GRA3_TOXGO
ID GRA3_TOXGO Reviewed; 222 AA.
AC B6KEU8; B9PMW9; B9Q877; Q27914; Q8MWP7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 3.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Dense granule protein 3 {ECO:0000312|EMBL:AAN03693.1};
DE AltName: Full=P30 {ECO:0000303|PubMed:7739670};
GN Name=GRA3 {ECO:0000312|EMBL:ABQ41276.1};
GN Synonyms=Tg556 {ECO:0000303|PubMed:19127325};
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=RH {ECO:0000269|PubMed:16149193};
RX PubMed=16149193; DOI=10.1017/s0031182005007559;
RA Henriquez F.L., Nickdel M.B., McLeod R., Lyons R.E., Lyons K.,
RA Dubremetz J.F., Grigg M.E., Samuel B.U., Roberts C.W.;
RT "Toxoplasma gondii dense granule protein 3 (GRA3) is a type I transmembrane
RT protein that possesses a cytoplasmic dilysine (KKXX) endoplasmic reticulum
RT (ER) retrieval motif.";
RL Parasitology 131:169-179(2005).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HOST CAMLG, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=RH {ECO:0000269|PubMed:19127325};
RC TISSUE=Tachyzoite {ECO:0000269|PubMed:19127325};
RX PubMed=19127325; DOI=10.3347/kjp.2008.46.4.209;
RA Kim J.Y., Ahn H.J., Ryu K.J., Nam H.W.;
RT "Interaction between parasitophorous vacuolar membrane-associated GRA3 and
RT calcium modulating ligand of host cell endoplasmic reticulum in the
RT parasitism of Toxoplasma gondii.";
RL Korean J. Parasitol. 46:209-216(2008).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAN03693.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=RH {ECO:0000312|EMBL:AAN03693.1};
RC TISSUE=Tachyzoite {ECO:0000312|EMBL:AAN03693.1};
RA Henriquez F.L., Roberts C.W.;
RT "Identification and characterization of a Toxoplasma gondii protein with a
RT N-terminal portion identical to GRA3.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAN03693.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=RH {ECO:0000312|EMBL:ABQ41276.1};
RC TISSUE=Tachyzoite {ECO:0000312|EMBL:ABQ41276.1};
RA Chen Y., Yu L., Zhang S.;
RT "Cloning and sequencing of the CRA3 gene from Toxoplasma gondii RH
RT strain.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-146.
RC STRAIN=RH {ECO:0000269|PubMed:7739670};
RC TISSUE=Tachyzoite {ECO:0000269|PubMed:7739670};
RX PubMed=7739670; DOI=10.1016/0166-6851(94)90169-4;
RA Bermudes D., Dubremetz J.-F., Achbarou A., Joiner K.A.;
RT "Cloning of a cDNA encoding the dense granule protein GRA3 from Toxoplasma
RT gondii.";
RL Mol. Biochem. Parasitol. 68:247-257(1994).
CC -!- FUNCTION: Direct host-parasite interaction occurs at the cytoplasmic
CC faces of the parasitophorous vacuole membrane (PVM) and the host
CC endoplasmic reticulum (ER) membrane via GRA3 and host CAMLG
CC association. Direct insertion of GRA3 ER retrieval motif into the host
CC ER membrane contributes to the host ER recruitment to the PVM.
CC {ECO:0000269|PubMed:19127325}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts (via N-terminus) with human
CC host CAMLG (via N-terminus). {ECO:0000269|PubMed:16149193,
CC ECO:0000269|PubMed:19127325, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16149193,
CC ECO:0000269|PubMed:19127325}. Host endoplasmic reticulum
CC {ECO:0000269|PubMed:16149193, ECO:0000269|PubMed:19127325}.
CC Parasitophorous vacuole membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Located in dense granules of tachyzoites.
CC Upon infection, secreted to the PVM. {ECO:0000255,
CC ECO:0000269|PubMed:16149193, ECO:0000269|PubMed:19127325}.
CC -!- DOMAIN: The KKXX motif functions as an ER retrieval signal that
CC rationalizes association with PVM and the host cell ER.
CC {ECO:0000269|PubMed:16149193}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13772.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA, matches the N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC13773.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC13773.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA, matches the N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF414079; AAN03693.1; -; mRNA.
DR EMBL; EF552406; ABQ41276.1; -; mRNA.
DR EMBL; U13771; AAC13772.1; ALT_SEQ; mRNA.
DR EMBL; U13771; AAC13773.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; B6KEU8; -.
DR VEuPathDB; ToxoDB:TGARI_227280; -.
DR VEuPathDB; ToxoDB:TGCAST_227280; -.
DR VEuPathDB; ToxoDB:TGCOUG_227280; -.
DR VEuPathDB; ToxoDB:TGDOM2_227280; -.
DR VEuPathDB; ToxoDB:TGFOU_227280; -.
DR VEuPathDB; ToxoDB:TGGT1_227280; -.
DR VEuPathDB; ToxoDB:TGMAS_227280; -.
DR VEuPathDB; ToxoDB:TGME49_227280; -.
DR VEuPathDB; ToxoDB:TGP89_227280; -.
DR VEuPathDB; ToxoDB:TGPRC2_227280; -.
DR VEuPathDB; ToxoDB:TGRH88_046790; -.
DR VEuPathDB; ToxoDB:TGRUB_227280; -.
DR VEuPathDB; ToxoDB:TGVAND_227280; -.
DR VEuPathDB; ToxoDB:TGVEG_227280; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020005; C:symbiont-containing vacuole membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Cytoplasm; Host endoplasmic reticulum; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..222
FT /note="Dense granule protein 3"
FT /id="PRO_0000398815"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 219..222
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000269|PubMed:16149193"
FT CONFLICT 80
FT /note="G -> C (in Ref. 5; AAC13772/AAC13773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 24242 MW; 566766C70C14B942 CRC64;
MDRTICPFFI QSFTMSTALK RLIPFLVPFV VFLVAAALGG LAADQPENHQ ALAEPVTGVG
EAGVSPVNEA GESYSSATSG VQEATAPGAV LLDAIDAESD KVDNQAEGGE RMKKVEEELS
LLRRELYDRT DRPGLKRAVI LSLATSAAIG GRMVSRTLRD NIPGYFVVIN AILAAYYIRK
VLTYRRRVMT KRQPFMSSVK NFFRRKPKDE GAGVDKASKK QT
