ID A0A671PGE9_9TELE Unreviewed; 1081 AA.
AC A0A671PGE9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Membrane-bound transcription factor site-1 protease {ECO:0000256|ARBA:ARBA00067283};
DE EC=3.4.21.112 {ECO:0000256|ARBA:ARBA00066596};
DE AltName: Full=Endopeptidase S1P {ECO:0000256|ARBA:ARBA00081324};
GN Name=LOC107672278 {ECO:0000313|Ensembl:ENSSANP00000056940.1};
OS Sinocyclocheilus anshuiensis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=1608454 {ECO:0000313|Ensembl:ENSSANP00000056940.1, ECO:0000313|Proteomes:UP000472260};
RN [1] {ECO:0000313|Ensembl:ENSSANP00000056940.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSANP00000056940.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Processes precursors containing basic and
CC hydrophobic/aliphatic residues at P4 and P2, respectively, with a
CC relatively relaxed acceptance of amino acids at P1 and P3.;
CC EC=3.4.21.112; Evidence={ECO:0000256|ARBA:ARBA00050826};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004194}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004194}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR RefSeq; XP_016320896.1; XM_016465410.1.
DR AlphaFoldDB; A0A671PGE9; -.
DR Ensembl; ENSSANT00000060600.1; ENSSANP00000056940.1; ENSSANG00000028253.1.
DR GeneID; 107672278; -.
DR KEGG; sanh:107672278; -.
DR OrthoDB; 1740355at2759; -.
DR Proteomes; UP000472260; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07479; Peptidases_S8_SKI-1_like; 1.
DR FunFam; 3.40.50.200:FF:000008; Membrane-bound transcription factor site-1 protease preproprotein; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR055143; MBTP1_N.
DR InterPro; IPR057060; MBTPS1_3rd.
DR InterPro; IPR057032; MBTPS1_4th.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR050131; Peptidase_S8_subtilisin-like.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034185; Site-1_peptidase_cat_dom.
DR PANTHER; PTHR43806:SF7; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-1 PROTEASE; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF23001; MBTP1_N; 1.
DR Pfam; PF23094; MBTPS1_3rd; 1.
DR Pfam; PF23090; MBTPS1_4th; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000472260};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1081
FT /note="Membrane-bound transcription factor site-1 protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025648155"
FT TRANSMEM 1026..1046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..149
FT /note="Membrane-bound transcription factor site-1 protease-
FT like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF23001"
FT DOMAIN 233..488
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 509..640
FT /note="MBTPS1 third"
FT /evidence="ECO:0000259|Pfam:PF23094"
FT DOMAIN 641..907
FT /note="MBTPS1 fourth"
FT /evidence="ECO:0000259|Pfam:PF23090"
FT REGION 903..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1061
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 242
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 438
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1081 AA; 120430 MW; 7012260F36F323AD CRC64;
MGNDQKRTAG TMIVRLCLLV AFLGGRLPLV GTEEDSGPFS TPFPSPLNAD ALLSPNCSQL
TLKLGFSTKV VKHEYIVAFN GYFTAKARSD FISSALRDVD AVNWRIVRRD NPASDYPSDF
EVVEIRQDAR SSLLTLQDHP YIKRVTPQRM VLRSLKLTDS GTDGASPCND TRWVQKWQSW
QSSRPLRRTS LSLGYGFWHA TGRHSSRRLL RAIPRHVAQI LQADVLWQMG HTGSGVKVAV
FDTGLSEKHP HFKNVKERTN WTNEKTLDDG LGHGTFVAGV IASMRECQGF APDSELHIFR
VFTNSQVSYT SWFLDAFNYA ILKKIDVLNL SIGGPDFMDH PFVDKVWELT ANKAIMASAI
GNDGPLYGTL NNPADQMDVI GVGGIDFEDN IARFSSRGMT TWELPGGYGR VKPDIVTYGS
GVRGSGLKEG CRSLSGTSVA SPVVAGAVTL LASTVLNREL VNPASMKQAL IASARRLPGV
NMFEQGHGKL DLLRAYQILN SYKPQASLSP SYIDLTECPY MWPYCSQPIY YGGMPTIVNV
TILNGMGVTG RIVDKPIWQP YLPQNGDYVD VAVSYSPVLW PWAGYLAVSI SVAKKAASWE
GIAQGHVMVT VASPAENDSA IGGEMTSTVK LPVKVKIVPT PPRSKRILWD QYHNLRYPPG
YFPRDNLRMK NDPLDWNGDH IHTNFRDMYQ HLRSMGYFVE VLGAPITCFD ASQYGTLLMV
DSEEEYFPEE ITKLRRDIDN GLSLMIFSDW YNTSVMRKVK FYDENTRQWW MPDTGGANVP
ALNDLISVWG MAFSDGLYEG DFTMADHDMY YASGCSIASF PEDGIVIAQT LKDQGLEVLK
QETAVVENVP VLGLYQTPSE GGGRIALYGD SNCIDDSHRQ KDCFWLLDAL LQYTSYSMTP
PSLTHSKNRV VPPTGTDRPL PQRLEGNHLY RYSKVLEAHL GDPKPRPLPA CPHLSWAKPQ
PLNETAPSNL WKHQKLLSVD MDKVVLPNVR PYRPQVRPLS PGESGAWDIP GGIMPGRYNQ
EVGQTIPMFA FLGAMVVLSF FVVQLTKAKS KPKRRKPRVK RPLYLQQQQQ QTPHSGKNPT
V
//
