ID   TOR_SCHHA               Reviewed;         313 AA.
AC   Q9BLM6;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Tetraspanning orphan receptor {ECO:0000250|UniProtKB:C4QM85};
DE   AltName: Full=Complement C2 receptor inhibitor tetraspanning {ECO:0000250|UniProtKB:C4QM85};
DE   AltName: Full=Complement C2 receptor inhibitor trispanning {ECO:0000303|PubMed:10734221};
DE   AltName: Full=Trispanning orphan receptor {ECO:0000312|EMBL:AAK11492.1};
DE            Short=Sh-TOR {ECO:0000303|PubMed:10366712, ECO:0000303|PubMed:10734221};
DE   Flags: Fragment;
GN   Name=TOR {ECO:0000303|PubMed:10366712, ECO:0000303|PubMed:10734221};
GN   Synonyms=TM3 {ECO:0000312|EMBL:AAK11492.1};
OS   Schistosoma haematobium (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6185;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAK11492.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, AND PHOSPHORYLATION.
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   [2] {ECO:0000305}
RP   FUNCTION, AND INTERACTION WITH HUMAN C2B.
RX   PubMed=10734221; DOI=10.1016/s0014-5793(00)01304-1;
RA   Inal J.M., Sim R.B.;
RT   "A Schistosoma protein, Sh-TOR, is a novel inhibitor of complement which
RT   binds human C2.";
RL   FEBS Lett. 470:131-134(2000).
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. {ECO:0000250|UniProtKB:Q5J7P3, ECO:0000269|PubMed:10366712,
CC       ECO:0000269|PubMed:10734221}.
CC   -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with human
CC       C2a. {ECO:0000269|PubMed:10734221}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10366712};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:10366712}. Note=Located
CC       on the surface tegumental plasma membrane, and tegumental surface pits
CC       of adult schistosomes so in contact with host blood plasma.
CC       {ECO:0000269|PubMed:10366712}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in parasitic larvae (cercariae)
CC       and at a lower level in adults. {ECO:0000269|PubMed:10366712}.
CC   -!- PTM: Phosphorylated on tyrosine residues.
CC       {ECO:0000269|PubMed:10366712}.
CC   -!- MISCELLANEOUS: Specifically and strongly recognized by a serum from
CC       baboons vaccinated with irradiated parasite. Potential vaccine
CC       candidate molecule. {ECO:0000269|PubMed:10366712,
CC       ECO:0000303|PubMed:10366712}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK11492.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U57714; AAK11492.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q9BLM6; -.
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; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..313
FT                   /note="Tetraspanning orphan receptor"
FT                   /id="PRO_0000412758"
FT   TOPO_DOM        <1..54
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        76..82
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..129
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..313
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          192..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   313 AA;  34846 MW;  60DA5651B27BEF1B CRC64;
     PQCESETNFH YDIPPGYKDD VLVDVNNMSP SLVSDTQKHE RGSHEVKIKH FSPYIAVCVT
     TFSLAFCCFM VHAAITRQPT HLLPFFFIQV FDLIICLIHI LGFMSSTSDI RLVIHTKTGP
     IYIKSTGLTF IILSISCMML AFKAYCLGMV WDCYKYLMLN RRGNLLDDWY SDQWGHLSTF
     WSLLRTGRNR GNNSIGNSGS PNEPNTRPRP DTITYDPAND LPKYEDILKI RNAYAPPPYY
     CSNTNGNVNT TTTDAVTTNT TITSATTANA TTTITTNANT NTSTTTSVIS PLTTTNKDDT
     QINNASSNAH SSC