UGO_TOXGG
ID UGO_TOXGG Reviewed; 2122 AA.
AC S7UQV8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Unique GC organizer UGO {ECO:0000303|PubMed:30742070};
GN Name=UGO {ECO:0000303|PubMed:30742070};
GN ORFNames=TGGT1_238390 {ECO:0000312|EMBL:EPR60366.1};
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 GC, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30742070; DOI=10.1038/s41564-018-0339-8;
RA Bisio H., Lunghi M., Brochet M., Soldati-Favre D.;
RT "Phosphatidic acid governs natural egress in Toxoplasma gondii via a
RT guanylate cyclase receptor platform.";
RL Nat. Microbiol. 4:420-428(2019).
CC -!- FUNCTION: In tachyzoites, required for the cellular trafficking of
CC guanylate cyclase GC to the cell membrane and for GC guanylate cyclase
CC activity. {ECO:0000269|PubMed:30742070}.
CC -!- SUBUNIT: Interacts with guanylate cyclase GC; the interaction regulates
CC guanylate cyclase GC trafficking and catalytic activity.
CC {ECO:0000269|PubMed:30742070}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30742070};
CC Multi-pass membrane protein {ECO:0000255}. Note=In intracellular
CC tachyzoites, localizes to the apical cap, to the cytoplasm in disperse
CC foci and to the residual body. {ECO:0000269|PubMed:30742070}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in tachyzoites severely
CC impairs lytic parasite growth in host cells (PubMed:30742070).
CC Guanylate cyclase GC is unstable and remains trapped along the
CC secretory pathway (PubMed:30742070). Tachyzoite natural and induced
CC egress, motility and invasion are impaired (PubMed:30742070). Loss of
CC microneme secretion in response to phosphatidic acid or a decrease in
CC vacuolar pH (PubMed:30742070). {ECO:0000269|PubMed:30742070}.
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DR EMBL; AAQM03000188; EPR60366.1; -; Genomic_DNA.
DR AlphaFoldDB; S7UQV8; -.
DR EnsemblProtists; EPR60366; EPR60366; TGGT1_238390.
DR VEuPathDB; ToxoDB:TGGT1_238390; -.
DR Proteomes; UP000005641; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..2122
FT /note="Unique GC organizer UGO"
FT /id="PRO_0000452810"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1859..1879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1956..1976
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1989..2009
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2017..2037
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2040..2060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 337..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1515..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1639..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2102..2122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1275
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 2122 AA; 231880 MW; 54B56BC7552DDEDC CRC64;
MRMQWFLLRH AYFIKGEDFA VAVALLDLAL YVLIGTNSLQ FLDQSPEKAL FGMITSALIF
IIALCGFVIV RMFRTSKYKI ETYIMPVLII CNIASVFYMQ LINKLVGFMT LQLPVLTFLI
TGYPYVWLVA FVLIGMGGGL IAQSVVCSVS LGSSCPPSVW VDVGLYALQL ISGSVAYFTV
YELGILIVRY KRHPARYLDA FSDLTALDTI VFSPVFGLGG ETARQVQVNQ LMAPEKPNLD
GLTFLRSASQ VSQTTNRIVS RAFYHANTPP HSSSRDALPA DKALGAERSD RAGSAVFSPN
TLGPLGAPSA GLRDFGPGRP VPGASVVVPK SLKQHAAALH AGANSPHGSP PLQPHGALPG
APRSNTLRGC SGQVSLVPRE EESDPACGSL RASVESKATH RSAATLSACE SKSRSGRVAG
LFRGLSKRPG GPDCEEAAPA EPATSLGSKE LGRKKTAGSK AQSSVPILLP RPQSIEETTW
RGLASGDLSK DTPVASLASR RNLRMDEQSG DADKASSDVS RDPAKKGAGP FVAEAPVHTA
VLPSSSFHSE FPLSRRDSGK ELLSDLRESR ERTARAASHD THAAADDSGL QGDPALAAEA
RVRTALHYHR RWFFSQLFHF RRARRRHRRG AGARDGELVF ERGEPDEVES EESCDDSRSR
PRETASLSHF SRLSRSRRHK TRTYRRGRSS DGTTAGTSDS DSHGESLEDE GSDSGQESES
EESRRRRMRS SRNRRRETSS EDSSSGTSVR SEGRHCREGR ANSSVFSSGI RRYFSFFSAA
TRCAHAASSE EERPVRPARH SWRRGSGDSR ECSASTSGVS EACEHSSDAS WASSSSLCGS
CEKRSIRMSR RRRREGKSRP HASSVSRAER HRGHVSVDLA PLLPSRLFFD TFLNSVRRAE
RLSKEGRLPA SVSRQSSETR GSRTAFLNGD KGCSPTSEAP ERSFPASANE VSFRRNEGWE
RYYDMLLPSL PPFPSARPLY VKPRKNSQAF QNVAVSVSRN ETEMTASSPA TSFDGPRAVS
LSPEGRGARE SSDGGGATAP SDLHSRPARA KSLVAAMLHT YPTCPQPPSD LSLFTTPPAS
PSSLNEVQAS RSSSARITSV ELGALGKQQG EAAPAGTDAV EEDRDATEDA RGSLSSPTGA
SRRGDRCRRS WSSCEARSSV EMKPNLSIRD ARASESPLQS AAPLLSEEKK SRKAQSCAQC
RRCGRSRTRL QPSGRLGSSS REDLVGEADS HVSPEKEVFV SSRREKREEQ VPRSRREERR
DRRGRRWRRG RRRRKARECS ETEERRDSSS EWSGTQYSSQ ERRSHEAVGG VAQLTPICVD
DECGKGDAGL SPLLRSEAEE SEGEGDMRER QIYETHSDGD VEELSEEERE DRGRSWLRWL
FPWGAGEGQG GEKNRRKRSR SEGRREREFI SAERRYLEHH RRSRVSSVAD SRWGSGSEAS
ADAYPALRRR KGSRVYPVSK PQWFQPSGLT ACSSKNSWLA VPPDISLVSA APALPTPSPS
SLSFSGLDQE LDCDANSSTA VSSSLPDSTA WQGSGAAASA SSPSLRASVD AHFAEAELHA
AEHSDGVSVS PRNSPGALSA RPMSAAGMPN PDSGIATQTP QTPQTPHTQR PLLLAQSLVA
ASGKPLPPTR ADFEAQRSQG LGDLSQKTPR VFSPQGLGRS QGYGPGGSSY ALDSSREAGP
SGRLSATPST RLQGSGGPAF PHSSFPQAIG AAGTPTAPSR DSRTFFGDTG AARASRAGLS
GRLASRGTAL APKGTRRLKS GYSVGAADAK DKQKGKVLRY QLVQKFHDRL PWWVARIIVY
TDAALENCRR RRRLMQRATW KTKVAMPVRN MLGLFSDEKI ETWYVQWLNA FNAKYYPRVA
WLLFLICFYA TAFHGLLRLR GFIENYPLCI DAVRASPLGE AGFLILVAVR FASQPILSFL
LLLPLLRHSG SRLIDFLFCS RAPATPLKSY KLYRWMLALS FLQFVYAVFD NTWHLIAEPG
SRHVNPLTII PASPSLEIAA VQTVYILAVR TPTINLIFLL YIITYIIIFF VALPPGVQQV
QLFTISMAGW LFTCVGGQLF YTRAFEVNRR RLFCKYVLPY MLYLEEIAAI LYSNPQGEYP
LDEGSEDEVS MGSGHLVGDR SA
