RASP2_TOXGG
ID RASP2_TOXGG Reviewed; 437 AA.
AC S7UMJ0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Rhoptry apical surface protein 2 {ECO:0000303|PubMed:31492901};
DE Short=TgRASP2 {ECO:0000303|PubMed:31492901};
GN Name=RASP2 {ECO:0000303|PubMed:31492901};
GN ORFNames=TGGT1_315160 {ECO:0000312|EMBL:EPR58892.1};
OS Toxoplasma gondii (strain ATCC 50853 / GT1).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=507601 {ECO:0000312|Proteomes:UP000005641};
RN [1] {ECO:0000312|Proteomes:UP000005641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50853 / GT1 {ECO:0000312|Proteomes:UP000005641};
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RASP1 AND RASP3, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 62-PHE--LEU-179; 123-LYS--LYS-129; 230-GLU--GLU-363 AND 380-LYS--THR-387.
RX PubMed=31492901; DOI=10.1038/s41467-019-11979-z;
RA Suarez C., Lentini G., Ramaswamy R., Maynadier M., Aquilini E.,
RA Berry-Sterkers L., Cipriano M., Chen A.L., Bradley P., Striepen B.,
RA Boulanger M.J., Lebrun M.;
RT "A lipid-binding protein mediates rhoptry discharge and invasion in
RT Plasmodium falciparum and Toxoplasma gondii parasites.";
RL Nat. Commun. 10:4041-4041(2019).
CC -!- FUNCTION: Essential for tachyzoite invasion of host cells by
CC controlling rhoptry secretion (PubMed:31492901). Binds to phosphatidic
CC acid (PA) and phosphatidylinositol 4,5-bisphosphate (PIP2) lipids and
CC thus, likely contributes to the assembly of the machinery that docks or
CC primes the rhoptry to the parasite cell membrane prior to the fusion
CC with the host cell membrane (PubMed:31492901).
CC {ECO:0000269|PubMed:31492901}.
CC -!- SUBUNIT: Interacts with RASP1 (PubMed:31492901). Interacts with RASP3
CC (PubMed:31492901). {ECO:0000269|PubMed:31492901}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, rhoptry
CC membrane {ECO:0000269|PubMed:31492901}; Peripheral membrane protein
CC {ECO:0000269|PubMed:31492901}; Cytoplasmic side
CC {ECO:0000269|PubMed:31492901}. Note=Localizes to the extremity of the
CC neck of the rhoptry (PubMed:31492901). Associates only with mature
CC rhoptries (PubMed:31492901). {ECO:0000269|PubMed:31492901}.
CC -!- DEVELOPMENTAL STAGE: Expressed in tachyzoites (at protein level).
CC {ECO:0000269|PubMed:31492901}.
CC -!- DOMAIN: The C2 domain is a non-calcium binding domain
CC (PubMed:31492901). Cooperates with the PH domain in the binding to
CC phosphatidic acid (PA) and phosphatidylinositol 4,5-bisphosphate (PIP2)
CC (PubMed:31492901). {ECO:0000269|PubMed:31492901}.
CC -!- DOMAIN: The PH domain cooperates with the C2 domain in the binding to
CC phosphatidic acid (PA) and phosphatidylinositol 4,5-bisphosphate
CC (PIP2). {ECO:0000269|PubMed:31492901}.
CC -!- DISRUPTION PHENOTYPE: Intracellular replication, parasite egress and
CC motility occur normally; however, host cell invasion is severely
CC reduced (PubMed:31492901). Complete inhibition of rhoptry secretion
CC without affecting microneme secretion or rhoptry morphology
CC (PubMed:31492901). {ECO:0000269|PubMed:31492901}.
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; AAQM03000250; EPR58892.1; -; Genomic_DNA.
DR SMR; S7UMJ0; -.
DR EnsemblProtists; EPR58892; EPR58892; TGGT1_315160.
DR VEuPathDB; ToxoDB:TGGT1_315160; -.
DR Proteomes; UP000005641; Unassembled WGS sequence.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Membrane.
FT CHAIN 1..437
FT /note="Rhoptry apical surface protein 2"
FT /id="PRO_0000456209"
FT DOMAIN 45..179
FT /note="C2"
FT /evidence="ECO:0000305|PubMed:31492901"
FT DOMAIN 230..338
FT /note="PH"
FT /evidence="ECO:0000305|PubMed:31492901"
FT MUTAGEN 62..179
FT /note="Missing: Mislocalizes to the cytoplasm. Impairs
FT tachyzoite lytic cycle."
FT /evidence="ECO:0000269|PubMed:31492901"
FT MUTAGEN 123..129
FT /note="KIFLFKK->DIFLFDD: No defect in subcellular
FT localization and tachyzoite lytic cycle. Impairs tachyzoite
FT lytic cycle; when associated with 230-E--E-363 DEL."
FT /evidence="ECO:0000269|PubMed:31492901"
FT MUTAGEN 230..363
FT /note="Missing: No defect in subcellular localization and
FT tachyzoite lytic cycle. Impairs tachyzoite lytic cycle;
FT when associated with 123-D--D-129 but not when associated
FT with 380-K--T-387."
FT /evidence="ECO:0000269|PubMed:31492901"
FT MUTAGEN 380..387
FT /note="Missing: No defect in subcellular localization and
FT tachyzoite lytic cycle. Impairs tachyzoite lytic cycle;
FT when associated with 230-E--E-363 DEL and 123-D--D-129."
FT /evidence="ECO:0000269|PubMed:31492901"
SQ SEQUENCE 437 AA; 49682 MW; 75591F8C06986295 CRC64;
MALVLRLMGG AAGMGAKAVG GACCELGSAC FRQITKGLPH PTECGCLGSL FFYLGIHDHQ
KFNVLVEIHE LDRVPKSCSL YMTIEAGRWS ATSQVVKVKG QDQRVVVEER LMVHIRQVDN
EVKIFLFKKG LVKTTRLANL VLKVKEDMID KKFPKRTWYN MKVENGKSQP RINLSLHKLD
PGLPTNQSPL LQQAMLIAQQ EADEKGEELK LDLAKMTAKE RLTFFSQVLE GPLERLNANG
GACMQFYYKA VEVKPDRWEW CYWESAAACK EGKEKEGSIP FLAISLVLPD RKNRNVFFVR
YHDKDNQHDV FFRRVDRDRN LWSDGLYEFI EKLRAYRETC STRVPSQKGA DGEEKKKKKK
RREDGEDSSG EKSPRKSGGK KSRRPSTSPR LDISTARRLH SPRAQVPSKS PCAHQQMYEE
VMISTQSSVV GDEEPQT
