1433_GIAIC
ID 1433_GIAIC Reviewed; 248 AA.
AC E2RU97;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=14-3-3 protein {ECO:0000303|PubMed:16368691, ECO:0000303|PubMed:24658679, ECO:0000303|PubMed:26551337, ECO:0000303|PubMed:28932813, ECO:0000312|EMBL:EDO79081.1};
DE AltName: Full=GI-14-3-3 {ECO:0000303|PubMed:28932813};
DE AltName: Full=g14-3-3 {ECO:0000303|PubMed:16368691, ECO:0000303|PubMed:19733174, ECO:0000303|PubMed:21135098, ECO:0000303|PubMed:22452640, ECO:0000303|PubMed:24147113, ECO:0000303|PubMed:24658679, ECO:0000303|PubMed:26551337};
GN ORFNames=GL50803_006430 {ECO:0000312|EMBL:KAE8304865.1},
GN GL50803_6430 {ECO:0000312|EMBL:EDO79081.1};
OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=184922 {ECO:0000312|EMBL:EDO79081.1};
RN [1] {ECO:0000312|EMBL:AAZ91664.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 202-219, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION, PTM,
RP PHOSPHORYLATION AT THR-214, POLYGLYCYLATION, AND MUTAGENESIS OF LYS-53 AND
RP THR-214.
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000303|PubMed:16368691,
RC ECO:0000312|EMBL:AAZ91664.1};
RX PubMed=16368691; DOI=10.1074/jbc.m509673200;
RA Lalle M., Salzano A.M., Crescenzi M., Pozio E.;
RT "The Giardia duodenalis 14-3-3 protein is post-translationally modified by
RT phosphorylation and polyglycylation of the C-terminal tail.";
RL J. Biol. Chem. 281:5137-5148(2006).
RN [2] {ECO:0000312|EMBL:EDO79081.1, ECO:0000312|EMBL:KAE8304865.1, ECO:0000312|Proteomes:UP000001548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000312|EMBL:EDO79081.1,
RC ECO:0000312|EMBL:KAE8304865.1, ECO:0000312|Proteomes:UP000001548};
RX PubMed=17901334; DOI=10.1126/science.1143837;
RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E.J., Palm D.,
RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA Svard S.G., Sogin M.L.;
RT "Genomic minimalism in the early diverging intestinal parasite Giardia
RT lamblia.";
RL Science 317:1921-1926(2007).
RN [3] {ECO:0007744|PDB:4F7R}
RP PROTEIN SEQUENCE OF 202-219, X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF THE
RP UNPHOSPHORYLATED UNPOLYGLYCYLATED FORM, SUBUNIT, DEVELOPMENTAL STAGE, PTM,
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-214,
RP POLYGLYCYLATION, MUTAGENESIS OF ARG-200; THR-208; THR-214; GLU-247 AND
RP LYS-248, AND CIRCULAR DICHROISM ANALYSIS.
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000303|PubMed:24658679};
RX PubMed=24658679; DOI=10.1371/journal.pone.0092902;
RA Fiorillo A., di Marino D., Bertuccini L., Via A., Pozio E., Camerini S.,
RA Ilari A., Lalle M.;
RT "The crystal structure of Giardia duodenalis 14-3-3 in the apo form: when
RT protein post-translational modifications make the difference.";
RL PLoS ONE 9:e92902-e92902(2014).
RN [4]
RP PROTEIN SEQUENCE OF 230-248, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP PTM, POLYGLYCYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000303|PubMed:21135098};
RX PubMed=21135098; DOI=10.1074/jbc.m110.181511;
RA Lalle M., Camerini S., Cecchetti S., Blasetti Fantauzzi C., Crescenzi M.,
RA Pozio E.;
RT "Giardia duodenalis 14-3-3 protein is polyglycylated by a tubulin tyrosine
RT ligase-like member and deglycylated by two metallocarboxypeptidases.";
RL J. Biol. Chem. 286:4471-4484(2011).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PTM, PHOSPHORYLATION
RP AT THR-214, GLYCYLATION AT GLU-246, AND MUTAGENESIS OF LYS-53; VAL-183;
RP THR-214; GLU-246 AND GLU-247.
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000303|PubMed:19733174};
RX PubMed=19733174; DOI=10.1016/j.ijpara.2009.07.010;
RA Lalle M., Bavassano C., Fratini F., Cecchetti S., Boisguerin P.,
RA Crescenzi M., Pozio E.;
RT "Involvement of 14-3-3 protein post-translational modifications in Giardia
RT duodenalis encystation.";
RL Int. J. Parasitol. 40:201-213(2010).
RN [6]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000303|PubMed:19861170};
RX PubMed=19861170; DOI=10.1016/j.parint.2009.10.005;
RA Alvarado M.E., Wasserman M.;
RT "Analysis of phosphorylated proteins and inhibition of kinase activity
RT during Giardia intestinalis excystation.";
RL Parasitol. Int. 59:54-61(2010).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=23058231; DOI=10.1016/j.exppara.2012.09.014;
RA Lingdan L., Pengtao G., Wenchao L., Jianhua L., Ju Y., Chengwu L., He L.,
RA Guocai Z., Wenzhi R., Yujiang C., Xichen Z.;
RT "Differential dissolved protein expression throughout the life cycle of
RT Giardia lamblia.";
RL Exp. Parasitol. 132:465-469(2012).
RN [8]
RP SUBUNIT, INTERACTION WITH GL50803_112076; GL50803_94117; GL50803_11043;
RP GL50803_17143; GL50803_13608; GL50803_22165; GL50803_34684 AND
RP GL50803_17472, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000303|PubMed:22452640};
RX PubMed=22452640; DOI=10.1021/pr3000199;
RA Lalle M., Camerini S., Cecchetti S., Sayadi A., Crescenzi M., Pozio E.;
RT "Interaction network of the 14-3-3 protein in the ancient protozoan
RT parasite Giardia duodenalis.";
RL J. Proteome Res. 11:2666-2683(2012).
RN [9]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT THR-214, AND
RP POLYGLYCYLATION.
RX PubMed=24147113; DOI=10.1371/journal.pone.0078090;
RA Lalle M., Leptourgidou F., Camerini S., Pozio E., Skoulakis E.M.;
RT "Interkingdom complementation reveals structural conservation and
RT functional divergence of 14-3-3 proteins.";
RL PLoS ONE 8:e78090-e78090(2013).
RN [10]
RP INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000303|PubMed:24728194};
RX PubMed=24728194; DOI=10.1128/ec.00041-14;
RA Paredez A.R., Nayeri A., Xu J.W., Krtkova J., Cande W.Z.;
RT "Identification of obscure yet conserved actin-associated proteins in
RT Giardia lamblia.";
RL Eukaryot. Cell 13:776-784(2014).
RN [11]
RP FUNCTION, SUBUNIT, INTERACTION WITH ACTIN, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000303|PubMed:28932813};
RX PubMed=28932813; DOI=10.1128/msphere.00248-17;
RA Krtkova J., Xu J., Lalle M., Steele-Ogus M., Alas G.C.M., Sept D.,
RA Paredez A.R.;
RT "14-3-3 Regulates Actin Filament Formation in the Deep-Branching Eukaryote
RT Giardia lamblia.";
RL MSphere 2:0-0(2017).
RN [12] {ECO:0007744|PDB:4ZQ0, ECO:0007744|PDB:5BY9}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF THE UNPHOSPHORYLATED
RP POLYGLYCYLATION MIMIC MUTANT AND IN COMPLEX WITH SYNTHETIC PHOSPHOPEPTIDE,
RP SUBUNIT, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000303|PubMed:26551337};
RX PubMed=26551337; DOI=10.1021/acs.jcim.5b00452;
RA Cau Y., Fiorillo A., Mori M., Ilari A., Botta M., Lalle M.;
RT "Molecular Dynamics Simulations and Structural Analysis of Giardia
RT duodenalis 14-3-3 Protein-Protein Interactions.";
RL J. Chem. Inf. Model. 55:2611-2622(2015).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner (By similarity). Binds with varying
CC affinity to various synthetic phosphopeptides having a consensus
CC binding motif RSX(pS/pT)XP, called mode-1, where X is any residue and
CC pS/pT is a phosphorylated serine/threonine, and to synthetic
CC phosphopeptides having a consensus binding motif Xp(S/T)X1-2-COOH,
CC called mode-3, in which the phosphorylated residue occupies the
CC penultimate C-terminal position in the target protein, but does not
CC bind to their unphosphorylated counterparts (PubMed:19733174). Binds to
CC synthetic human RAF1 phosphopeptides, but not to their unphosphorylated
CC forms. Binds to difopein, a polypeptide containing a phosphorylation-
CC independent binding motif (PubMed:16368691, PubMed:19733174). Involved
CC in encystation (PubMed:19733174). Involved in cell proliferation.
CC Required for actin and tubulin cytoskeletal organization. Regulates
CC actin filament formation and nuclear size (PubMed:28932813).
CC {ECO:0000250|UniProtKB:P62261, ECO:0000269|PubMed:16368691,
CC ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:28932813}.
CC -!- SUBUNIT: Homodimer (PubMed:16368691, PubMed:24658679, PubMed:28932813,
CC PubMed:26551337, PubMed:22452640). Homodimerizes via N-terminal domains
CC (PubMed:24658679, PubMed:26551337). Oligomerizes forming homotrimers,
CC homotetramers and protein filaments. Oligomerization is hindered by
CC polyglycylation in vivo (PubMed:24658679). Interacts with a large
CC number of both cytosolic and membrane proteins in trophozoites and
CC encysting parasites (PubMed:16368691, PubMed:22452640). Interacts with
CC a serine/threonine protein kinase GL50803_112076 (gCDC7). Component of
CC a multiprotein complex containing gCDC7 and GL50803_94117 (gDBF4), a
CC regulatory subunit of gCDC7, during both the trophozoite and encysting
CC stages of the parasite. Interacts with fructose-bisphosphate aldolase
CC GL50803_11043 (gFBA), pyruvate kinase GL50803_17143 (gPyk), acetyl-CoA
CC synthetase GL50803_13608 (gACS), protein kinase GL50803_22165 (gSTE),
CC DEAD box RNA helicase GL50803_34684 (gVASA) and Golgi/cell cycle
CC associated protein GL50803_17472 (gGCCA) (PubMed:22452640). Interacts
CC with actin (PubMed:24728194, PubMed:28932813). Interacts with both
CC monomeric phosphorylated and unphosphorylated actin. The interaction is
CC enhanced by phosphorylation of actin and inhibited by Rho GTPase Rac
CC (PubMed:28932813). {ECO:0000269|PubMed:16368691,
CC ECO:0000269|PubMed:22452640, ECO:0000269|PubMed:24658679,
CC ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:26551337,
CC ECO:0000269|PubMed:28932813}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16368691,
CC ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:19861170,
CC ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:24147113,
CC ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:28932813}. Nucleus
CC {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174,
CC ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:22452640}. Cell
CC projection, cilium, flagellum {ECO:0000269|PubMed:28932813}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:28932813}. Nucleus envelope
CC {ECO:0000269|PubMed:28932813}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:28932813}. Note=In trophozoites and cysts,
CC localizes intensely in the cytoplasm. Not detected in the central area
CC of the cell corresponding to the median body nor in flagella. Detected
CC in the nuclei of the encysting cells. Nuclear localization increases
CC during the transition of cells from the early to the late encysting
CC stage. Does not localize to the encystation-specific vesicles of the
CC encysting cells (PubMed:16368691, PubMed:19733174). In interphase
CC cells, detected throughout the cell with somewhat enriched at the
CC cortex and perinuclear region. Associates with the intracytoplasmic
CC axonemes of all flagella, but it is most apparent in the anterior
CC flagella of interphase cells. Localizes also to the nuclear
CC envelope/endoplasmic reticulum and to the microtubule bare area of the
CC ventral disc during interphase. In mitotic cells, disassociates from
CC the intracytoplasmic axonemes and localizes around the spindle. During
CC cytokinesis, localizes with the ingressing furrow, which does not
CC utilize a contractile ring (PubMed:28932813). Does no colocalize with
CC F-actin (PubMed:24728194, PubMed:28932813).
CC {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174,
CC ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}.
CC -!- DEVELOPMENTAL STAGE: Expressed during excystation, the differentiation
CC from cyst to trophozoite (at protein level) (PubMed:19861170).
CC Expressed in trophozoites (at protein level) (PubMed:24658679,
CC PubMed:19733174, PubMed:24147113, PubMed:24728194, PubMed:28932813,
CC PubMed:22452640, PubMed:23058231, PubMed:21135098). Highly expressed
CC during encystation stage, the differentiation from trophozoite to cyst
CC (at protein level) (PubMed:24658679, PubMed:19733174, PubMed:24147113,
CC PubMed:22452640). Expressed in feces extracted cysts (at protein level)
CC (PubMed:19861170, PubMed:23058231). Expression in them is significantly
CC lower than in trophozoites (at protein level) (PubMed:23058231).
CC Constitutively expressed throughout the life cycle (PubMed:16368691).
CC {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174,
CC ECO:0000269|PubMed:19861170, ECO:0000269|PubMed:21135098,
CC ECO:0000269|PubMed:22452640, ECO:0000269|PubMed:23058231,
CC ECO:0000269|PubMed:24147113, ECO:0000269|PubMed:24658679,
CC ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}.
CC -!- INDUCTION: By encystation. {ECO:0000269|PubMed:16368691}.
CC -!- PTM: Phosphorylated constitutively throughout the life cycle.
CC Phosphorylation is very high in trophozoites and encysting cells of 12
CC hours (PubMed:16368691). Phosphorylated during excystation
CC (PubMed:19861170). Phosphorylation promotes its binding to various
CC target proteins and is critical for encystation process.
CC Phosphorylation modification is not influenced by polyglycylation
CC modification (PubMed:19733174). {ECO:0000269|PubMed:16368691,
CC ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:19861170}.
CC -!- PTM: Polyglycylated on a glutamate residue, resulting in polyglycine
CC chain on the gamma-carboxyl group (PubMed:16368691, PubMed:24658679,
CC PubMed:19733174, PubMed:24147113, PubMed:21135098). Polyglycylated by
CC the tubulin--tyrosine ligase-like protein GL50803_8456 (gTTLL3). The
CC polyglycine chain is shortened by metallopeptidases of the M20 family,
CC namely dipeptidases GL50803_15832 (gDIP1) and GL50803_8407 (gDIP2)
CC (PubMed:21135098). The length of the polyglycine chain is developmental
CC stage-dependent. In trophozoites, glycine residues range from 10 to 31,
CC with the greatest occurrence of 21 residues. In 12 hour encystation
CC stage, glycine residues range from 6 to 22, with the greatest
CC occurrence of 10 residues. The differential rate of
CC polyglycylation/deglycylation during the encystation process regulates
CC the intracellular localization of this protein. Relocalizes partially
CC from the cytoplasm inside the nuclei following the shortening of the
CC polyglycine chain in encysting cells (PubMed:16368691,
CC PubMed:19733174). Polyglycylation modification is not influenced by
CC phosphorylation modification (PubMed:19733174). Polyglycylation
CC prevents oligomerization in vivo (PubMed:24658679).
CC {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174,
CC ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:24147113,
CC ECO:0000269|PubMed:24658679}.
CC -!- DISRUPTION PHENOTYPE: Knockdown with morpholino results in dramatically
CC reduced parasite growth, accumulation of multinucleate cells, abnormal
CC flagellar positioning, and polarity and cytokinesis defects. Overall
CC cytoplasmic actin organization is disrupted with ectopic short actin
CC filaments, however, nuclei are enlarged with actin filaments covering
CC the width of the nuclei. {ECO:0000269|PubMed:28932813}.
CC -!- BIOTECHNOLOGY: This protein may be used to design small molecules that
CC inhibit its interactions with the target proteins. The inhibitors could
CC be used as drugs to treat giardiasis, a disease caused by this
CC parasite. {ECO:0000305|PubMed:26551337}.
CC -!- MISCELLANEOUS: Despite sequential and structural similarity, is not a
CC functional ortholog of Drosophila 14-3-3 protein epsilon.
CC {ECO:0000269|PubMed:24147113}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; DQ146480; AAZ91664.1; -; Genomic_DNA.
DR EMBL; AACB02000020; EDO79081.1; -; Genomic_DNA.
DR EMBL; AACB03000001; KAE8304865.1; -; Genomic_DNA.
DR RefSeq; XP_001706755.1; XM_001706703.1.
DR PDB; 4F7R; X-ray; 3.20 A; A/B/C/D=1-248.
DR PDB; 4ZQ0; X-ray; 3.10 A; A/B/C/D=5-238.
DR PDB; 5BY9; X-ray; 4.00 A; A/B/C/D=1-246.
DR PDBsum; 4F7R; -.
DR PDBsum; 4ZQ0; -.
DR PDBsum; 5BY9; -.
DR SMR; E2RU97; -.
DR STRING; 184922.E2RU97; -.
DR EnsemblProtists; EDO79081; EDO79081; GL50803_6430.
DR GeneID; 5699649; -.
DR KEGG; gla:GL50803_006430; -.
DR VEuPathDB; GiardiaDB:GL50803_6430; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; E2RU97; -.
DR OMA; IPCATTG; -.
DR OrthoDB; 1176818at2759; -.
DR Proteomes; UP000001548; Chromosome 5.
DR Proteomes; UP000001548; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051219; F:phosphoprotein binding; IDA:UniProtKB.
DR GO; GO:0050815; F:phosphoserine residue binding; IDA:UniProtKB.
DR GO; GO:1990051; P:activation of protein kinase C activity; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Endoplasmic reticulum; Flagellum;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..248
FT /note="14-3-3 protein"
FT /id="PRO_0000455962"
FT COILED 13..33
FT /evidence="ECO:0000255"
FT COILED 91..111
FT /evidence="ECO:0000255"
FT MOTIF 237..248
FT /note="Putative polyglycylation target motif (T/G)X0-
FT 1(D/E)X1-3-G(D/E)X1-2(gE)2-4, where X is polar or
FT negatively charged amino acid, and gE is polyglycylated
FT glutamine"
FT /evidence="ECO:0000269|PubMed:16368691"
FT BINDING 135..136
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000269|PubMed:26551337,
FT ECO:0007744|PDB:4ZQ0"
FT SITE 53
FT /note="Interaction with phosphoserine"
FT /evidence="ECO:0000269|PubMed:26551337,
FT ECO:0007744|PDB:4ZQ0"
FT SITE 60
FT /note="Interaction with phosphoserine"
FT /evidence="ECO:0000269|PubMed:26551337,
FT ECO:0007744|PDB:4ZQ0"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16368691,
FT ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:24147113,
FT ECO:0000269|PubMed:24658679"
FT MOD_RES 246
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000269|PubMed:19733174"
FT MUTAGEN 53
FT /note="K->E: Loss or strongly decreased binding to
FT synthetic human RAF1 phosphopeptides. Loss of binding to
FT difopein."
FT /evidence="ECO:0000269|PubMed:16368691,
FT ECO:0000269|PubMed:19733174"
FT MUTAGEN 183
FT /note="V->D: Loss of binding to difopein."
FT /evidence="ECO:0000269|PubMed:19733174"
FT MUTAGEN 200
FT /note="R->K: Increased oligomerization."
FT /evidence="ECO:0000269|PubMed:24658679"
FT MUTAGEN 208
FT /note="T->A: Slightly decreased oligomerization."
FT /evidence="ECO:0000269|PubMed:24658679"
FT MUTAGEN 214
FT /note="T->A: Loss of phosphorylation by a protein kinase.
FT No effect on subcellular localization. Dramatic decrease in
FT the number of encysting parasites and cysts, but a large
FT increase in the number of trophozoites. In encysting cells
FT of 12 hours, significantly slower cyst conversion rate
FT compared to the wild-type. No effect on binding to
FT difopein. Decreased binding to a number of synthetic
FT phosphopeptides."
FT /evidence="ECO:0000269|PubMed:16368691,
FT ECO:0000269|PubMed:19733174"
FT MUTAGEN 214
FT /note="T->E: Phosphomimetic mutant. No effect on
FT oligomerization. No effect on binding to difopein. Altered
FT binding intensity or capability to various synthetic
FT phosphopeptides."
FT /evidence="ECO:0000269|PubMed:19733174,
FT ECO:0000269|PubMed:24658679"
FT MUTAGEN 246
FT /note="E->A: Loss of polyglycylation. In trophozoites,
FT encysting cells and cysts, localizes to the nuclei in
FT addition to the cytoplasm. Increased encystation and
FT increased number of cysts. In encysting cells of 12 hours,
FT significantly faster cyst conversion rate compared to the
FT wild-type."
FT /evidence="ECO:0000269|PubMed:19733174"
FT MUTAGEN 247
FT /note="E->A: No effect on polyglycylation."
FT /evidence="ECO:0000269|PubMed:19733174"
FT MUTAGEN 247
FT /note="Missing: Prevention of oligomerization and filament
FT formation by the polyglycylation of E-246; when associated
FT with K-248 del."
FT /evidence="ECO:0000269|PubMed:24658679"
FT MUTAGEN 248
FT /note="Missing: Prevention of oligomerization and filament
FT formation by the polyglycylation of E-246; when associated
FT with E-247 del."
FT /evidence="ECO:0000269|PubMed:24658679"
SQ SEQUENCE 248 AA; 28576 MW; 83E4D80EDED75B14 CRC64;
MAEAFTREDY VFMAQLNENA ERYDEMVETM RKISGMEGEL SDKERNLLSV AYKNVIGPRR
AAWRIVSSIE AKEKGRQKPN AKRIEQIRVY RQKIEKELSD ICNDILKLLQ EQFVPRSTNA
DAKVFYYKMQ GDYYRYLAEY SSGEDKEKIA GSALNAYNSA FEISQQLPPT HPIRLGLALN
FSVFYYEILA SPDRACELAR KAFDAAITDL DKLTEESYKD STLIMQLLRD NLNLWVTDSA
GDDNAEEK
