{"gene":"PF3D7_1003600","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2014,"finding":"PF3D7_1003600 (IMC1c) is expressed in all three zoite stages (merozoite, ookinete, sporozoite) in P. berghei and is assembled into the subpellicular network (SPN) AFTER pellicle formation, in contrast to other alveolins assembled concurrently with pellicle development. Repeated failure to disrupt the pbimc1c gene by double-crossover homologous recombination provided genetic evidence that IMC1c is necessary for asexual blood-stage parasite development.","method":"GFP tagging in P. berghei, live fluorescence microscopy, attempted gene disruption by double-crossover homologous recombination","journal":"Parasitology research","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization with functional consequence (essentiality inferred from recurrent failed disruption), single lab, two orthogonal approaches","pmids":["25185663"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2017,"finding":"PF3D7_1003600 (IMC1c) is S-palmitoylated on a conserved cysteine motif. Non-palmitoylated IMC1c showed normal expression, stability, and trafficking, but parasites carrying the palmitoylation-deficient mutant displayed reduced osmotic stress resistance and reduced tensile strength, indicating that palmitoylation of IMC1c enhances cytoskeletal function by strengthening the connection between the SPN and the inner membrane complex via lipid anchoring.","method":"Site-directed mutagenesis of palmitoylation sites, osmotic stress assays, mechanical strength assays in P. berghei","journal":"Molecular and biochemical parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — mutagenesis with multiple functional readouts, single lab","pmids":["28223095"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2023,"finding":"PF3D7_1003600 (IMC1c) is essential for the asexual blood stage of P. falciparum. Conditional knockdown or loss-of-function experiments showed that parasites lacking IMC1c cannot survive, demonstrating an essential function in intraerythrocytic development.","method":"Conditional knockdown / gene essentiality assay in P. falciparum asexual blood stage","journal":"mBio","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — direct genetic loss-of-function with defined phenotypic readout, single lab, single method reported in abstract","pmids":["37712738"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"finding":"PF3D7_1003600 (IMC1c) physically interacts with PbIMC1g (a different IMC1 family member) in P. berghei, as demonstrated by pairwise yeast two-hybrid assays. The core sub-repeat motif 'EKI(V)V(I)EVP' in PbIMC1g is essential for this interaction. IMC1c is described as a component of the PHIL1 complex in this context, and together with IMC1g it helps anchor the glideosome to the subpellicular network.","method":"Pairwise yeast two-hybrid assay; motif mutagenesis","journal":"mBio","confidence":"Low","confidence_rationale":"Tier 3 / Weak — yeast two-hybrid only (no orthogonal confirmation in parasite), single lab","pmids":["39576115"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2025,"finding":"PF3D7_1003600 (IMC1c) does NOT require interaction with PfIMC1g to localize properly to the inner membrane complex in P. falciparum, and PfIMC1g similarly does not require PfIMC1c for its localization. This indicates that these two alveolins are not interdependent for compartment-specific recruitment, in contrast to the sequential dependency seen for other alveolin pairs (e.g., PfIMC1e requires PfIMC1f for basal complex recruitment). Additionally, alveolin domains of IMC1c contain unique signatures for specialized localization and are not interchangeable with domains from other alveolins.","method":"Conditional knockdown/depletion of individual alveolins with fluorescence localization readout; domain-swap experiments in P. falciparum","journal":"Cellular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization experiments with functional dependency testing, multiple alveolins tested in parallel, single lab","pmids":["41019501"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_1003600 (IMC1c) is an essential alveolin/intermediate filament-like protein of the P. falciparum inner membrane complex that is incorporated into the subpellicular network after pellicle formation, is S-palmitoylated on a conserved cysteine motif to strengthen cytoskeletal attachment to the IMC via lipid anchoring, interacts with IMC1g (as part of the PHIL1 complex) to help anchor the glideosome to the subpellicular network, and localizes to the IMC independently of IMC1g through unique signatures within its alveolin domain."},"narrative":{"mechanistic_narrative":"PF3D7_1003600 (IMC1c) is an alveolin-family protein of the Plasmodium inner membrane complex (IMC) that contributes to the mechanical integrity of the parasite pellicle and is essential for asexual blood-stage development [PMID:25185663, PMID:37712738]. In P. berghei, IMC1c is expressed across the merozoite, ookinete, and sporozoite zoite stages and, distinctively among alveolins, is incorporated into the subpellicular network only after pellicle formation rather than concurrently with it [PMID:25185663]. IMC1c is S-palmitoylated on a conserved cysteine motif; while palmitoylation is dispensable for its expression, stability, and trafficking, palmitoylation-deficient parasites show reduced osmotic-stress resistance and tensile strength, indicating that lipid anchoring of IMC1c strengthens the connection between the subpellicular network and the IMC membrane [PMID:28223095]. IMC1c physically interacts with the alveolin IMC1g via a core sub-repeat motif in IMC1g, an interaction placed in the context of the PHIL1 complex that anchors the glideosome to the subpellicular network [PMID:39576115]. However, IMC1c and IMC1g are not interdependent for IMC recruitment in P. falciparum, and unique signatures within the IMC1c alveolin domain—non-interchangeable with those of other alveolins—direct its specialized localization [PMID:41019501].","teleology":[{"year":2014,"claim":"Establishing when and where IMC1c assembles into the pellicle showed it joins the subpellicular network late and is required for parasite viability, distinguishing it from co-assembling alveolins.","evidence":"GFP tagging, live fluorescence microscopy, and repeated failed gene disruption by double-crossover homologous recombination in P. berghei","pmids":["25185663"],"confidence":"Medium","gaps":["Essentiality inferred from failure to disrupt rather than a conditional depletion","Mechanism of late SPN incorporation not defined","No molecular partners identified at this stage"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2017,"claim":"Testing the functional role of a post-translational modification revealed that S-palmitoylation of IMC1c strengthens cytoskeletal mechanics rather than governing its expression or trafficking.","evidence":"Site-directed mutagenesis of palmitoylation sites with osmotic-stress and mechanical-strength assays in P. berghei","pmids":["28223095"],"confidence":"Medium","gaps":["Palmitoyl-transferase responsible not identified","Direct evidence of lipid anchoring to the IMC membrane not shown biochemically","Whether palmitoylation is regulated across stages unknown"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2023,"claim":"Confirming essentiality in the human-infective species established IMC1c as required for intraerythrocytic survival of P. falciparum, extending the P. berghei genetic inference.","evidence":"Conditional knockdown / gene essentiality assay in P. falciparum asexual blood stage","pmids":["37712738"],"confidence":"Medium","gaps":["Terminal phenotype of depleted parasites not detailed in the corpus","Which developmental step fails upon loss not resolved","Single method reported"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"claim":"Identifying a direct binding partner placed IMC1c within a defined molecular interaction, linking it to IMC1g and, in that context, to glideosome anchoring via the PHIL1 complex.","evidence":"Pairwise yeast two-hybrid assays with motif mutagenesis identifying the required EKI(V)V(I)EVP sub-repeat in PbIMC1g (P. berghei)","pmids":["39576115"],"confidence":"Low","gaps":["Yeast two-hybrid only, with no orthogonal confirmation in the parasite","Whether the interaction is direct in vivo unconfirmed","IMC1c's specific contribution to the PHIL1 complex not separated from IMC1g's"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2025,"claim":"Testing whether the IMC1c–IMC1g interaction governs localization showed the two alveolins are recruited independently, and that IMC1c carries unique, non-interchangeable alveolin-domain signatures for its targeting.","evidence":"Conditional depletion of individual alveolins with fluorescence localization readout and domain-swap experiments in P. falciparum","pmids":["41019501"],"confidence":"Medium","gaps":["The specific sequence determinants within the alveolin domain that direct localization not mapped","The trans factor that recruits IMC1c to the IMC unidentified","Reconciliation of independent recruitment with the reported IMC1g interaction not fully resolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"How IMC1c is recruited to the subpellicular network after pellicle formation, and the molecular basis by which its unique alveolin-domain signatures specify localization, remain open.","evidence":"","pmids":[],"confidence":"Low","gaps":["No recruitment factor or targeting mechanism identified","Structural basis of alveolin-domain specialization unknown","Direct in-parasite validation of the IMC1g interaction lacking"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["PHIL1 complex (contextual membership reported in P. berghei) [#3]"],"partners":["IMC1G (DIRECT INTERACTION BY YEAST TWO-HYBRID, P. BERGHEI) [#3]"],"other_free_text":["S-palmitoylated on a conserved cysteine motif; palmitoylation enhances cytoskeletal mechanical strength without affecting expression or trafficking [#1]","Assembled into the subpellicular network after pellicle formation, unlike co-assembling alveolins [#0]","Essential for asexual blood-stage development in both P. berghei (failed disruption) and P. falciparum (conditional knockdown) [#0, #2]","Localizes to the IMC independently of IMC1g via unique, non-interchangeable alveolin-domain signatures [#4]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"20037583","id":"PMC_20037583","title":"Transcriptional profiling of growth perturbations of the human malaria parasite Plasmodium falciparum.","date":"2009","source":"Nature biotechnology","url":"https://pubmed.ncbi.nlm.nih.gov/20037583","citation_count":160,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"37712738","id":"PMC_37712738","title":"Essential function of alveolin PfIMC1g in the Plasmodium falciparum asexual blood stage.","date":"2023","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/37712738","citation_count":25,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfIMC1c"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"25185663","id":"PMC_25185663","title":"Distinct temporal recruitment of Plasmodium alveolins to the subpellicular network.","date":"2014","source":"Parasitology research","url":"https://pubmed.ncbi.nlm.nih.gov/25185663","citation_count":21,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PbIMC1c"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28223095","id":"PMC_28223095","title":"Palmitoylation of Plasmodium alveolins promotes cytoskeletal function.","date":"2017","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/28223095","citation_count":16,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["IMC1c"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"39576115","id":"PMC_39576115","title":"An inner membrane complex protein IMC1g in Plasmodium berghei is involved in asexual stage schizogony and parasite transmission.","date":"2024","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/39576115","citation_count":6,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["IMC1c","PbIMC1c"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"41019501","id":"PMC_41019501","title":"Malaria Cytoskeletal Proteins Require Alveolin-Alveolin Interactions for Differential Localization: Recruitment and Organization of Alveolin Proteins.","date":"2025","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/41019501","citation_count":2,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfIMC1c"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5583,"output_tokens":1584,"usd":0.020255,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6564,"output_tokens":2676,"usd":0.04986,"stage2_stop_reason":"end_turn"},"total_usd":0.070115,"stage1_batch_id":"msgbatch_01DisAaTypwmC8QwdMBuePHo","stage2_batch_id":"msgbatch_0184zxZTqxiEfdYYfPMfkqjb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"PF3D7_1003600 (IMC1c) is expressed in all three zoite stages (merozoite, ookinete, sporozoite) in P. berghei and is assembled into the subpellicular network (SPN) AFTER pellicle formation, in contrast to other alveolins assembled concurrently with pellicle development. Repeated failure to disrupt the pbimc1c gene by double-crossover homologous recombination provided genetic evidence that IMC1c is necessary for asexual blood-stage parasite development.\",\n      \"method\": \"GFP tagging in P. berghei, live fluorescence microscopy, attempted gene disruption by double-crossover homologous recombination\",\n      \"journal\": \"Parasitology research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization with functional consequence (essentiality inferred from recurrent failed disruption), single lab, two orthogonal approaches\",\n      \"pmids\": [\"25185663\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"PF3D7_1003600 (IMC1c) is S-palmitoylated on a conserved cysteine motif. Non-palmitoylated IMC1c showed normal expression, stability, and trafficking, but parasites carrying the palmitoylation-deficient mutant displayed reduced osmotic stress resistance and reduced tensile strength, indicating that palmitoylation of IMC1c enhances cytoskeletal function by strengthening the connection between the SPN and the inner membrane complex via lipid anchoring.\",\n      \"method\": \"Site-directed mutagenesis of palmitoylation sites, osmotic stress assays, mechanical strength assays in P. berghei\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — mutagenesis with multiple functional readouts, single lab\",\n      \"pmids\": [\"28223095\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"PF3D7_1003600 (IMC1c) is essential for the asexual blood stage of P. falciparum. Conditional knockdown or loss-of-function experiments showed that parasites lacking IMC1c cannot survive, demonstrating an essential function in intraerythrocytic development.\",\n      \"method\": \"Conditional knockdown / gene essentiality assay in P. falciparum asexual blood stage\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — direct genetic loss-of-function with defined phenotypic readout, single lab, single method reported in abstract\",\n      \"pmids\": [\"37712738\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"PF3D7_1003600 (IMC1c) physically interacts with PbIMC1g (a different IMC1 family member) in P. berghei, as demonstrated by pairwise yeast two-hybrid assays. The core sub-repeat motif 'EKI(V)V(I)EVP' in PbIMC1g is essential for this interaction. IMC1c is described as a component of the PHIL1 complex in this context, and together with IMC1g it helps anchor the glideosome to the subpellicular network.\",\n      \"method\": \"Pairwise yeast two-hybrid assay; motif mutagenesis\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — yeast two-hybrid only (no orthogonal confirmation in parasite), single lab\",\n      \"pmids\": [\"39576115\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"PF3D7_1003600 (IMC1c) does NOT require interaction with PfIMC1g to localize properly to the inner membrane complex in P. falciparum, and PfIMC1g similarly does not require PfIMC1c for its localization. This indicates that these two alveolins are not interdependent for compartment-specific recruitment, in contrast to the sequential dependency seen for other alveolin pairs (e.g., PfIMC1e requires PfIMC1f for basal complex recruitment). Additionally, alveolin domains of IMC1c contain unique signatures for specialized localization and are not interchangeable with domains from other alveolins.\",\n      \"method\": \"Conditional knockdown/depletion of individual alveolins with fluorescence localization readout; domain-swap experiments in P. falciparum\",\n      \"journal\": \"Cellular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization experiments with functional dependency testing, multiple alveolins tested in parallel, single lab\",\n      \"pmids\": [\"41019501\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1003600 (IMC1c) is an essential alveolin/intermediate filament-like protein of the P. falciparum inner membrane complex that is incorporated into the subpellicular network after pellicle formation, is S-palmitoylated on a conserved cysteine motif to strengthen cytoskeletal attachment to the IMC via lipid anchoring, interacts with IMC1g (as part of the PHIL1 complex) to help anchor the glideosome to the subpellicular network, and localizes to the IMC independently of IMC1g through unique signatures within its alveolin domain.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1003600 (IMC1c) is an alveolin-family protein of the Plasmodium inner membrane complex (IMC) that contributes to the mechanical integrity of the parasite pellicle and is essential for asexual blood-stage development [#0, #2]. In P. berghei, IMC1c is expressed across the merozoite, ookinete, and sporozoite zoite stages and, distinctively among alveolins, is incorporated into the subpellicular network only after pellicle formation rather than concurrently with it [#0]. IMC1c is S-palmitoylated on a conserved cysteine motif; while palmitoylation is dispensable for its expression, stability, and trafficking, palmitoylation-deficient parasites show reduced osmotic-stress resistance and tensile strength, indicating that lipid anchoring of IMC1c strengthens the connection between the subpellicular network and the IMC membrane [#1]. IMC1c physically interacts with the alveolin IMC1g via a core sub-repeat motif in IMC1g, an interaction placed in the context of the PHIL1 complex that anchors the glideosome to the subpellicular network [#3]. However, IMC1c and IMC1g are not interdependent for IMC recruitment in P. falciparum, and unique signatures within the IMC1c alveolin domain—non-interchangeable with those of other alveolins—direct its specialized localization [#4].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Establishing when and where IMC1c assembles into the pellicle showed it joins the subpellicular network late and is required for parasite viability, distinguishing it from co-assembling alveolins.\",\n      \"evidence\": \"GFP tagging, live fluorescence microscopy, and repeated failed gene disruption by double-crossover homologous recombination in P. berghei\",\n      \"pmids\": [\"25185663\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Essentiality inferred from failure to disrupt rather than a conditional depletion\", \"Mechanism of late SPN incorporation not defined\", \"No molecular partners identified at this stage\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Testing the functional role of a post-translational modification revealed that S-palmitoylation of IMC1c strengthens cytoskeletal mechanics rather than governing its expression or trafficking.\",\n      \"evidence\": \"Site-directed mutagenesis of palmitoylation sites with osmotic-stress and mechanical-strength assays in P. berghei\",\n      \"pmids\": [\"28223095\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Palmitoyl-transferase responsible not identified\", \"Direct evidence of lipid anchoring to the IMC membrane not shown biochemically\", \"Whether palmitoylation is regulated across stages unknown\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Confirming essentiality in the human-infective species established IMC1c as required for intraerythrocytic survival of P. falciparum, extending the P. berghei genetic inference.\",\n      \"evidence\": \"Conditional knockdown / gene essentiality assay in P. falciparum asexual blood stage\",\n      \"pmids\": [\"37712738\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Terminal phenotype of depleted parasites not detailed in the corpus\", \"Which developmental step fails upon loss not resolved\", \"Single method reported\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Identifying a direct binding partner placed IMC1c within a defined molecular interaction, linking it to IMC1g and, in that context, to glideosome anchoring via the PHIL1 complex.\",\n      \"evidence\": \"Pairwise yeast two-hybrid assays with motif mutagenesis identifying the required EKI(V)V(I)EVP sub-repeat in PbIMC1g (P. berghei)\",\n      \"pmids\": [\"39576115\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Yeast two-hybrid only, with no orthogonal confirmation in the parasite\", \"Whether the interaction is direct in vivo unconfirmed\", \"IMC1c's specific contribution to the PHIL1 complex not separated from IMC1g's\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Testing whether the IMC1c–IMC1g interaction governs localization showed the two alveolins are recruited independently, and that IMC1c carries unique, non-interchangeable alveolin-domain signatures for its targeting.\",\n      \"evidence\": \"Conditional depletion of individual alveolins with fluorescence localization readout and domain-swap experiments in P. falciparum\",\n      \"pmids\": [\"41019501\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"The specific sequence determinants within the alveolin domain that direct localization not mapped\", \"The trans factor that recruits IMC1c to the IMC unidentified\", \"Reconciliation of independent recruitment with the reported IMC1g interaction not fully resolved\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How IMC1c is recruited to the subpellicular network after pellicle formation, and the molecular basis by which its unique alveolin-domain signatures specify localization, remain open.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No recruitment factor or targeting mechanism identified\", \"Structural basis of alveolin-domain specialization unknown\", \"Direct in-parasite validation of the IMC1g interaction lacking\"],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198 structural molecule activity\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0042802 identical/protein binding (to IMC1g)\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"inner membrane complex / subpellicular network\", \"supporting_discovery_ids\": [0, 4]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"pellicle/cytoskeleton assembly and mechanical integrity\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"glideosome anchoring to subpellicular network (PHIL1 complex context)\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"complexes\": [\n      \"PHIL1 complex (contextual membership reported in P. berghei) [#3]\"\n    ],\n    \"partners\": [\n      \"IMC1g (direct interaction by yeast two-hybrid, P. berghei) [#3]\"\n    ],\n    \"other_free_text\": [\n      \"S-palmitoylated on a conserved cysteine motif; palmitoylation enhances cytoskeletal mechanical strength without affecting expression or trafficking [#1]\",\n      \"Assembled into the subpellicular network after pellicle formation, unlike co-assembling alveolins [#0]\",\n      \"Essential for asexual blood-stage development in both P. berghei (failed disruption) and P. falciparum (conditional knockdown) [#0, #2]\",\n      \"Localizes to the IMC independently of IMC1g via unique, non-interchangeable alveolin-domain signatures [#4]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1003600","name":null,"product":"inner membrane complex protein 1c","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1202000","name":null,"product":"inner membrane complex protein 1c","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0802400","name":null,"product":"inner membrane complex protein 1c, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"IMC1c","evaluation":null}