ID A0A0B2V3V4_TOXCA Unreviewed; 1004 AA.
AC A0A0B2V3V4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Membrane-bound transcription factor site-1 protease {ECO:0000313|EMBL:KHN76164.1};
GN Name=MBTPS1 {ECO:0000313|EMBL:KHN76164.1};
GN ORFNames=Tcan_05185 {ECO:0000313|EMBL:KHN76164.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN76164.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN76164.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN76164.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHN76164.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPKZ01002567; KHN76164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2V3V4; -.
DR STRING; 6265.A0A0B2V3V4; -.
DR OMA; LEYTTTG; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1004
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002095898"
FT TRANSMEM 958..980
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 142..399
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 348
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1004 AA; 111307 MW; E4C49441B8FE8506 CRC64;
MFGRAVCLVA AASLVRLAAI SVSCKSESKS FIVTFDGYYM SSNRLRSIVE AVGRNQTINV
EQRPNRLSDF DVIEVSACNA SRVVDCLRKS LRVRHVSPNV AFQAHAPSRR TLGRRGGTAS
LEIHQVTKVL NANKLWDMGF KGQGVKVAVF DTGLSQHHPH FRQIVERTDW TNEQTADDGL
GHGTFVTGII ASSNKKCAGF APAASIYVYK VFTKKQVSFT SWFLDAFNHA ILRSINVLNL
SIGGPDFTDL PFMDKVWELT ANGVILISAI GNDGPKFGTL NNPADQMDVI GVGGINIDSK
VARFSSRGMT TWELPGGYGR VKPDIVTFGA SVYGSALDGG CRALSGTSVA SPVVAGAVTV
MLSGIDDHRL WNPAVVKQAL VEGAVRLPNA ATMFEQGAGR IDLLASFDYM RKYEPSITLI
PPYIDFTECP YMWPYCSQPL YVSTIPTIVN VTIINGLGVS GRIVEPVTII NGLGVSGRIV
EPPIWEPFVD ENGDLLKISI SYPDLLWPWS GYMAVAMSVA QDGKSYEGTA AGRITVTVTT
DAHGMKKRST ATFMLRVRII PTPPRSQRII WDQYRNMRYP PGYLPRDDLR DRANPLDWTA
DHPHTNFKAL YQHLRSGGYH IEVLGEPLTC VDLSEYAMYI VVDPEDEFFA SEREKLYLDV
VDAGLNLVVF ADWFNATVID KIRFLDENTK QWWQPETGGT NLPALNDLLS HWNITLGAQV
FDGMVTLGRT AIKYSSGTSI VRTPPGSWVA EANLTDLGAE TITGEKSAQF YETAVFTFYR
SENISKQKPG FVAVFGDSTC LEVGTSVELK GCIPLLDALL ESANEGDLSE NLRRVLKPME
IVFPEEGSSA IPLPKRITTS NFAKYSKVIS GFEDDGSPIF RPQPQCRRFP ISVPHPVTNV
TSPSDLNEER RQNGRAESFY DKIRSDATAA QFHELDQFFD ANTDLDRRVV FTQTISILAY
YNISYVIWGF IVVAIFAFYY RSSLRRTVLQ IRVFRRVLRR LRIA
//