PG67
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by divalent copper and zinc ions, but not by nickel or cobalt. Inhibited by its prosegment, but not smaller fragments. Inhibited by 4-(2-aminoethyl)benzenesulfonyl fluoride (AEBSF), a serine protease inhibitor. {ECO:0000250|UniProtKB:Q14703}.
uniprot
proteins
amino_acid_sequence
MKLVSTWLLVLVVLLCGKRHLGDRLGTRALEKAPCPSCSHLTLKVEFSSTVVEYEYIVAFNGYFTAKARNSFISSALKSSEVENWRIIPRNNPSSDYPSDFEVIQIKEKQKAGLLTLEDHPNIKRVTPQRKVFRSLKFAESNPIVPCNETRWSQKWQSSRPLKRASLSLGSGFWHATGRHSSRRLLRAIPRQVAQTLQADVLWQMGYTGANVRVAVFDTGLSEKHPHFKNVKERTNWTNERTLDDGLGHGTFVAGVIASMRECQGFAPDAELHIFRVFTNNQVSYTSWFLDAFNYAILKKMDVLNLSIGGPDFMDHPFVDKVWELTANNVIMVSAIGNDGPLYGTLNNPADQMDVIGVGGIDFEDNIARFSSRGMTTWELPGGYGRVKPDIVTYGAGVRGSGVKGGCRALSGTSVASPVVAGAVTLLVSTVQKRELVNPASVKQALIASARRLPGVNMFEQGHGKLDLLRAYQILSSYKPQASLSPSYIDLTECPYMWPYCSQPIYYGGMPTIVNVTILNGMGVTGRIVDKPEWRPYLPQNGDNIEVAFSYSSVLWPWSGYLAISISVTKKAASWEGIAQGHIMITVASPAETELHSGAEHTSTVKLPIKVKIIPTPPRSKRVLWDQYHNLRYPPGYFPRDNLRMKNDPLDWNGDHVHTNFRDMYQHLRSMGYFVEVLGAPFTCFDATQYGTLLLVDSEEEYFPEEIAKLRRDVDNGLSLVIFSDWYNTSVMRKVKFYDENTRQWWMPDTGGANIPALNELLSVWNMGFSDGLYEGEFVLANHDMYYASGCSIAKFPEDGVVITQTFKDQGLEVLKQETAVVENVPILGLYQIPSEGGGRIVLYGDSNCLDDSHRQKDCFWLLDALLQYTSYGVTPPSLSHSGNRQRPPSGAGLAPPERMEGNHLHRYSKVLEAHLGDPKPRPLPACPHLSWAKPQPLNETAPSNLWKHQKLLSIDLDKVVLPNFRSNRPQVRPLSPGESGAWDIPGGIMPGRYNQEVGQTIPVFAFLGAMVALAFFVVQISKAKSRPKRRRPRAKRPQLAQQAHPARTPSV
uniprot
proteins
ec_number
3.4.21.112
uniprot
proteins
function
FUNCTION: Serine protease that cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4: known substrates include SREBF1/SREBP1, SREBF2/SREBP2, BDNF, GNPTAB, ATF6, ATF6B and FAM20C (By similarity). Cleaves substrates after Arg-Ser-Val-Leu (SREBP2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu (By similarity). Catalyzes the first step regulated intramembrane proteolysis activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 (By similarity). Also mediates the first step of the regulated intramembrane proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B) (By similarity). Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysosomes (By similarity). Cleaves the propeptide from FAM20C which is required for FAM20C secretion from the Golgi apparatus membrane and for enhancement of FAM20C kinase activity, promoting osteoblast differentiation and biomineralization (PubMed:34349020). Involved in the regulation of M6P-dependent Golgi-to-lysosome trafficking of lysosomal enzymes (By similarity). It is required for the activation of CREB3L2/BBF2H7, a transcriptional activator of MIA3/TANGO and other genes controlling mega vesicle formation (By similarity). Therefore, it plays a key role in the regulation of mega vesicle-mediated collagen trafficking (By similarity). Promotes FAD binding to the ETFA/ETFB complex and is therefore involved in mitochondrial respiratory chain regulation (By similarity). In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the first step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression (By similarity). {ECO:0000250|UniProtKB:Q14703, ECO:0000269|PubMed:34349020}.
uniprot
proteins
mass_dalton
117457
uniprot
proteins
post_translational_modification
PTM: The 148 kDa zymogen is processed progressively into two membrane-bound 120 and 106 kDa forms in the endoplasmic reticulum, and into a secreted 98 kDa form. The propeptide is autocatalytically removed through an intramolecular cleavage after Leu-186. Further cleavage generates 14, 10, and 8 kDa intermediates. {ECO:0000250|UniProtKB:Q14703}.
uniprot
proteins
protein_family
Peptidase S8 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
34349020
uniprot
proteins
pubmed
35362222
uniprot
proteins
pubmed
9990022
uniprot
proteins
sequence_length
1052
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14703}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:9990022}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:Q14703}. Mitochondrion {ECO:0000250|UniProtKB:Q14703}. Note=May sort to other organelles, including lysosomal and/or endosomal compartments. The 98 kDa form is secreted. {ECO:0000250|UniProtKB:Q14703}.
uniprot
proteins
transmembrane_region
TRANSMEM 1000..1022; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins