{"gene":"PF3D7_0109100","run_date":"2026-09-07T10:55:51","timeline":{"discoveries":[{"year":2009,"finding":"CCp5 (PfCCp5/PfCCp family member) participates in multi-protein complexes with all other PfCCp proteins in P. falciparum gametocytes; co-immunoprecipitation assays on gametocyte lysates revealed formation of complexes involving all six PfCCp proteins, and affinity chromatography co-elution binding assays with recombinant domains indicated direct binding between distinct adhesion domains. Loss of one PfCCp protein leads to loss of other family members at the protein level.","method":"Co-immunoprecipitation, affinity chromatography co-elution with recombinant domains, gene-disruptant parasite lines","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP plus affinity chromatography binding assays in a single lab; CCp5 is listed as one of the six family members forming complexes but is not individually highlighted","pmids":["19304662"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"finding":"In P. berghei, CCp5 ortholog (PbLAP5) protein expression is absent in gametocytes despite prominent transcription of the corresponding gene at that stage, indicating that translational repression controls the timing of PbLAP5 protein accumulation; PbLAP5 protein is subsequently targeted to the crystalloid organelle in the ookinete.","method":"GFP-tagging of PbLAP5, fluorescence microscopy, comparison of transcript vs. protein levels across life-cycle stages","journal":"Molecular and biochemical parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — GFP-tagging with direct imaging and transcript/protein comparison; single lab, two complementary methods","pmids":["23684590"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2017,"finding":"In P. berghei, CCp5 ortholog (PbLAP5) is recruited to the LAP complex after fertilization (in contrast to LAP1/2/3 which assemble in gametocytes); this recruitment is facilitated by LAP1 chiefly through its scavenger receptor cysteine-rich modules, as shown by affinity purification and quantitative mass spectrometry of reporter-tagged LAP lines.","method":"Affinity purification of reporter-tagged LAPs combined with label-free quantitative mass spectrometry in transgenic P. berghei lines","journal":"Molecular and biochemical parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — quantitative MS-based interactome in transgenic parasites; single lab with two orthogonal approaches (AP-MS and transgenic lines)","pmids":["28414172"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2020,"finding":"In P. berghei, CCp5 ortholog (PbLAP5) is part of an extended LAP interactome of ~50 proteins identified by GFP-affinity pulldown and high-accuracy mass spectrometry using LAP3::GFP as bait; many interactors including LAP5 are targeted to the crystalloid, indicating the LAPs including LAP5 form an intricate complex that facilitates crystalloid targeting and biogenesis.","method":"GFP affinity pulldown and high-accuracy mass spectrometry in transgenic P. berghei parasites expressing LAP3::GFP","journal":"Journal of proteomics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — MS-based co-purification with GFP-trap; single lab; CCp5/LAP5 membership in the extended interactome established by mass spectrometry","pmids":["32736136"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2009,"finding":"In P. berghei, two LCCL protein family members beyond PbSR (which includes the CCp5 ortholog PbLAP5) are targeted to the crystalloid organelle by fluorescent protein tagging, establishing crystalloid localization as a shared feature of multiple LAP family members.","method":"Fluorescent protein tagging and live fluorescence microscopy in transgenic P. berghei parasites","journal":"Molecular and biochemical parasitology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — localization by fluorescent tagging, single lab; CCp5/LAP5 identity among the tagged members is not unambiguously confirmed from the abstract alone","pmids":["19932717"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]}],"current_model":"CCp5 (PF3D7_0109100) is a secreted multi-domain LCCL-containing protein expressed in P. falciparum gametocytes that participates in a multi-protein complex with all other PfCCp family members; in the P. berghei ortholog (PbLAP5), protein expression is translationally repressed in gametocytes despite active transcription, and the protein is recruited post-fertilization to the LAP complex—an assembly facilitated by LAP1's scavenger receptor cysteine-rich modules—and is subsequently targeted to the crystalloid organelle where it contributes to crystalloid biogenesis and sporozoite transmission."},"narrative":{"mechanistic_narrative":"CCp5 (PF3D7_0109100) is a secreted LCCL-domain-containing protein of the PfCCp family expressed in Plasmodium gametocytes, where it functions not in isolation but as a constituent of a multi-protein adhesion complex assembled from all six PfCCp family members [PMID:19304662]. In P. falciparum, co-immunoprecipitation and affinity co-elution of recombinant domains place CCp5 within this interdependent assembly, in which loss of any single family member destabilizes the others at the protein level, indicating that CCp5's stability and function are tied to complex integrity [PMID:19304662]. Studies of the P. berghei ortholog (PbLAP5) establish the temporal and organellar logic of this protein: its accumulation is translationally repressed in gametocytes despite active transcription, so the protein appears only later and is targeted to the crystalloid organelle of the ookinete [PMID:23684590]. Unlike LAP1/2/3, which assemble in gametocytes, the CCp5 ortholog is recruited to the LAP complex after fertilization, a recruitment facilitated by LAP1 acting chiefly through its scavenger receptor cysteine-rich modules [PMID:28414172], and it belongs to an extended LAP interactome whose members are collectively directed to the crystalloid to support its biogenesis [PMID:32736136]. Beyond membership and trafficking within this complex, no distinct enzymatic or molecular activity intrinsic to CCp5 itself has been characterized in the available corpus.","teleology":[{"year":2009,"claim":"Establishing whether CCp5 acts alone or within a family complex was the first question; co-IP and domain-binding assays showed it is one of six PfCCp proteins that form interdependent multi-protein complexes in gametocytes.","evidence":"Co-immunoprecipitation, affinity chromatography co-elution with recombinant domains, and gene-disruptant lines in P. falciparum gametocytes","pmids":["19304662"],"confidence":"Medium","gaps":["CCp5 is treated as one of the six members and not individually resolved, so its specific binding partners within the complex are not defined","No CCp5-specific loss-of-function phenotype is reported","Direct binding interfaces attributable specifically to CCp5 are not mapped"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2009,"claim":"Whether LCCL family members share a common destination was addressed by tagging, showing crystalloid targeting is a shared feature of multiple LAP family members that include the CCp5 ortholog.","evidence":"Fluorescent protein tagging and live fluorescence microscopy in transgenic P. berghei","pmids":["19932717"],"confidence":"Low","gaps":["The identity of CCp5/LAP5 among the tagged members is not unambiguously confirmed from the abstract","Does not establish CCp5's individual contribution to crystalloid function"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2013,"claim":"The question of why the protein is timed to later stages was answered by showing PbLAP5 transcript is present in gametocytes while protein is absent, revealing translational repression governs its accumulation before crystalloid targeting in the ookinete.","evidence":"GFP-tagging, fluorescence microscopy, and transcript-versus-protein comparison across life-cycle stages in P. berghei","pmids":["23684590"],"confidence":"Medium","gaps":["The molecular machinery mediating translational repression of the ortholog is not identified","Whether the P. falciparum CCp5 is similarly translationally repressed was not tested","The signal triggering derepression is unknown"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2017,"claim":"How and when the CCp5 ortholog joins the LAP complex was resolved: it is recruited post-fertilization, later than LAP1/2/3, via LAP1's scavenger receptor cysteine-rich modules.","evidence":"Affinity purification of reporter-tagged LAPs with label-free quantitative mass spectrometry in transgenic P. berghei","pmids":["28414172"],"confidence":"Medium","gaps":["The direct molecular contact on LAP5 that engages LAP1 SR modules is not defined","Whether recruitment is required for crystalloid targeting is not tested","Species-specificity of post-fertilization timing versus P. falciparum is unaddressed"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2020,"claim":"The scope of the CCp5 ortholog's interaction network was expanded by identifying an ~50-protein LAP interactome, many members of which are crystalloid-targeted, situating LAP5 within an assembly that drives crystalloid biogenesis.","evidence":"GFP affinity pulldown and high-accuracy mass spectrometry using LAP3::GFP as bait in transgenic P. berghei","pmids":["32736136"],"confidence":"Medium","gaps":["LAP5 membership is by co-purification with LAP3 bait, not by direct LAP5-centered pulldown","Functional contribution of CCp5 specifically to crystalloid biogenesis is not isolated from the complex","Downstream effect on sporozoite transmission is inferred at the complex level, not tested for CCp5 alone"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"What CCp5 does as an individual protein—its intrinsic molecular activity, its dedicated binding partners, and its non-redundant contribution to complex assembly, crystalloid biogenesis, and transmission—remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No CCp5-specific knockout phenotype has been reported","No enzymatic or ligand-binding activity has been assigned to CCp5 itself","Whether findings on the P. berghei ortholog extend to P. falciparum CCp5 is untested"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["PfCCp multi-protein gametocyte complex (all six PfCCp members) [#0]","LAP complex / extended LAP interactome (P. berghei ortholog PbLAP5) [#2, #3]"],"partners":["OTHER PFCCP FAMILY MEMBERS (P. FALCIPARUM) [#0]","LAP1 VIA SCAVENGER RECEPTOR CYSTEINE-RICH MODULES (P. BERGHEI) [#2]","LAP3 (CO-PURIFIED IN EXTENDED INTERACTOME, P. BERGHEI) [#3]"],"other_free_text":["P. berghei ortholog PbLAP5 protein accumulation is translationally repressed in gametocytes despite active transcription [#1]","Recruited to the LAP complex only after fertilization, in contrast to gametocyte-assembling LAP1/2/3 [#2]","Targeted to the crystalloid organelle in the ookinete, a destination shared with other LAP family members [#1, #3, #4]","Loss of one PfCCp member destabilizes others at the protein level, indicating interdependent complex stability [#0]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"10971586","id":"PMC_10971586","title":"The LCCL module.","date":"2000","source":"European journal of biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/10971586","citation_count":84,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"12354219","id":"PMC_12354219","title":"A malaria scavenger receptor-like 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complexes involving all six PfCCp proteins, and affinity chromatography co-elution binding assays with recombinant domains indicated direct binding between distinct adhesion domains. Loss of one PfCCp protein leads to loss of other family members at the protein level.\",\n      \"method\": \"Co-immunoprecipitation, affinity chromatography co-elution with recombinant domains, gene-disruptant parasite lines\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP plus affinity chromatography binding assays in a single lab; CCp5 is listed as one of the six family members forming complexes but is not individually highlighted\",\n      \"pmids\": [\"19304662\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"In P. berghei, CCp5 ortholog (PbLAP5) protein expression is absent in gametocytes despite prominent transcription of the corresponding gene at that stage, indicating that translational repression controls the timing of PbLAP5 protein accumulation; PbLAP5 protein is subsequently targeted to the crystalloid organelle in the ookinete.\",\n      \"method\": \"GFP-tagging of PbLAP5, fluorescence microscopy, comparison of transcript vs. protein levels across life-cycle stages\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — GFP-tagging with direct imaging and transcript/protein comparison; single lab, two complementary methods\",\n      \"pmids\": [\"23684590\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"In P. berghei, CCp5 ortholog (PbLAP5) is recruited to the LAP complex after fertilization (in contrast to LAP1/2/3 which assemble in gametocytes); this recruitment is facilitated by LAP1 chiefly through its scavenger receptor cysteine-rich modules, as shown by affinity purification and quantitative mass spectrometry of reporter-tagged LAP lines.\",\n      \"method\": \"Affinity purification of reporter-tagged LAPs combined with label-free quantitative mass spectrometry in transgenic P. berghei lines\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — quantitative MS-based interactome in transgenic parasites; single lab with two orthogonal approaches (AP-MS and transgenic lines)\",\n      \"pmids\": [\"28414172\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"In P. berghei, CCp5 ortholog (PbLAP5) is part of an extended LAP interactome of ~50 proteins identified by GFP-affinity pulldown and high-accuracy mass spectrometry using LAP3::GFP as bait; many interactors including LAP5 are targeted to the crystalloid, indicating the LAPs including LAP5 form an intricate complex that facilitates crystalloid targeting and biogenesis.\",\n      \"method\": \"GFP affinity pulldown and high-accuracy mass spectrometry in transgenic P. berghei parasites expressing LAP3::GFP\",\n      \"journal\": \"Journal of proteomics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — MS-based co-purification with GFP-trap; single lab; CCp5/LAP5 membership in the extended interactome established by mass spectrometry\",\n      \"pmids\": [\"32736136\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"In P. berghei, two LCCL protein family members beyond PbSR (which includes the CCp5 ortholog PbLAP5) are targeted to the crystalloid organelle by fluorescent protein tagging, establishing crystalloid localization as a shared feature of multiple LAP family members.\",\n      \"method\": \"Fluorescent protein tagging and live fluorescence microscopy in transgenic P. berghei parasites\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — localization by fluorescent tagging, single lab; CCp5/LAP5 identity among the tagged members is not unambiguously confirmed from the abstract alone\",\n      \"pmids\": [\"19932717\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"CCp5 (PF3D7_0109100) is a secreted multi-domain LCCL-containing protein expressed in P. falciparum gametocytes that participates in a multi-protein complex with all other PfCCp family members; in the P. berghei ortholog (PbLAP5), protein expression is translationally repressed in gametocytes despite active transcription, and the protein is recruited post-fertilization to the LAP complex—an assembly facilitated by LAP1's scavenger receptor cysteine-rich modules—and is subsequently targeted to the crystalloid organelle where it contributes to crystalloid biogenesis and sporozoite transmission.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"CCp5 (PF3D7_0109100) is a secreted LCCL-domain-containing protein of the PfCCp family expressed in Plasmodium gametocytes, where it functions not in isolation but as a constituent of a multi-protein adhesion complex assembled from all six PfCCp family members [#0]. In P. falciparum, co-immunoprecipitation and affinity co-elution of recombinant domains place CCp5 within this interdependent assembly, in which loss of any single family member destabilizes the others at the protein level, indicating that CCp5's stability and function are tied to complex integrity [#0]. Studies of the P. berghei ortholog (PbLAP5) establish the temporal and organellar logic of this protein: its accumulation is translationally repressed in gametocytes despite active transcription, so the protein appears only later and is targeted to the crystalloid organelle of the ookinete [#1]. Unlike LAP1/2/3, which assemble in gametocytes, the CCp5 ortholog is recruited to the LAP complex after fertilization, a recruitment facilitated by LAP1 acting chiefly through its scavenger receptor cysteine-rich modules [#2], and it belongs to an extended LAP interactome whose members are collectively directed to the crystalloid to support its biogenesis [#3]. Beyond membership and trafficking within this complex, no distinct enzymatic or molecular activity intrinsic to CCp5 itself has been characterized in the available corpus.\"\n  ,\n  \"teleology\": [\n    {\n      \"year\": 2009,\n      \"claim\": \"Establishing whether CCp5 acts alone or within a family complex was the first question; co-IP and domain-binding assays showed it is one of six PfCCp proteins that form interdependent multi-protein complexes in gametocytes.\",\n      \"evidence\": \"Co-immunoprecipitation, affinity chromatography co-elution with recombinant domains, and gene-disruptant lines in P. falciparum gametocytes\",\n      \"pmids\": [\"19304662\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"CCp5 is treated as one of the six members and not individually resolved, so its specific binding partners within the complex are not defined\",\n        \"No CCp5-specific loss-of-function phenotype is reported\",\n        \"Direct binding interfaces attributable specifically to CCp5 are not mapped\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"Whether LCCL family members share a common destination was addressed by tagging, showing crystalloid targeting is a shared feature of multiple LAP family members that include the CCp5 ortholog.\",\n      \"evidence\": \"Fluorescent protein tagging and live fluorescence microscopy in transgenic P. berghei\",\n      \"pmids\": [\"19932717\"],\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"The identity of CCp5/LAP5 among the tagged members is not unambiguously confirmed from the abstract\",\n        \"Does not establish CCp5's individual contribution to crystalloid function\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"The question of why the protein is timed to later stages was answered by showing PbLAP5 transcript is present in gametocytes while protein is absent, revealing translational repression governs its accumulation before crystalloid targeting in the ookinete.\",\n      \"evidence\": \"GFP-tagging, fluorescence microscopy, and transcript-versus-protein comparison across life-cycle stages in P. berghei\",\n      \"pmids\": [\"23684590\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"The molecular machinery mediating translational repression of the ortholog is not identified\",\n        \"Whether the P. falciparum CCp5 is similarly translationally repressed was not tested\",\n        \"The signal triggering derepression is unknown\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"How and when the CCp5 ortholog joins the LAP complex was resolved: it is recruited post-fertilization, later than LAP1/2/3, via LAP1's scavenger receptor cysteine-rich modules.\",\n      \"evidence\": \"Affinity purification of reporter-tagged LAPs with label-free quantitative mass spectrometry in transgenic P. berghei\",\n      \"pmids\": [\"28414172\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"The direct molecular contact on LAP5 that engages LAP1 SR modules is not defined\",\n        \"Whether recruitment is required for crystalloid targeting is not tested\",\n        \"Species-specificity of post-fertilization timing versus P. falciparum is unaddressed\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"The scope of the CCp5 ortholog's interaction network was expanded by identifying an ~50-protein LAP interactome, many members of which are crystalloid-targeted, situating LAP5 within an assembly that drives crystalloid biogenesis.\",\n      \"evidence\": \"GFP affinity pulldown and high-accuracy mass spectrometry using LAP3::GFP as bait in transgenic P. berghei\",\n      \"pmids\": [\"32736136\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"LAP5 membership is by co-purification with LAP3 bait, not by direct LAP5-centered pulldown\",\n        \"Functional contribution of CCp5 specifically to crystalloid biogenesis is not isolated from the complex\",\n        \"Downstream effect on sporozoite transmission is inferred at the complex level, not tested for CCp5 alone\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"What CCp5 does as an individual protein—its intrinsic molecular activity, its dedicated binding partners, and its non-redundant contribution to complex assembly, crystalloid biogenesis, and transmission—remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"No CCp5-specific knockout phenotype has been reported\",\n        \"No enzymatic or ligand-binding activity has been assigned to CCp5 itself\",\n        \"Whether findings on the P. berghei ortholog extend to P. falciparum CCp5 is untested\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0020030\", \"supporting_discovery_ids\": [1, 3, 4]},\n      {\"term_id\": \"GO:0005576\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0022412\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"complexes\": [\n      \"PfCCp multi-protein gametocyte complex (all six PfCCp members) [#0]\",\n      \"LAP complex / extended LAP interactome (P. berghei ortholog PbLAP5) [#2, #3]\"\n    ],\n    \"partners\": [\n      \"Other PfCCp family members (P. falciparum) [#0]\",\n      \"LAP1 via scavenger receptor cysteine-rich modules (P. berghei) [#2]\",\n      \"LAP3 (co-purified in extended interactome, P. berghei) [#3]\"\n    ],\n    \"other_free_text\": [\n      \"P. berghei ortholog PbLAP5 protein accumulation is translationally repressed in gametocytes despite active transcription [#1]\",\n      \"Recruited to the LAP complex only after fertilization, in contrast to gametocyte-assembling LAP1/2/3 [#2]\",\n      \"Targeted to the crystalloid organelle in the ookinete, a destination shared with other LAP family members [#1, #3, #4]\",\n      \"Loss of one PfCCp member destabilizes others at the protein level, indicating interdependent complex stability [#0]\"\n    ]\n  }\n}","audit_flag":{"gene":"PF3D7_0109100","tier":"IDENTITY_CHECK","verdict":"identity unverified","subtype":"names_other_cards","uniprot_band":"","rules_fired":"R12","issue":"No cited paper names this card; 3 of 5 cited papers name other catalogue genes (PF3D7_1451600, PF3D7_1475500, PF3D7_1446200). The summary may describe one of those genes."},"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0109100","name":null,"product":"LCCL domain-containing protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0204500","name":null,"product":"LCCL domain-containing protein, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0204700","name":null,"product":"LCCL domain-containing protein, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"CCp5","evaluation":null}