ID M3YC21_MUSPF Unreviewed; 1050 AA.
AC M3YC21;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Membrane bound transcription factor peptidase, site 1 {ECO:0000313|Ensembl:ENSMPUP00000008878.1};
DE SubName: Full=Membrane-bound transcription factor site-1 protease {ECO:0000313|RefSeq:XP_004753962.1};
GN Name=MBTPS1 {ECO:0000313|Ensembl:ENSMPUP00000008878.1,
GN ECO:0000313|RefSeq:XP_004753962.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000008878.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000008878.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004753962.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004753962.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; AEYP01035253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01035254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004753962.1; XM_004753905.3.
DR STRING; 9669.ENSMPUP00000008878; -.
DR MEROPS; S08.063; -.
DR Ensembl; ENSMPUT00000009022.1; ENSMPUP00000008878.1; ENSMPUG00000008948.1.
DR GeneID; 101691039; -.
DR KEGG; mpuf:101691039; -.
DR CTD; 8720; -.
DR eggNOG; KOG4266; Eukaryota.
DR GeneTree; ENSGT00490000043404; -.
DR HOGENOM; CLU_004504_1_0_1; -.
DR OMA; LEYTTTG; -.
DR OrthoDB; 5606at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0005795; C:Golgi stack; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0007040; P:lysosome organization; 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:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IEA:Ensembl.
DR CDD; cd07479; Peptidases_S8_SKI-1_like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; 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; 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 Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; 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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1050
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041158864"
FT TRANSMEM 1000..1020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 209..464
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 875..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 249
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 414
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1050 AA; 117303 MW; 1EB230CADF4DAB7F CRC64;
MKLVNIWLLL LVVLLCGRKH LGDRLEKKSF EKAPCPGCSH LTLKVEFSST VVEYEYIVAF
NGYFTAKARN SFISSALKSS EIDNWRIIPR NNPSSDYPSD FEVIQIKEKQ KAGLLTLEDH
PNIKRVTPQR KVFRSLKYAE SDPVAPCNET RWSQKWQSSR PLRRASLSLG SGFWHATGRH
SSRRLLRAIP RQVAQTLQAD VLWQMGYTGA NVRVAVFDTG LSEKHPHFKN VKERTNWTNE
RTLDDGLGHG TFVAGVIASM RECQGFAPDA ELHIFRVFTN NQVSYTSWFL DAFNYAILKK
MDVLNLSIGG PDFMDHPFVD KVWELTANNV IMVSAIGNDG PLYGTLNNPA DQMDVIGVGG
IDFEDNIARF SSRGMTTWEL PGGYGRVKPD IVTYGAGVRG SGVKGGCRAL SGTSVASPVV
AGAVTLLVST VQKRELVNPA SMKQALIASA RRLPGVNMFE QGHGKLDLLR AYQILNSYKP
QASLSPSYID LTECPYMWPY CSQPIYYGGM PTVANITVLN GMGVTGRIVD KPDWQPYLPQ
NGDNIEVAFS YSSVLWPWSG YLAISISVTK KAASWEGVAQ GHVTVTVASP AESKNGAEQT
STVKLPIKVK IIPAPPRSKR VLWDQYHNLR YPPGYFPRDN LRMKNDPLDW NGDHIHTNFR
DMYQHLRSMG YFVEVLGSPF TCFDASQYGT LLMVDSEEEY FPEEVAKLRR DVDNGLSLIV
FSDWYNTSVM RKVKFYDENT RQWWMPDTGG ANVPALNELL SVWNMGFSDG LYEGDFTLAN
HDMYYASGCS IAKFPEDGIV ITQTFKDQGL EVLKQETAVV ENVPILGLYQ IPTEGGGRIV
LYGDSNCLDD SHRQRDCFWL LDALLQYTSY GVTPPSLSHS GNRQRPPSGA GSATPERMEG
NHLHRYSKVL EARLGGPEPR ALPACPHLSW AKPQPLNETA PSNLWKHQKL LSIDLDKVVL
PNFRSNRPQV RPLSPGESGA WDIPGGIMPG RYNQEVGQTI PVFAFLGAMV VLAFFVVQIN
KARSRPKRRK PRVKRPQLVQ QAHPPKTPSV
//
