ID   CDC50_TOXGG             Reviewed;         524 AA.
AC   S7WII9;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=CDC50-related protein CDC50.1 {ECO:0000303|PubMed:30742070};
GN   Name=CDC50.1 {ECO:0000303|PubMed:30742070};
GN   ORFNames=TGGT1_230820 {ECO:0000312|EMBL:EPR64123.1};
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 and UGO to the cell membrane (PubMed:30742070).
CC       May play a role in the folding of the GC P-type ATPase-like domain to
CC       sense vacuolar changes in phosphatidic acid and pH levels which trigger
CC       parasite egress (PubMed:30742070). {ECO:0000269|PubMed:30742070}.
CC   -!- SUBUNIT: Interacts with GC; the interaction regulates guanylate cyclase
CC       GC trafficking and sensing environmental changes.
CC       {ECO:0000269|PubMed:30742070}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:30742070}; Multi-
CC       pass membrane protein {ECO:0000255}. Note=In intracellular tachyzoites,
CC       localizes to the apical cap, to the cytoplasm in disperse foci and to
CC       the residual body. {ECO:0000269|PubMed:30742070}.
CC   -!- DISRUPTION PHENOTYPE: Conditional knockout in tachyzoites severely
CC       impairs lytic parasite growth in host cells without affecting
CC       intracellular replication (PubMed:30742070). Loss of egress from host
CC       cells; however, tachyzoite motility and host cell invasion are normal
CC       (PubMed:30742070). Guanylate cyclase GC is unstable and, together with
CC       UGO, remains trapped along the secretory pathway (PubMed:30742070).
CC       Loss of microneme secretion in response to phosphatidic acid or a
CC       decrease in vacuolar pH (PubMed:30742070).
CC       {ECO:0000269|PubMed:30742070}.
CC   -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR   EMBL; AAQM03000026; EPR64123.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7WII9; -.
DR   EnsemblProtists; EPR64123; EPR64123; TGGT1_230820.
DR   VEuPathDB; ToxoDB:TGGT1_230820; -.
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:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR   InterPro; IPR005045; CDC50/LEM3_fam.
DR   PANTHER; PTHR10926; PTHR10926; 1.
DR   Pfam; PF03381; CDC50; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..524
FT                   /note="CDC50-related protein CDC50.1"
FT                   /id="PRO_0000452809"
FT   TOPO_DOM        1..181
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        203..473
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        474..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        495..524
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   524 AA;  58191 MW;  78C0A8FC5E446979 CRC64;
     MGENSTTGLR GQADVSQFSD AAVEPTLSSP PTGQRQQSLP LFGEETCSIS SAPSVGGGGG
     WPFQRQGSSR LTSRGTSLSS CSDAGSGLGA LRQREDSFPE YHGVGLPLGG KYALDGTGLV
     LAPRVPFIFS HQLPSLTGLD EAGFSDTRKV PSTYQALAAR FVHQVHQEAG NGMYPLWSAG
     VVLRLCLLGA LFFVSVGAWL IFEDEQHVEC KLNYAEKTLQ EGSSRYLLKG ISSAHCTREV
     NELKGEEISV YAEMGHFFQN DAQVLWSRND RQLAGKIFTD PKDVRECEPL ATAVVGNVTK
     VLHPCGALAW AVFTDKYQFL EGTPEGDNDQ VPMKPIPLNQ TQAVLLHSWP WQDMYKNPPA
     EDRAAVLDKV YFWMSPVDND DGEDMYKTRE EARAELLMDR LNYEEAGEMV ENGHFIQWMQ
     TAALGTFRKL YGSLEGPLKL PVSAHITVMY DVSSWKGKKA IVLVQKSRLG GRSLFIGIAY
     LSFGCLLTML VFYMLWKKWQ YRREGEEIRD LRWQTKTRGS KKTK