{"gene":"PF3D7_0214100","run_date":"2026-09-08T16:26:55","timeline":{"discoveries":[{"year":2001,"finding":"SEC31 (PfSec31p) is expressed in P. falciparum-infected erythrocytes as an ~160 kDa protein absent from uninfected erythrocytes, is largely insoluble in nonionic detergent (suggesting cytoskeletal attachment), and localizes partly within the parasite and partly to structures in the erythrocyte cytoplasm that overlap with PfSar1p and the cytoadherence protein PfEMP1, supporting a role in vesicle-mediated protein trafficking outside the parasite plasma membrane.","method":"Western blot with affinity-purified antibodies against recombinant WD-40 and intervening domain fragments; Triton X-100 solubility fractionation; confocal immunofluorescence co-localization with PfSar1p and PfEMP1","journal":"Journal of cell science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization experiment with functional consequence (cytoskeletal insolubility + co-localization with trafficking and virulence markers), single lab, multiple orthogonal methods","pmids":["11591825"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"finding":"SEC31 tagged with mCherry at its C-terminus localizes to discrete cytoplasmic puncta distant from the DAPI-stained nucleus in blood-stage P. berghei parasites, with a distribution similar to that of SEC13 and SEC16, consistent with its function as a COPII vesicle coat protein at the transitional ER (tER). This pattern is present across trophozoite and gametocyte stages and changes during midgut-to-salivary-gland sporozoite maturation.","method":"Endogenous C-terminal mCherry tagging followed by live-cell fluorescence imaging; comparison with SEC13-GFP and SEC16-mCherry; co-staining with ER Tracker","journal":"Scientific reports","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct live-cell localization with multiple fluorescent marker comparisons, single lab, single organism","pmids":["30050042"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2019,"finding":"Domain analysis of SEC31 across Haemosporidia (including P. falciparum, P. knowlesi, P. yoelii, P. chabaudi, P. berghei) shows that, unlike most other apicomplexans, Haemosporidia SEC31 retains the 'Sec16_C' domain present in human SEC31, whereas SEC31 orthologs from other apicomplexan clades lack this domain.","method":"In silico domain composition and phylogenetic analysis of SEC31 sequences across apicomplexan genomes","journal":"BMC genomics","confidence":"Low","confidence_rationale":"Tier 4 / Weak — computational prediction only, no experimental validation","pmids":["30704415"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""},{"species":"Plasmodium knowlesi","strain":""},{"species":"Plasmodium yoelii","strain":""},{"species":"Plasmodium chabaudi","strain":""},{"species":"Plasmodium berghei","strain":""}]}],"current_model":"SEC31 (PF3D7_0214100) is a COPII outer-coat protein in Plasmodium falciparum and P. berghei that localizes to transitional ER exit sites within the parasite and is also exported to the erythrocyte cytoplasm where it co-localizes with the COPII GTPase PfSar1p and the virulence protein PfEMP1, supporting a role in the vesicle-mediated trafficking of parasite proteins—including cytoadherence factors—across the host erythrocyte; in blood-stage P. berghei the protein displays discrete cytoplasmic puncta consistent with COPII vesicle coat function, and its large insolubility in nonionic detergent in P. falciparum suggests cytoskeletal association."},"narrative":{"mechanistic_narrative":"SEC31 (PF3D7_0214100) is a COPII outer-coat protein of Plasmodium that functions in vesicle-mediated protein trafficking during the blood stage [PMID:11591825, PMID:30050042]. In P. falciparum-infected erythrocytes it is expressed as an ~160 kDa protein absent from uninfected cells, is largely insoluble in nonionic detergent (consistent with cytoskeletal attachment), and localizes partly within the parasite and partly to erythrocyte-cytoplasmic structures that overlap with the COPII GTPase PfSar1p and the cytoadherence virulence protein PfEMP1, linking it to trafficking of parasite proteins beyond the parasite plasma membrane [PMID:11591825]. In P. berghei, endogenously tagged SEC31 forms discrete cytoplasmic puncta distinct from the nucleus with a distribution matching SEC13 and SEC16, consistent with COPII coat function at transitional ER exit sites across trophozoite, gametocyte, and sporozoite stages [PMID:30050042]. Domain analysis indicates that Haemosporidia SEC31, including the P. falciparum ortholog, retains the Sec16_C domain found in human SEC31, unlike SEC31 from other apicomplexan clades [PMID:30704415]. Beyond these localization and domain-level observations, the biochemical activity and interaction partners of SEC31 have not been characterized in the available corpus.","teleology":[{"year":2001,"claim":"Establishing whether a COPII coat component participates in trafficking beyond the parasite boundary addressed how Plasmodium exports virulence factors into the host cell; SEC31 was shown to reside partly in the erythrocyte cytoplasm alongside PfSar1p and PfEMP1.","evidence":"Western blot with anti-recombinant-domain antibodies, Triton X-100 solubility fractionation, and confocal co-localization in P. falciparum-infected erythrocytes","pmids":["11591825"],"confidence":"Medium","gaps":["Co-localization does not demonstrate direct physical interaction with PfSar1p or PfEMP1","No functional perturbation (knockdown/knockout) to test a causal role in PfEMP1 export or cytoadherence","Basis of detergent insolubility / proposed cytoskeletal attachment not molecularly defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"claim":"Whether SEC31 behaves as a canonical COPII coat protein at ER exit sites in vivo was tested by endogenous tagging, showing punctate distribution matching SEC13 and SEC16 across multiple life-cycle stages.","evidence":"Endogenous C-terminal mCherry tagging with live-cell imaging, comparison to SEC13-GFP and SEC16-mCherry, and ER Tracker co-staining in P. berghei","pmids":["30050042"],"confidence":"Medium","gaps":["Does not establish assembly into a functional COPII coat complex biochemically","No test of an exported/erythrocyte-cytoplasmic pool as reported in P. falciparum","Functional consequence of the puncta redistribution during sporozoite maturation unresolved"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2019,"claim":"Whether SEC31 domain architecture in malaria parasites differs from other apicomplexans was assessed computationally, revealing retention of the human-like Sec16_C domain in Haemosporidia.","evidence":"In silico domain composition and phylogenetic analysis of SEC31 across apicomplexan genomes","pmids":["30704415"],"confidence":"Low","gaps":["Computational prediction only, with no experimental validation of the Sec16_C domain function","Functional significance of domain retention for SEC16 interaction or coat assembly untested"],"attribution":[{"species":"Plasmodium falciparum","strain":""},{"species":"Plasmodium knowlesi","strain":""},{"species":"Plasmodium yoelii","strain":""},{"species":"Plasmodium chabaudi","strain":""},{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"Whether SEC31 is functionally required for COPII-mediated trafficking or for PfEMP1 export and cytoadherence, and whether it directly interacts with PfSar1p, SEC13, or SEC16, remains unresolved.","evidence":"No loss-of-function or direct interaction study for SEC31 present in the corpus","pmids":[],"confidence":"Low","gaps":["No genetic knockout/knockdown phenotype for SEC31","No reciprocal biochemical demonstration of COPII complex membership","No direct evidence linking SEC31 to virulence-factor export function"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["COPII coat"],"partners":["PFSAR1P (CO-LOCALIZATION, P. FALCIPARUM)","PFEMP1 (CO-LOCALIZATION, P. FALCIPARUM)","SEC13 (CO-DISTRIBUTION, P. BERGHEI)","SEC16 (CO-DISTRIBUTION, P. BERGHEI)"],"other_free_text":["~160 kDa protein expressed in P. falciparum-infected erythrocytes and largely insoluble in nonionic detergent, suggesting cytoskeletal association [#0]","Haemosporidia SEC31, including P. falciparum, retains a human-like Sec16_C domain absent from other apicomplexan orthologs [#2]","No loss-of-function or direct-interaction data for SEC31 in the corpus"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"11591825","id":"PMC_11591825","title":"Evidence for a role for a Plasmodium falciparum homologue of Sec31p in the export of proteins to the surface of malaria parasite-infected erythrocytes.","date":"2001","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/11591825","citation_count":70,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35162991","id":"","title":"Mapping PP1c and Its Inhibitor 2 Interactomes Reveals Conserved and Specific Networks in Asexual and Sexual Stages of Plasmodium.","date":"2022","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/35162991","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"36040030","id":"","title":"TurboID Identification of Evolutionarily Divergent Components of the Nuclear Pore Complex in the Malaria Model Plasmodium berghei.","date":"2022","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/36040030","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30050042","id":"","title":"Nuclear Pore Complex Components in the Malaria Parasite Plasmodium berghei.","date":"2018","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/30050042","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"34440567","id":"","title":"Unique Endomembrane Systems and Virulence in Pathogenic Protozoa.","date":"2021","source":"Life (Basel, Switzerland)","url":"https://pubmed.ncbi.nlm.nih.gov/34440567","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"32529065","id":"","title":"Identification of Plasmodium falciparum HSP70-2 as a resident of the Plasmodium export compartment.","date":"2020","source":"Heliyon","url":"https://pubmed.ncbi.nlm.nih.gov/32529065","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"33604307","id":"","title":"Rab5b-Associated Arf1 GTPase Regulates Export of N-Myristoylated Adenylate Kinase 2 From the Endoplasmic Reticulum in Plasmodium falciparum.","date":"2021","source":"Frontiers in cellular and infection microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/33604307","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26043001","id":"","title":"Genome-Wide Collation of the Plasmodium falciparum WDR Protein Superfamily Reveals Malarial Parasite-Specific Features.","date":"2015","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/26043001","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30704415","id":"","title":"A genome-wide analysis of coatomer protein (COP) subunits of apicomplexan parasites and their evolutionary relationships.","date":"2019","source":"BMC genomics","url":"https://pubmed.ncbi.nlm.nih.gov/30704415","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23282319","id":"","title":"Module-based subnetwork alignments reveal novel transcriptional regulators in malaria parasite Plasmodium falciparum.","date":"2012","source":"BMC systems biology","url":"https://pubmed.ncbi.nlm.nih.gov/23282319","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"25418785","id":"","title":"Genome-wide RIP-Chip analysis of translational repressor-bound mRNAs in the Plasmodium gametocyte.","date":"2014","source":"Genome biology","url":"https://pubmed.ncbi.nlm.nih.gov/25418785","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"25802338","id":"","title":"The Plasmodium Class XIV Myosin, MyoB, Has a Distinct Subcellular Location in Invasive and Motile Stages of the Malaria Parasite and an Unusual Light Chain.","date":"2015","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/25802338","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"24009698","id":"","title":"Food vacuole associated enolase in plasmodium undergoes multiple post-translational modifications: evidence for atypical ubiquitination.","date":"2013","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/24009698","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SEC31"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":16834,"output_tokens":1179,"usd":0.034093,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6008,"output_tokens":2264,"usd":0.04332,"stage2_stop_reason":"end_turn"},"total_usd":0.077413,"stage1_batch_id":"msgbatch_01NE1MTa8x1hW7Lo4tAaNzY1","stage2_batch_id":"msgbatch_0141vaQdeFvbo2q39AinvXM9","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2001,\n      \"finding\": \"SEC31 (PfSec31p) is expressed in P. falciparum-infected erythrocytes as an ~160 kDa protein absent from uninfected erythrocytes, is largely insoluble in nonionic detergent (suggesting cytoskeletal attachment), and localizes partly within the parasite and partly to structures in the erythrocyte cytoplasm that overlap with PfSar1p and the cytoadherence protein PfEMP1, supporting a role in vesicle-mediated protein trafficking outside the parasite plasma membrane.\",\n      \"method\": \"Western blot with affinity-purified antibodies against recombinant WD-40 and intervening domain fragments; Triton X-100 solubility fractionation; confocal immunofluorescence co-localization with PfSar1p and PfEMP1\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization experiment with functional consequence (cytoskeletal insolubility + co-localization with trafficking and virulence markers), single lab, multiple orthogonal methods\",\n      \"pmids\": [\"11591825\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"SEC31 tagged with mCherry at its C-terminus localizes to discrete cytoplasmic puncta distant from the DAPI-stained nucleus in blood-stage P. berghei parasites, with a distribution similar to that of SEC13 and SEC16, consistent with its function as a COPII vesicle coat protein at the transitional ER (tER). This pattern is present across trophozoite and gametocyte stages and changes during midgut-to-salivary-gland sporozoite maturation.\",\n      \"method\": \"Endogenous C-terminal mCherry tagging followed by live-cell fluorescence imaging; comparison with SEC13-GFP and SEC16-mCherry; co-staining with ER Tracker\",\n      \"journal\": \"Scientific reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct live-cell localization with multiple fluorescent marker comparisons, single lab, single organism\",\n      \"pmids\": [\"30050042\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Domain analysis of SEC31 across Haemosporidia (including P. falciparum, P. knowlesi, P. yoelii, P. chabaudi, P. berghei) shows that, unlike most other apicomplexans, Haemosporidia SEC31 retains the 'Sec16_C' domain present in human SEC31, whereas SEC31 orthologs from other apicomplexan clades lack this domain.\",\n      \"method\": \"In silico domain composition and phylogenetic analysis of SEC31 sequences across apicomplexan genomes\",\n      \"journal\": \"BMC genomics\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — computational prediction only, no experimental validation\",\n      \"pmids\": [\"30704415\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium knowlesi\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium yoelii\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium chabaudi\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"SEC31 (PF3D7_0214100) is a COPII outer-coat protein in Plasmodium falciparum and P. berghei that localizes to transitional ER exit sites within the parasite and is also exported to the erythrocyte cytoplasm where it co-localizes with the COPII GTPase PfSar1p and the virulence protein PfEMP1, supporting a role in the vesicle-mediated trafficking of parasite proteins—including cytoadherence factors—across the host erythrocyte; in blood-stage P. berghei the protein displays discrete cytoplasmic puncta consistent with COPII vesicle coat function, and its large insolubility in nonionic detergent in P. falciparum suggests cytoskeletal association.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SEC31 (PF3D7_0214100) is a COPII outer-coat protein of Plasmodium that functions in vesicle-mediated protein trafficking during the blood stage [#0, #1]. In P. falciparum-infected erythrocytes it is expressed as an ~160 kDa protein absent from uninfected cells, is largely insoluble in nonionic detergent (consistent with cytoskeletal attachment), and localizes partly within the parasite and partly to erythrocyte-cytoplasmic structures that overlap with the COPII GTPase PfSar1p and the cytoadherence virulence protein PfEMP1, linking it to trafficking of parasite proteins beyond the parasite plasma membrane [#0]. In P. berghei, endogenously tagged SEC31 forms discrete cytoplasmic puncta distinct from the nucleus with a distribution matching SEC13 and SEC16, consistent with COPII coat function at transitional ER exit sites across trophozoite, gametocyte, and sporozoite stages [#1]. Domain analysis indicates that Haemosporidia SEC31, including the P. falciparum ortholog, retains the Sec16_C domain found in human SEC31, unlike SEC31 from other apicomplexan clades [#2]. Beyond these localization and domain-level observations, the biochemical activity and interaction partners of SEC31 have not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2001,\n      \"claim\": \"Establishing whether a COPII coat component participates in trafficking beyond the parasite boundary addressed how Plasmodium exports virulence factors into the host cell; SEC31 was shown to reside partly in the erythrocyte cytoplasm alongside PfSar1p and PfEMP1.\",\n      \"evidence\": \"Western blot with anti-recombinant-domain antibodies, Triton X-100 solubility fractionation, and confocal co-localization in P. falciparum-infected erythrocytes\",\n      \"pmids\": [\"11591825\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Co-localization does not demonstrate direct physical interaction with PfSar1p or PfEMP1\",\n        \"No functional perturbation (knockdown/knockout) to test a causal role in PfEMP1 export or cytoadherence\",\n        \"Basis of detergent insolubility / proposed cytoskeletal attachment not molecularly defined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Whether SEC31 behaves as a canonical COPII coat protein at ER exit sites in vivo was tested by endogenous tagging, showing punctate distribution matching SEC13 and SEC16 across multiple life-cycle stages.\",\n      \"evidence\": \"Endogenous C-terminal mCherry tagging with live-cell imaging, comparison to SEC13-GFP and SEC16-mCherry, and ER Tracker co-staining in P. berghei\",\n      \"pmids\": [\"30050042\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Does not establish assembly into a functional COPII coat complex biochemically\",\n        \"No test of an exported/erythrocyte-cytoplasmic pool as reported in P. falciparum\",\n        \"Functional consequence of the puncta redistribution during sporozoite maturation unresolved\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Whether SEC31 domain architecture in malaria parasites differs from other apicomplexans was assessed computationally, revealing retention of the human-like Sec16_C domain in Haemosporidia.\",\n      \"evidence\": \"In silico domain composition and phylogenetic analysis of SEC31 across apicomplexan genomes\",\n      \"pmids\": [\"30704415\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Computational prediction only, with no experimental validation of the Sec16_C domain function\",\n        \"Functional significance of domain retention for SEC16 interaction or coat assembly untested\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium knowlesi\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium yoelii\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium chabaudi\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether SEC31 is functionally required for COPII-mediated trafficking or for PfEMP1 export and cytoadherence, and whether it directly interacts with PfSar1p, SEC13, or SEC16, remains unresolved.\",\n      \"evidence\": \"No loss-of-function or direct interaction study for SEC31 present in the corpus\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No genetic knockout/knockdown phenotype for SEC31\",\n        \"No reciprocal biochemical demonstration of COPII complex membership\",\n        \"No direct evidence linking SEC31 to virulence-factor export function\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [\n      {\"term_id\": \"GO:0070971\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0030127\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0090110\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [\"COPII coat\"],\n    \"partners\": [\"PfSar1p (co-localization, P. falciparum)\", \"PfEMP1 (co-localization, P. falciparum)\", \"SEC13 (co-distribution, P. berghei)\", \"SEC16 (co-distribution, P. berghei)\"],\n    \"other_free_text\": [\n      \"~160 kDa protein expressed in P. falciparum-infected erythrocytes and largely insoluble in nonionic detergent, suggesting cytoskeletal association [#0]\",\n      \"Haemosporidia SEC31, including P. falciparum, retains a human-like Sec16_C domain absent from other apicomplexan orthologs [#2]\",\n      \"No loss-of-function or direct-interaction data for SEC31 in the corpus\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0214100","name":null,"product":"protein transport protein SEC31","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0311000","name":null,"product":"protein transport protein SEC31, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0406700","name":null,"product":"protein transport protein SEC31, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"SEC31","evaluation":null}