TOR_SCHMA
ID TOR_SCHMA Reviewed; 419 AA.
AC C4QM85; G3LUQ6; Q9U597;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Tetraspanning orphan receptor {ECO:0000303|PubMed:19281639};
DE AltName: Full=Complement C2 receptor inhibitor tetraspanning {ECO:0000303|PubMed:19281639};
DE AltName: Full=Complement C2 receptor inhibitor trispanning {ECO:0000303|PubMed:10366712};
DE Short=SmCRIT {ECO:0000303|PubMed:10366712};
DE AltName: Full=Trispanning orphan receptor;
DE Short=Sm-TOR {ECO:0000303|PubMed:10366712};
GN Name=TOR {ECO:0000303|PubMed:19281639}; ORFNames=Smp_093840;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Larva {ECO:0000269|PubMed:19281639};
RX PubMed=19281639; DOI=10.1017/s0031182009005757;
RA Lochmatter C., Schifferli J.A., Martin P.J.;
RT "Schistosoma mansoni TOR is a tetraspanning orphan receptor on the parasite
RT surface.";
RL Parasitology 136:487-498(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF21676.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 139-419, SUBCELLULAR LOCATION, AND POTENTIAL
RP USE AS A VACCINE.
RX PubMed=10366712; DOI=10.1016/s0167-4781(99)00051-2;
RA Inal J.M.;
RT "Schistosoma TOR (trispanning orphan receptor), a novel, antigenic surface
RT receptor of the blood-dwelling, Schistosoma parasite.";
RL Biochim. Biophys. Acta 1445:283-298(1999).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND POTENTIAL USE AS A VACCINE.
RX PubMed=23121675; DOI=10.1111/j.1365-2249.2012.04667.x;
RA Lochmatter C., Schneider C.L., Ingram K., Keiser J., Schifferli J.A.;
RT "Schistosoma mansoni tetraspanning orphan receptor (SmTOR): a new vaccine
RT candidate against schistosomiasis.";
RL Clin. Exp. Immunol. 170:342-357(2012).
CC -!- FUNCTION: Cell surface receptor that binds to human complement C2a
CC protein. This results in inhibition of the classical and lectin
CC pathways of complement activation, probably due to interference with
CC binding of C2a to C4b and interference with cleavage by C1 or MASP2
CC such that C3 convertase cannot be formed. This infers resistance to
CC complement-mediated cell lysis, allowing parasite survival and
CC infection (By similarity). {ECO:0000250|UniProtKB:Q5J7P3,
CC ECO:0000250|UniProtKB:Q9BLM6}.
CC -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with human
CC C2a. {ECO:0000250|UniProtKB:Q9BLM6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10366712,
CC ECO:0000269|PubMed:19281639}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10366712, ECO:0000269|PubMed:19281639}.
CC Note=Located on the surface tegumental plasma membrane, and tegumental
CC surface pits of adult schistosomes so in contact with host blood
CC plasma. {ECO:0000269|PubMed:10366712, ECO:0000269|PubMed:19281639}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in parasitic larvae (cercariae)
CC and at a lower level in eggs, miracidiae, schistosomulae and adults.
CC {ECO:0000269|PubMed:19281639}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000250|UniProtKB:Q9BLM6}.
CC -!- BIOTECHNOLOGY: Potential vaccine candidate molecule (PubMed:10366712,
CC PubMed:23121675). Induces an immune response in mice and confers
CC protection against S.mansoni infection (PubMed:23121675).
CC {ECO:0000269|PubMed:23121675, ECO:0000305|PubMed:10366712,
CC ECO:0000305|PubMed:23121675}.
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DR EMBL; JN560697; AEN25587.1; -; mRNA.
DR EMBL; AF051138; AAF21676.1; -; mRNA.
DR AlphaFoldDB; C4QM85; -.
DR TCDB; 2.A.74.1.5; the 4 tms multidrug endosomal transporter (met) family.
DR EnsemblMetazoa; Smp_093840.1; Smp_093840.1; Smp_093840.
DR WBParaSite; Smp_093840.1; Smp_093840.1; Smp_093840.
DR HOGENOM; CLU_1162417_0_0_1; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..419
FT /note="Tetraspanning orphan receptor"
FT /id="PRO_0000412760"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 303..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 257
FT /note="C -> R (in Ref. 2; AAF21676)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="M -> T (in Ref. 2; AAF21676)"
FT /evidence="ECO:0000305"
FT CONFLICT 273..274
FT /note="RG -> KS (in Ref. 2; AAF21676)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..306
FT /note="RNRGNNSI -> PNGSNNPN (in Ref. 2; AAF21676)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="P -> R (in Ref. 2; AAF21676)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="P -> L (in Ref. 2; AAF21676)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="D -> G (in Ref. 2; AAF21676)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="A -> T (in Ref. 2; AAF21676)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="L -> V (in Ref. 2; AAF21676)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="T -> I (in Ref. 2; AAF21676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46712 MW; 16D6B81CA4E561D4 CRC64;
MPRAPALLTN DARHQFTCCL CLHVRTGTII FGITQIIIQL VFISFLFLMT FNPRLIPEDN
HGNTDPSEDK IRFYVFSTLF RLVPAVSDIH ESLTLPSPGT RNVNGNKLYL GHNVESETNF
NYDIPPGYKD DVLVDVNNMS PSLVSYTQKN ERGSHEVKIK HFSPYIAVCV TTFSLAFCCF
MVHGAITKQP THLLPFFFIQ VFDLIICLIH ILGFMSSTSD LRLMIHTKTG PIYIKSTGFT
FIILSISCMM LAFKAYCLGM VWDCYKYLML NRRGNLLDDW YSDQWGHLST FWSLLRAGRN
RGNNSIGNSG SPNEPNTRPR PEPITYDPAN DLPKYEDILK IPANAYAPPP YYCSNINGNV
NTTEASAVTT NTSNSATAAN TTTTTTNTGT TTSVISTLTT TNKDDTQINS APSNAHSSC
