RON2_TOXGM
ID RON2_TOXGM Reviewed; 1479 AA.
AC B6KV60; F6KDI4; Q45WA8; S8EWN0;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Rhoptry neck protein 2;
DE AltName: Full=145 kDa AMA1-associated protein;
DE Short=AAP145;
DE Flags: Precursor;
GN Name=RON2; ORFNames=TGME49_100100, TGME49_300100;
OS Toxoplasma gondii (strain ATCC 50611 / Me49).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=508771;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=RH;
RX PubMed=16002398; DOI=10.1074/jbc.m504158200;
RA Bradley P.J., Ward C., Cheng S.J., Alexander D.L., Coller S., Coombs G.H.,
RA Dunn J.D., Ferguson D.J., Sanderson S.J., Wastling J.M., Boothroyd J.C.;
RT "Proteomic analysis of rhoptry organelles reveals many novel constituents
RT for host-parasite interactions in Toxoplasma gondii.";
RL J. Biol. Chem. 280:34245-34258(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH AMA1,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=RH;
RX PubMed=21347343; DOI=10.1371/journal.ppat.1001276;
RA Lamarque M., Besteiro S., Papoin J., Roques M., Vulliez-Le Normand B.,
RA Morlon-Guyot J., Dubremetz J.F., Fauquenoy S., Tomavo S., Faber B.W.,
RA Kocken C.H., Thomas A.W., Boulanger M.J., Bentley G.A., Lebrun M.;
RT "The RON2-AMA1 interaction is a critical step in moving junction-dependent
RT invasion by apicomplexan parasites.";
RL PLoS Pathog. 7:E1001276-E1001276(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50611 / Me49;
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16309467; DOI=10.1111/j.1462-5822.2005.00646.x;
RA Lebrun M., Michelin A., El Hajj H., Poncet J., Bradley P.J., Vial H.,
RA Dubremetz J.F.;
RT "The rhoptry neck protein RON4 re-localizes at the moving junction during
RT Toxoplasma gondii invasion.";
RL Cell. Microbiol. 7:1823-1833(2005).
RN [5]
RP FUNCTION, INTERACTION WITH AMA1, AND SUBCELLULAR LOCATION.
RX PubMed=16244709; DOI=10.1371/journal.ppat.0010017;
RA Alexander D.L., Mital J., Ward G.E., Bradley P., Boothroyd J.C.;
RT "Identification of the moving junction complex of Toxoplasma gondii: a
RT collaboration between distinct secretory organelles.";
RL PLoS Pathog. 1:E17-E17(2005).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE MJ COMPLEX, INTERACTION WITH AMA1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19247437; DOI=10.1371/journal.ppat.1000309;
RA Besteiro S., Michelin A., Poncet J., Dubremetz J.F., Lebrun M.;
RT "Export of a Toxoplasma gondii rhoptry neck protein complex at the host
RT cell membrane to form the moving junction during invasion.";
RL PLoS Pathog. 5:E1000309-E1000309(2009).
RN [7]
RP FUNCTION, INTERACTION WITH AMA1, AND TOPOLOGY.
RX PubMed=21347354; DOI=10.1371/journal.ppat.1001282;
RA Tyler J.S., Boothroyd J.C.;
RT "The C-terminus of Toxoplasma RON2 provides the crucial link between AMA1
RT and the host-associated invasion complex.";
RL PLoS Pathog. 7:E1001282-E1001282(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1297-1333 IN COMPLEX WITH AMA1,
RP DISULFIDE BOND, AND MUTAGENESIS OF ASP-1297; ASP-1304; PRO-1309; CYS-1313;
RP LEU-1319 AND CYS-1323.
RX PubMed=21778402; DOI=10.1126/science.1204988;
RA Tonkin M.L., Roques M., Lamarque M.H., Pugniere M., Douguet D.,
RA Crawford J., Lebrun M., Boulanger M.J.;
RT "Host cell invasion by apicomplexan parasites: insights from the co-
RT structure of AMA1 with a RON2 peptide.";
RL Science 333:463-467(2011).
CC -!- FUNCTION: Essential rhoptry neck protein that plays an important role
CC in host cell invasion. Upon host invasion by tachyzoites, the protein
CC is injected into the host cell where it functions as a receptor for
CC apical membrane antigen 1 (AMA1) on the parasite. Part of the moving
CC junction (MJ) complex, a ringlike structure formed between the plasma
CC membranes of the apical tip of the parasite and the target host cell.
CC During invasion, the MJ migrates from the anterior to the posterior of
CC the parasite, leading to internalization of the parasite into a
CC parasitophorous vacuole (PV). {ECO:0000269|PubMed:16244709,
CC ECO:0000269|PubMed:19247437, ECO:0000269|PubMed:21347343,
CC ECO:0000269|PubMed:21347354}.
CC -!- SUBUNIT: Component of the moving junction (MJ) complex, composed of
CC AMA1, a transmembrane protein on the parasite surface, and a complex of
CC the rhoptry neck proteins RON2, RON4, RON5 and RON8 localized to the
CC cytoplasmic face of the host plasma membrane. Interacts (via C-
CC terminus) with AMA1 (via ectodomain); RON2 serves as the receptor for
CC AMA1 on the host plasma membrane. AMA1 and the RON proteins are
CC initially in distinct compartments within the parasite, namely the
CC micronemes and the rhoptries, and interaction happens only upon
CC initiation of invasion when the micronemes and rhoptries discharge.
CC {ECO:0000269|PubMed:16244709, ECO:0000269|PubMed:19247437,
CC ECO:0000269|PubMed:21347343, ECO:0000269|PubMed:21347354,
CC ECO:0000269|PubMed:21778402}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21347343}. Cytoplasm
CC {ECO:0000269|PubMed:21347343}. Host cell membrane
CC {ECO:0000269|PubMed:16244709, ECO:0000269|PubMed:19247437,
CC ECO:0000269|PubMed:21347343}; Single-pass type I membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:21347343}.
CC Note=Initially localizes to rhoptries, specialized secretory organelles
CC of apicomplexan parasites important for host cell invasion
CC (PubMed:16002398,PubMed:16244709). Upon host invasion by tachyzoites,
CC the protein is injected into the host cell, where it spans the host
CC cell membrane (PubMed:21347343). {ECO:0000269|PubMed:16002398,
CC ECO:0000269|PubMed:16244709, ECO:0000269|PubMed:21347343}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B6KV60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B6KV60-2; Sequence=VSP_046510, VSP_046511;
CC -!- SIMILARITY: Belongs to the apicomplexan parasites RON2 family.
CC {ECO:0000305}.
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DR EMBL; DQ096563; AAZ38163.1; -; mRNA.
DR EMBL; HQ110093; ADN06068.1; -; mRNA.
DR EMBL; KE138839; EPT25468.1; -; Genomic_DNA.
DR RefSeq; XP_018635197.1; XM_018782383.1. [B6KV60-1]
DR PDB; 2Y8S; X-ray; 2.55 A; B/E=1297-1333.
DR PDB; 2Y8T; X-ray; 1.95 A; B/E=1297-1332.
DR PDBsum; 2Y8S; -.
DR PDBsum; 2Y8T; -.
DR AlphaFoldDB; B6KV60; -.
DR SMR; B6KV60; -.
DR EnsemblProtists; TGME49_300100-t26_1; TGME49_300100-t26_1; TGME49_300100. [B6KV60-1]
DR GeneID; 7895166; -.
DR KEGG; tgo:TGME49_300100; -.
DR VEuPathDB; ToxoDB:TGME49_300100; -.
DR HOGENOM; CLU_254159_0_0_1; -.
DR PhylomeDB; B6KV60; -.
DR Proteomes; UP000001529; Chromosome XII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disulfide bond;
KW Host cell membrane; Host membrane; Membrane; Secreted; Signal; Tachyzoite;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1479
FT /note="Rhoptry neck protein 2"
FT /id="PRO_0000422339"
FT TOPO_DOM 25..1277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1278..1298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1299..1479
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 49..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1333
FT /note="Interaction with AMA1"
FT REGION 1419..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1313..1323
FT /evidence="ECO:0000269|PubMed:21778402"
FT VAR_SEQ 246..276
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16002398"
FT /id="VSP_046510"
FT VAR_SEQ 406..504
FT /note="TIGHVLTLMIAYLDYESFFGASPSKPFHSWVSLAASAGNNTGFAMLDEMCDN
FT HRGPKRRGQKHWYQTGGARKHKNRDMLPLHRQLCDALELVLNGVQQI -> SKEVAAWL
FT TSNDARLGCGNRSEYPIDLRVSAV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16002398"
FT /id="VSP_046511"
FT MUTAGEN 1297
FT /note="D->A: Impairs interaction with AMA1."
FT /evidence="ECO:0000269|PubMed:21778402"
FT MUTAGEN 1304
FT /note="D->A: Impairs interaction with AMA1."
FT /evidence="ECO:0000269|PubMed:21778402"
FT MUTAGEN 1309
FT /note="P->A: Impairs interaction with AMA1."
FT /evidence="ECO:0000269|PubMed:21778402"
FT MUTAGEN 1313
FT /note="C->A: Impairs interaction with AMA1 and inhibits
FT host cell invasion."
FT /evidence="ECO:0000269|PubMed:21778402"
FT MUTAGEN 1319
FT /note="L->A: Impairs interaction with AMA1."
FT /evidence="ECO:0000269|PubMed:21778402"
FT MUTAGEN 1323
FT /note="C->A: Impairs interaction with AMA1 and inhibits
FT host cell invasion."
FT /evidence="ECO:0000269|PubMed:21778402"
FT HELIX 1298..1304
FT /evidence="ECO:0007829|PDB:2Y8T"
FT STRAND 1312..1316
FT /evidence="ECO:0007829|PDB:2Y8T"
FT TURN 1317..1319
FT /evidence="ECO:0007829|PDB:2Y8T"
FT STRAND 1320..1323
FT /evidence="ECO:0007829|PDB:2Y8T"
FT TURN 1330..1332
FT /evidence="ECO:0007829|PDB:2Y8T"
SQ SEQUENCE 1479 AA; 166464 MW; D916320FBF56793A CRC64;
MTKRAGLPLG RAFLVLILLS AADSLFFSSF PRSALQLFSS VLFTDAAEPD SDATPGLRPQ
PSPRTFRPTG YQRIEVKTVD EELPEDLKVY TASTRGSSSR TFEVRNAGGR QEGFTLSVLT
AGGPLPHGSW SWSGTPPEVQ TTGGSQISFG WVPDTETPSL PERNLLQLKR MLRDEGLIEA
VQLRAAEKGC PVAVLHNLRQ LPVNFREVLH EEYESRSNPA KMYEVANSYV QQRGSDAARW
SVSQSVELSL LEMHATSTTD PRGSSAVPSF LETGPQVRVA MTDAVPSGIR VYATPPAPRP
VPVQSNQTEK ERSPTSKRLV GMQLGLYLIC KLAALFGHPT LFLNPYYTEQ QLLEAVAQAL
GIAPPHRGDF ENEGNEAQAT ANQHNGSADQ LLAAIEIFRL GPNPYTIGHV LTLMIAYLDY
ESFFGASPSK PFHSWVSLAA SAGNNTGFAM LDEMCDNHRG PKRRGQKHWY QTGGARKHKN
RDMLPLHRQL CDALELVLNG VQQIQIDLMD ELGKYKTGVE PLVDPATNSA RIHTRTCRGL
SPVCDYEATI LAPVRALEPH EQQDSLRTKK AFNLVTGYGS GHVGQITGSI AEPFSHSWRT
RWGKVVADPT AYGEIFERTL WFDDRELMAK SSGALFRQYD RIAKDSMSFG VFMNVENGLL
KKDMRSKLEA YISQRKSFVE KRQQSRFAKL RKKIPENDPY ALRAAIFLAL NSRTFCAQPT
SFLSSFRTFL TNQYHKLSQG RNLPRSQRSL MAFMRTGQVK FFQEWCSFDP LAVNALFLFR
FAVSGTDPAA LHDRQHTRVS RNKKTMRILN SKWTPAVLKK LMRKVNHKHM AREAKALLLR
SLDPTVLSSI VTAFDFITHT QANLEVNQNA FMYHEVRARE VSRQSAAEKG SHRLHERGLV
RETDDMIKRW AEHGIPGDIK RRLARGEKLP EGMSFGGIPI PNLTNWDAQL NSKWLEAYNA
YLRHPYGRAA LNARDPVALL VKDSRDRLQA EAEGTIFLGR IAKRVHQSKN LLRRAGRALK
TFFLSLLREN ERSEYAVWFG VKVDMRQVIQ TCRQINSVAE VVKNDRLYDF ITDGWMELVK
DVVAGYTKAS VRVPGFDTIS AANEQLRKEG VAAATARNQG FLSIHYDYAN LPEEERKKEF
QRSMCMEQCE ALWKLVMAFV MPNLQNPKKL KGYEKDFSGA KEIEKLNSPH HVNAFRFSLS
VQIDFFDNML DKTSKKNLKA MKFGASTWFT YAMKLAGQVN SEMGNPNLGT ALYMQAAYYG
NYIRKWMEQR RKSRKQAIIG VLTLGMMGLY ALLNVADIVQ HMEDIGGAPP VSCVTNEILG
VTCAPQAIAK ATTSAARVAT QDFLKVGLFA GMAPYLMLPM AVVSVWNILK SEIKVLLQFE
MALKHTFTRL KRWLAAPFKN WWAKRGRLKD ALFRRASQTY RKTEQETKQP PRPRNLHNPS
SWGDTELDSL GVPPEPFVQD FEIKYTTPVF PMSAPLIKA
