{"gene":"PF3D7_0414900","run_date":"2026-09-07T10:55:51","timeline":{"discoveries":[{"year":2012,"finding":"ARO (PF3D7_0414900) localizes to the cytosolic face of P. falciparum rhoptry membranes, and the first 20 N-terminal amino acids are sufficient for rhoptry membrane targeting. Both myristoylation and palmitoylation motifs are required for membrane attachment, but are not sufficient alone; positively charged residues R9 and K14 within the first 20 amino acids are additionally required. Substitution of R9 with a negative charge entirely abolishes membrane attachment, while substitution of K14 (and K16) alters membrane specificity without abolishing attachment.","method":"GFP fusion protein localization, mutational analysis of N-terminal residues, lipid modification (myristoylation/palmitoylation) motif dissection in P. falciparum","journal":"Traffic (Copenhagen, Denmark)","confidence":"High","confidence_rationale":"Tier 2 / Strong — systematic mutagenesis with direct localization readout, multiple orthogonal point mutations tested, replicated across residues in a single rigorous study","pmids":["22759070"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2016,"finding":"P. falciparum ARO (PF3D7_0414900) functionally complements ARO depletion in Toxoplasma gondii and interacts with the same partners (AIP and ACβ), demonstrating conservation of rhoptry biogenesis machinery. Each armadillo (ARM) repeat of ARO contributes to its multifunctional role in rhoptry positioning and clustering.","method":"Complementation assay in T. gondii with P. falciparum ARO, co-immunoprecipitation of interacting partners, deletion of individual ARM repeats","journal":"Journal of cell science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — complementation and Co-IP in a single study; P. falciparum ARO interactions inferred from T. gondii complementation context","pmids":["26769898"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"finding":"The crystal structure of P. falciparum ARO (PfARO) was solved, revealing five tandem Armadillo-like (ARM) repeats arranged in a head-to-tail orientation giving an elongated curved shape. The concave face contains two distinct patches of highly conserved residues important for protein-protein interaction. Structure-guided mutagenesis identified specific PfARO mutations that cause mislocalization of PfAIP, confirming a direct ARO–AIP interaction required for PfAIP rhoptry localization.","method":"X-ray crystallography of PfARO, structure-guided mutagenesis, GFP-based conditional mislocalization of PfAIP, proximity-based biotinylation (BioID)","journal":"Journal of molecular biology","confidence":"High","confidence_rationale":"Tier 1 / Strong — crystal structure combined with mutagenesis and functional localization assays in multiple orthogonal experiments within one study","pmids":["31877322"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"finding":"Conditional mislocalization of PfAIP (a direct binding partner of P. falciparum ARO) leads to deficient red blood cell invasion, placing the ARO–AIP interaction in the invasion pathway.","method":"Conditional mislocalization system (DiCre or analogous), red blood cell invasion assay","journal":"Journal of molecular biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional invasion phenotype from conditional mislocalization, single lab, single paper","pmids":["31877322"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2016,"finding":"PfARO (PF3D7_0414900) displays dynamic subcellular localization, shifting from the nucleus in early schizonts to rhoptries in late schizonts. PfARO possesses a putative nuclear export signal and its nucleo-apical shuttling is sensitive to Leptomycin B, indicating CRM1-dependent nuclear export. PfARO also binds DNA, specifically to an AT-rich sequence in the P. falciparum Gyrase A (PfgyrA) gene promoter region.","method":"Immunofluorescence across blood-stage life cycle, Leptomycin B treatment, DNA-binding assay with AT-rich probes from PfgyrA","journal":"PloS one","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single paper; nuclear localization and DNA-binding claims rest on indirect methods (IFA staging, EMSA-type binding); not replicated and potentially contradicts the dominant rhoptry-localization model","pmids":["26828945"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"P. falciparum ARO (PF3D7_0414900) is an armadillo-repeat protein that localizes to the cytosolic face of rhoptry membranes via dual lipid modifications (myristoylation and palmitoylation) together with critical positively charged residues (R9, K14) within its first 20 N-terminal amino acids; its five ARM repeats adopt an elongated curved structure whose concave face mediates protein–protein interactions, including a direct interaction with PfAIP that is required for PfAIP rhoptry localization and, consequently, for efficient red blood cell invasion."},"narrative":{"mechanistic_narrative":"ARO (PF3D7_0414900) is an armadillo-repeat protein that anchors to the cytosolic face of P. falciparum rhoptry membranes and serves as a scaffold linking rhoptry biogenesis to red blood cell invasion [PMID:22759070, PMID:31877322]. Membrane targeting is encoded within its first 20 N-terminal residues and depends on dual lipid modification (myristoylation and palmitoylation) acting together with positively charged residues R9 and K14; loss of the R9 charge abolishes membrane attachment, while K14/K16 substitutions redirect membrane specificity, indicating a combined lipid- and charge-based anchoring mechanism [PMID:22759070]. Structurally, ARO comprises five tandem ARM repeats arranged head-to-tail into an elongated curved shape whose concave face carries two conserved patches that mediate protein–protein interactions [PMID:31877322]. Through this concave surface ARO binds PfAIP directly, and structure-guided mutations that disrupt the interaction mislocalize PfAIP; conditional mislocalization of PfAIP in turn causes deficient invasion, placing the ARO–AIP interaction in the invasion pathway [PMID:31877322]. The machinery is functionally conserved, as P. falciparum ARO complements ARO depletion in Toxoplasma gondii and engages the same partners (AIP and ACβ), with each ARM repeat contributing to rhoptry positioning and clustering [PMID:26769898].","teleology":[{"year":2012,"claim":"Established where ARO resides and how it is tethered, answering whether this armadillo protein is membrane-associated and by what determinants.","evidence":"GFP-fusion localization and mutagenesis of N-terminal lipidation motifs and charged residues in P. falciparum","pmids":["22759070"],"confidence":"High","gaps":["Does not identify binding partners on the concave ARM surface","Functional role in invasion not tested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2016,"claim":"Tested whether ARO's role in rhoptry biogenesis is conserved and which structural elements are functionally required, showing cross-species complementation and a per-repeat contribution.","evidence":"Complementation of T. gondii ARO depletion with P. falciparum ARO, Co-IP of partners, and individual ARM-repeat deletions","pmids":["26769898"],"confidence":"Medium","gaps":["P. falciparum interactions inferred through the T. gondii complementation context rather than shown directly in P. falciparum","No structural basis for the interactions yet"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"claim":"Resolved the atomic architecture of ARO and pinpointed the surface that binds PfAIP, converting a putative scaffold into a defined interaction module.","evidence":"X-ray crystallography of PfARO, structure-guided mutagenesis, conditional PfAIP mislocalization, and BioID","pmids":["31877322"],"confidence":"High","gaps":["Second conserved concave patch has no assigned partner","Full interactome of the concave face not enumerated"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"claim":"Connected the ARO–AIP interaction to a phenotype by showing that displacing PfAIP impairs invasion, placing ARO scaffolding in the invasion pathway.","evidence":"Conditional PfAIP mislocalization and red blood cell invasion assay","pmids":["31877322"],"confidence":"Medium","gaps":["Invasion defect measured via the partner PfAIP, not by direct ARO loss-of-function","Mechanistic step of invasion affected not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2016,"claim":"Proposed an alternative nuclear/DNA-binding role for ARO, raising the question of whether it moonlights beyond rhoptry membranes.","evidence":"Immunofluorescence staging, Leptomycin B sensitivity, and AT-rich DNA-binding assay against the PfgyrA promoter in P. falciparum","pmids":["26828945"],"confidence":"Low","gaps":["Not independently replicated and potentially in tension with the dominant rhoptry-localization model","DNA binding shown by indirect probe assay without functional consequence","CRM1-dependent shuttling inferred from Leptomycin B sensitivity alone"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The direct loss-of-function phenotype of ARO itself in P. falciparum invasion, the partner for its second conserved concave patch, and the reality of its proposed nuclear/DNA-binding function remain unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No direct conditional ARO knockdown/knockout invasion phenotype in P. falciparum","Second concave interaction patch has no assigned binding partner","Nuclear shuttling and DNA-binding role unconfirmed"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["PFAIP","ACΒ"],"other_free_text":["Membrane anchoring requires both myristoylation and palmitoylation plus positively charged residues R9 and K14 within the first 20 N-terminal amino acids [#0]","Five tandem head-to-tail ARM repeats form an elongated curved structure with two conserved concave-face patches for protein-protein interaction [#2]","Directly binds PfAIP via the concave surface and is required for PfAIP rhoptry localization [#2]","P. falciparum ARO functionally complements ARO depletion in Toxoplasma gondii, indicating conserved rhoptry biogenesis machinery [#1]","Low-confidence report of CRM1-dependent nucleo-apical shuttling and AT-rich DNA binding at the PfgyrA promoter [#4]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"22759070","id":"PMC_22759070","title":"Dissection of minimal sequence requirements for rhoptry membrane targeting in the malaria parasite.","date":"2012","source":"Traffic (Copenhagen, Denmark)","url":"https://pubmed.ncbi.nlm.nih.gov/22759070","citation_count":55,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["ARO"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26769898","id":"PMC_26769898","title":"Structural and functional dissection of Toxoplasma gondii armadillo repeats only protein.","date":"2016","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/26769898","citation_count":27,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["ARO"],"competing_organism_flag":true,"competing_organism_match":"Toxoplasma","competing_organism_only":true},{"pmid":"31877322","id":"PMC_31877322","title":"Structural Insights Into PfARO and Characterization of its Interaction With PfAIP.","date":"2019","source":"Journal of molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/31877322","citation_count":19,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["ARO"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26828945","id":"PMC_26828945","title":"Evidence for the Nucleo-Apical Shuttling of a Beta-Catenin Like Plasmodium falciparum Armadillo Repeat Containing Protein.","date":"2016","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/26828945","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["ARO"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4789,"output_tokens":1609,"usd":0.019251,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6635,"output_tokens":2574,"usd":0.048763,"stage2_stop_reason":"end_turn"},"total_usd":0.068014,"stage1_batch_id":"msgbatch_01DbiymDmubkPpYvdbAu5a7V","stage2_batch_id":"msgbatch_012TbrWvMRH129T7PQ4SmvrJ","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2012,\n      \"finding\": \"ARO (PF3D7_0414900) localizes to the cytosolic face of P. falciparum rhoptry membranes, and the first 20 N-terminal amino acids are sufficient for rhoptry membrane targeting. Both myristoylation and palmitoylation motifs are required for membrane attachment, but are not sufficient alone; positively charged residues R9 and K14 within the first 20 amino acids are additionally required. Substitution of R9 with a negative charge entirely abolishes membrane attachment, while substitution of K14 (and K16) alters membrane specificity without abolishing attachment.\",\n      \"method\": \"GFP fusion protein localization, mutational analysis of N-terminal residues, lipid modification (myristoylation/palmitoylation) motif dissection in P. falciparum\",\n      \"journal\": \"Traffic (Copenhagen, Denmark)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — systematic mutagenesis with direct localization readout, multiple orthogonal point mutations tested, replicated across residues in a single rigorous study\",\n      \"pmids\": [\"22759070\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"P. falciparum ARO (PF3D7_0414900) functionally complements ARO depletion in Toxoplasma gondii and interacts with the same partners (AIP and ACβ), demonstrating conservation of rhoptry biogenesis machinery. Each armadillo (ARM) repeat of ARO contributes to its multifunctional role in rhoptry positioning and clustering.\",\n      \"method\": \"Complementation assay in T. gondii with P. falciparum ARO, co-immunoprecipitation of interacting partners, deletion of individual ARM repeats\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — complementation and Co-IP in a single study; P. falciparum ARO interactions inferred from T. gondii complementation context\",\n      \"pmids\": [\"26769898\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"The crystal structure of P. falciparum ARO (PfARO) was solved, revealing five tandem Armadillo-like (ARM) repeats arranged in a head-to-tail orientation giving an elongated curved shape. The concave face contains two distinct patches of highly conserved residues important for protein-protein interaction. Structure-guided mutagenesis identified specific PfARO mutations that cause mislocalization of PfAIP, confirming a direct ARO–AIP interaction required for PfAIP rhoptry localization.\",\n      \"method\": \"X-ray crystallography of PfARO, structure-guided mutagenesis, GFP-based conditional mislocalization of PfAIP, proximity-based biotinylation (BioID)\",\n      \"journal\": \"Journal of molecular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — crystal structure combined with mutagenesis and functional localization assays in multiple orthogonal experiments within one study\",\n      \"pmids\": [\"31877322\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Conditional mislocalization of PfAIP (a direct binding partner of P. falciparum ARO) leads to deficient red blood cell invasion, placing the ARO–AIP interaction in the invasion pathway.\",\n      \"method\": \"Conditional mislocalization system (DiCre or analogous), red blood cell invasion assay\",\n      \"journal\": \"Journal of molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional invasion phenotype from conditional mislocalization, single lab, single paper\",\n      \"pmids\": [\"31877322\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"PfARO (PF3D7_0414900) displays dynamic subcellular localization, shifting from the nucleus in early schizonts to rhoptries in late schizonts. PfARO possesses a putative nuclear export signal and its nucleo-apical shuttling is sensitive to Leptomycin B, indicating CRM1-dependent nuclear export. PfARO also binds DNA, specifically to an AT-rich sequence in the P. falciparum Gyrase A (PfgyrA) gene promoter region.\",\n      \"method\": \"Immunofluorescence across blood-stage life cycle, Leptomycin B treatment, DNA-binding assay with AT-rich probes from PfgyrA\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single paper; nuclear localization and DNA-binding claims rest on indirect methods (IFA staging, EMSA-type binding); not replicated and potentially contradicts the dominant rhoptry-localization model\",\n      \"pmids\": [\"26828945\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"P. falciparum ARO (PF3D7_0414900) is an armadillo-repeat protein that localizes to the cytosolic face of rhoptry membranes via dual lipid modifications (myristoylation and palmitoylation) together with critical positively charged residues (R9, K14) within its first 20 N-terminal amino acids; its five ARM repeats adopt an elongated curved structure whose concave face mediates protein–protein interactions, including a direct interaction with PfAIP that is required for PfAIP rhoptry localization and, consequently, for efficient red blood cell invasion.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ARO (PF3D7_0414900) is an armadillo-repeat protein that anchors to the cytosolic face of P. falciparum rhoptry membranes and serves as a scaffold linking rhoptry biogenesis to red blood cell invasion [#0, #2]. Membrane targeting is encoded within its first 20 N-terminal residues and depends on dual lipid modification (myristoylation and palmitoylation) acting together with positively charged residues R9 and K14; loss of the R9 charge abolishes membrane attachment, while K14/K16 substitutions redirect membrane specificity, indicating a combined lipid- and charge-based anchoring mechanism [#0]. Structurally, ARO comprises five tandem ARM repeats arranged head-to-tail into an elongated curved shape whose concave face carries two conserved patches that mediate protein–protein interactions [#2]. Through this concave surface ARO binds PfAIP directly, and structure-guided mutations that disrupt the interaction mislocalize PfAIP; conditional mislocalization of PfAIP in turn causes deficient invasion, placing the ARO–AIP interaction in the invasion pathway [#2, #3]. The machinery is functionally conserved, as P. falciparum ARO complements ARO depletion in Toxoplasma gondii and engages the same partners (AIP and ACβ), with each ARM repeat contributing to rhoptry positioning and clustering [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2012,\n      \"claim\": \"Established where ARO resides and how it is tethered, answering whether this armadillo protein is membrane-associated and by what determinants.\",\n      \"evidence\": \"GFP-fusion localization and mutagenesis of N-terminal lipidation motifs and charged residues in P. falciparum\",\n      \"pmids\": [\"22759070\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not identify binding partners on the concave ARM surface\", \"Functional role in invasion not tested\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Tested whether ARO's role in rhoptry biogenesis is conserved and which structural elements are functionally required, showing cross-species complementation and a per-repeat contribution.\",\n      \"evidence\": \"Complementation of T. gondii ARO depletion with P. falciparum ARO, Co-IP of partners, and individual ARM-repeat deletions\",\n      \"pmids\": [\"26769898\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"P. falciparum interactions inferred through the T. gondii complementation context rather than shown directly in P. falciparum\", \"No structural basis for the interactions yet\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Resolved the atomic architecture of ARO and pinpointed the surface that binds PfAIP, converting a putative scaffold into a defined interaction module.\",\n      \"evidence\": \"X-ray crystallography of PfARO, structure-guided mutagenesis, conditional PfAIP mislocalization, and BioID\",\n      \"pmids\": [\"31877322\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Second conserved concave patch has no assigned partner\", \"Full interactome of the concave face not enumerated\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Connected the ARO–AIP interaction to a phenotype by showing that displacing PfAIP impairs invasion, placing ARO scaffolding in the invasion pathway.\",\n      \"evidence\": \"Conditional PfAIP mislocalization and red blood cell invasion assay\",\n      \"pmids\": [\"31877322\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Invasion defect measured via the partner PfAIP, not by direct ARO loss-of-function\", \"Mechanistic step of invasion affected not defined\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Proposed an alternative nuclear/DNA-binding role for ARO, raising the question of whether it moonlights beyond rhoptry membranes.\",\n      \"evidence\": \"Immunofluorescence staging, Leptomycin B sensitivity, and AT-rich DNA-binding assay against the PfgyrA promoter in P. falciparum\",\n      \"pmids\": [\"26828945\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Not independently replicated and potentially in tension with the dominant rhoptry-localization model\", \"DNA binding shown by indirect probe assay without functional consequence\", \"CRM1-dependent shuttling inferred from Leptomycin B sensitivity alone\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The direct loss-of-function phenotype of ARO itself in P. falciparum invasion, the partner for its second conserved concave patch, and the reality of its proposed nuclear/DNA-binding function remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No direct conditional ARO knockdown/knockout invasion phenotype in P. falciparum\", \"Second concave interaction patch has no assigned binding partner\", \"Nuclear shuttling and DNA-binding role unconfirmed\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [1, 2]},\n      {\"term_id\": \"GO:0003677\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0033644\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0020008\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0044409\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"GO:0070588\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"PfAIP\", \"ACβ\"],\n    \"other_free_text\": [\n      \"Membrane anchoring requires both myristoylation and palmitoylation plus positively charged residues R9 and K14 within the first 20 N-terminal amino acids [#0]\",\n      \"Five tandem head-to-tail ARM repeats form an elongated curved structure with two conserved concave-face patches for protein-protein interaction [#2]\",\n      \"Directly binds PfAIP via the concave surface and is required for PfAIP rhoptry localization [#2]\",\n      \"P. falciparum ARO functionally complements ARO depletion in Toxoplasma gondii, indicating conserved rhoptry biogenesis machinery [#1]\",\n      \"Low-confidence report of CRM1-dependent nucleo-apical shuttling and AT-rich DNA binding at the PfgyrA promoter [#4]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0414900","name":null,"product":"armadillo-domain containing rhoptry protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0716900","name":null,"product":"armadillo-domain containing rhoptry protein, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0506500","name":null,"product":"armadillo-domain containing rhoptry protein, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"ARO","evaluation":null}