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Database: UniProt
Entry: A0A095A2C3_SCHHA
LinkDB: A0A095A2C3_SCHHA
Original site: A0A095A2C3_SCHHA 
ID   A0A095A2C3_SCHHA        Unreviewed;      1209 AA.
AC   A0A095A2C3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Membrane-bound transcription factor site-1 protease {ECO:0000313|EMBL:KGB40987.1};
GN   ORFNames=MS3_09481 {ECO:0000313|EMBL:KGB40987.1};
OS   Schistosoma haematobium (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB40987.1};
RN   [1] {ECO:0000313|EMBL:KGB40987.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22246508; DOI=10.1038/ng.1065;
RA   Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA   Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA   Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA   Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA   Wang J., Gasser R.B.;
RT   "Whole-genome sequence of Schistosoma haematobium.";
RL   Nat. Genet. 44:221-225(2012).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; KL251672; KGB40987.1; -; Genomic_DNA.
DR   RefSeq; XP_012800747.1; XM_012945293.1.
DR   AlphaFoldDB; A0A095A2C3; -.
DR   STRING; 6185.A0A095A2C3; -.
DR   EnsemblMetazoa; XM_012945293.2; XP_012800747.2; MS3_0018327.
DR   GeneID; 24596657; -.
DR   KEGG; shx:MS3_00009089; -.
DR   CTD; 8720; -.
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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1094..1114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1126..1152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          163..460
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        172
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        216
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        401
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1209 AA;  137079 MW;  D5795E72AF2917BE CRC64;
     MPSYEYVSSV VETEFIISYY KHSCAQSRHR FLKSILNSFP LNYSIMERWY PPSNAIEKKS
     DFDVIKTLNL SRMNVSNFIQ YLSNISQIKS VSPQKQINRV LLNYDINDEE FSHNSNRFDS
     RRNLKLFGDS QRYSSPGTLP LDPLKQPWKL LQAEYAWSRG LCGNGVRVGI FDTGLASPDH
     KHFSLSNIIE RTDWTVDITN RSYSDDYIEA LDRHGHGTYV TGLIVAQNPN LYYSKFINSF
     NKHDDSTCPP WGFAPRADLF IFRVFTDTQI SYTSWFLDAF NYAISRKLHV INLSIGGPDF
     LDKPFVDKVL ELSANGILLV SAIGNDGPLF GTLNNPADQM DVLGVGGVDA LGRVARFSSR
     GMTGWELPAG YGRVKPDIVT FSTGVISSNL DGKCRVLSGT SVASPIVTGV VSLLINAALN
     HNANLINHEN GSLYYMNNVD NYPFVPINPI SIKQALIASA NQLDSVRVFG TNSIKWLQET
     DQSSMFEQGA GLVNLQSALE IVQRMKPQAS LMPSYLDLTQ CPYMWPYCSQ PLYSTMQPII
     INITILNSMD VVGRIEKPPI YHPYINYNGH RLHVGISYSQ YLWPWVGYLA VYLSVTPDSI
     DDIIPSSRFS GVAEGYISLV VESYDNIRNL SLSTNLRLPI KANIVPIPHR SKRILFDQFH
     SIHYPSGFIP RDDLTRSKEP LDWLGDHIHT NFLDLYTHLR RKSYFIEVLT STFDCFNASN
     YGTFLIIDPE EEFFPYEVEK LFIDVTEKGL SLIVFADWYN TSVMQSLRFY DTNTRRLWTP
     DTGGSNLPAL NELLRPFEIE FGDSVFSGNY VIGHRTVAYH SGSSLRKFPN QAIANHSGRT
     ALLKVNLVDI GKQFIQHDSM FSKSESETSL EGDKILVNSE PNLRLKPIIG KDPTPAILGL
     WTPIVENVVS EMGRLSIYGD SDCLSSTHLS SNCFWLLDAL LQFSTSSMGR IPRILIEQML
     TPNTDVWFDS SLTAPSRAKN SQLNLYSNVI KKEWDSSTLN TSYLPLEAYY SVKSCYIAPT
     ASISIDKDEP NESFYHPQRL LLYPVELYPS EKLYTTHYCH SFTSILSSDK NSFLISKPKL
     LLQSINDFIQ LDLYTSYNVT FICVIILLIV VCYFCKHCIM YFSNSILYVT GWILSMIRYM
     LVRILFGLYN LWRVHISDFS KKVFSKVYAT NNSTGSSSTT TAETSRLSPS IVQKISQQNR
     CNIHVCVHR
//
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