{"gene":"PBANKA_1349000","run_date":"2026-09-07T10:55:51","timeline":{"discoveries":[{"year":2002,"finding":"MSRP2 (P. yoelii ortholog) interacts with the amino-terminal region of P. yoelii MSP-1, as demonstrated by yeast two-hybrid screening and confirmed by in vitro binding experiments.","method":"Yeast two-hybrid system; in vitro binding assays","journal":"Eukaryotic cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — yeast two-hybrid plus in vitro binding, single lab, two orthogonal methods","pmids":["12477792"],"is_preprint":false,"attribution":[{"species":"Plasmodium yoelii","strain":""},{"species":"Plasmodium falciparum","strain":""}]},{"year":2004,"finding":"P. yoelii MSRP2 is expressed on the surface of schizonts, co-localizes with the amino-terminal portion of MSP-1 and with MSP-7, and is released from the parasite into culture supernatants, as shown by immunoprecipitation and immunofluorescence.","method":"Immunoprecipitation; immunofluorescence microscopy","journal":"Infection and immunity","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — immunoprecipitation and co-localization by IFA, single lab, two orthogonal methods","pmids":["14742548"],"is_preprint":false,"attribution":[{"species":"Plasmodium yoelii","strain":"17XL"}]},{"year":2010,"finding":"In P. falciparum, MSRP2 undergoes sequential proteolytic cleavages producing 28- and 25-kDa forms; unlike MSP7, MSRP2 is absent from merozoites and the 25-kDa form (MSRP2(25)) is soluble and secreted upon merozoite egress.","method":"Western blot with anti-MSRP2 antibodies; immunoblot analysis of merozoite fractions and supernatants","journal":"Eukaryotic cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct protein detection with specific antibodies and fractionation, single lab","pmids":["20472690"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2011,"finding":"PfSUB1, a subtilisin-like serine protease, proteolytically processes MSRP2 (MSP7-related protein-2) in P. falciparum, as determined by bioinformatic and proteomic analysis of the late asexual blood stage proteome.","method":"Proteomics; bioinformatic analysis of SUB1 cleavage sites","journal":"Infection and immunity","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — proteomics plus bioinformatics, single lab, established cleavage substrate","pmids":["21220481"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"P. berghei MSRP2 (PbMSRP2) directly interacts with mouse P-selectin, as shown by a systematic extracellular protein interaction screen and biochemical characterization; this interaction was mapped to involvement of the P-selectin C-type lectin and EGF-like domains.","method":"Extracellular protein interaction screen (AVEXIS); biochemical binding assays","journal":"Malaria journal","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — interaction screen plus biochemical follow-up, single lab, two methods","pmids":["26045295"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2013,"finding":"Members of the MSRP family in P. falciparum, unexpectedly, were identified as PEXEL/HT-negative exported proteins (PNEPs) that are exported into the host erythrocyte, indicating unanticipated export functions for MSRPs beyond the merozoite surface.","method":"Reporter export assays; indirect immunofluorescence in P. falciparum","journal":"PLoS pathogens","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, MSRP family members identified as PNEPs but MSRP2 specifically not individually characterized in the abstract","pmids":["23950716"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"Deletion of msrp2 (along with msp7 and msrp1) in a P. berghei triple-mutant produced no detectable impairment of life cycle progression, indicating MSRP2 is not individually required for parasite development through the life cycle.","method":"Targeted gene disruption; life cycle analysis of triple knockout parasites","journal":"Molecular and biochemical parasitology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — negative result from a triple mutant; contribution of MSRP2 alone not separable","pmids":["26222913"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]}],"current_model":"PBANKA_1349000 (MSRP2) is an MSP7-like protein whose P. yoelii ortholog is expressed on the schizont/merozoite surface and interacts with the N-terminal region of MSP-1 (shown by yeast two-hybrid and in vitro binding); in P. falciparum, MSRP2 undergoes sequential proteolytic processing by PfSUB1 generating 28- and 25-kDa forms, with the mature 25-kDa form secreted as a soluble protein upon merozoite egress rather than remaining on the merozoite surface; P. berghei MSRP2 additionally interacts with host P-selectin; deletion of msrp2 in a P. berghei triple mutant causes no detectable life-cycle defect."},"narrative":{"mechanistic_narrative":"MSRP2 (PBANKA_1349000) is an MSP7-like protein of malaria parasites associated with the schizont/merozoite surface and with the MSP-1 complex during blood-stage development [PMID:12477792, PMID:14742548]. In the P. yoelii ortholog, MSRP2 interacts with the amino-terminal region of MSP-1, co-localizes with the N-terminal portion of MSP-1 and with MSP-7 on the schizont surface, and is released into culture supernatants [PMID:12477792, PMID:14742548]. In P. falciparum, MSRP2 diverges from MSP7 in fate: it is absent from mature merozoites and is instead sequentially proteolytically processed into 28- and 25-kDa forms, with the mature 25-kDa species being soluble and secreted upon merozoite egress [PMID:20472690]; this processing is attributed to the subtilisin-like serine protease PfSUB1 [PMID:21220481]. In P. berghei, MSRP2 additionally binds host mouse P-selectin through the receptor's C-type lectin and EGF-like domains [PMID:26045295]. No individual functional requirement has been assigned to MSRP2: deletion of msrp2 within a P. berghei triple mutant produced no detectable life-cycle defect [PMID:26222913], and the biological consequence of its MSP-1 association, secretion, and P-selectin binding has not been resolved in the available corpus.","teleology":[{"year":2002,"claim":"Establishing that MSRP2 physically engages the MSP-1 machinery answered whether this MSP7-like protein belongs to the merozoite surface protein complex rather than acting independently.","evidence":"Yeast two-hybrid screen and in vitro binding assays with the P. yoelii MSP-1 N-terminus","pmids":["12477792"],"confidence":"Medium","gaps":["Binding interface on MSRP2 not mapped","Functional consequence of the MSP-1 interaction not tested","Shown only for the P. yoelii ortholog"],"attribution":[{"species":"Plasmodium yoelii","strain":""},{"species":"Plasmodium falciparum","strain":""}]},{"year":2004,"claim":"Localizing MSRP2 to the schizont surface alongside MSP-1 and MSP-7 and detecting its release established where and when it acts during blood-stage development.","evidence":"Immunoprecipitation and immunofluorescence co-localization in P. yoelii 17XL","pmids":["14742548"],"confidence":"Medium","gaps":["Mechanism and timing of release not defined","Whether release reflects processing not addressed here","Single ortholog studied"],"attribution":[{"species":"Plasmodium yoelii","strain":"17XL"}]},{"year":2010,"claim":"Showing that P. falciparum MSRP2 is processed into a soluble secreted 25-kDa form and is absent from merozoites distinguished its fate from the surface-retained MSP7, reframing MSRP2 as a secreted rather than surface-anchored protein.","evidence":"Western blot with anti-MSRP2 antibodies and fractionation of P. falciparum 3D7 merozoites and egress supernatants","pmids":["20472690"],"confidence":"Medium","gaps":["Function of the secreted 25-kDa form unknown","Fate of the 28-kDa intermediate not resolved","Divergence from MSP7 fate not explained mechanistically"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2011,"claim":"Identifying PfSUB1 as the protease that cleaves MSRP2 connected its processing to the egress protease cascade, giving a molecular basis for the sequential cleavage observed.","evidence":"Proteomic and bioinformatic analysis of SUB1 cleavage sites in the P. falciparum late asexual proteome","pmids":["21220481"],"confidence":"Medium","gaps":["Cleavage not reconstituted with purified enzyme and substrate","Order and sites of the two cleavages not resolved","Contribution of other proteases not excluded"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"Demonstrating that P. berghei MSRP2 binds host P-selectin raised the possibility of a host-interaction role distinct from its intra-parasite MSP-1 association.","evidence":"AVEXIS extracellular interaction screen with biochemical mapping to P-selectin C-type lectin and EGF-like domains in P. berghei","pmids":["26045295"],"confidence":"Medium","gaps":["In vivo relevance of P-selectin binding not shown","Whether the secreted or surface form mediates binding unclear","Affinity and physiological setting undefined"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2015,"claim":"Deleting msrp2 tested whether it is required for parasite development; the absence of a phenotype in a triple mutant indicated no individually essential life-cycle role under the conditions tested.","evidence":"Targeted gene disruption and life-cycle analysis of a P. berghei msp7/msrp1/msrp2 triple knockout","pmids":["26222913"],"confidence":"Low","gaps":["Contribution of MSRP2 alone cannot be separated from the triple deletion","Possible redundancy with family members not resolved","Subtle or condition-specific phenotypes not excluded"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"It remains unknown what biological function MSRP2 serves given its secretion, MSP-1 association, and P-selectin binding, and whether these roles are conserved or divergent across Plasmodium species.","evidence":"","pmids":[],"confidence":"Low","gaps":["No single-gene knockout phenotype defined","No mechanistic link between MSP-1 binding, secretion, and P-selectin binding","Species divergence in fate (surface vs secreted) not reconciled"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["MSP-1 surface complex (association via MSP-1 N-terminus; co-localizes with MSP-1 N-terminus and MSP-7)"],"partners":["MSP-1 (AMINO-TERMINAL REGION) [#0, #1]","MSP-7 (CO-LOCALIZATION) [#1]","PFSUB1 (PROTEASE THAT PROCESSES MSRP2) [#3]","HOST P-SELECTIN (C-TYPE LECTIN AND EGF-LIKE DOMAINS) [#4]"],"other_free_text":["In P. falciparum, MSRP2 is sequentially cleaved into 28- and 25-kDa forms; the 25-kDa form is soluble and secreted at egress and, unlike MSP7, is absent from merozoites [#2, #3].","MSRP family members in P. falciparum were identified as PEXEL/HT-negative exported proteins, but MSRP2 was not individually characterized in that report (Low confidence) [#5].","Deletion of msrp2 within a P. berghei triple mutant caused no detectable life-cycle defect; the individual requirement for MSRP2 could not be separated [#6]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"25359557","id":"PMC_25359557","title":"A comprehensive evaluation of rodent malaria parasite genomes and gene expression.","date":"2014","source":"BMC biology","url":"https://pubmed.ncbi.nlm.nih.gov/25359557","citation_count":219,"is_preprint":false,"source_species":["Pb"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23950716","id":"PMC_23950716","title":"Identification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium 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two-hybrid system; in vitro binding assays\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — yeast two-hybrid plus in vitro binding, single lab, two orthogonal methods\",\n      \"pmids\": [\"12477792\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium yoelii\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2004,\n      \"finding\": \"P. yoelii MSRP2 is expressed on the surface of schizonts, co-localizes with the amino-terminal portion of MSP-1 and with MSP-7, and is released from the parasite into culture supernatants, as shown by immunoprecipitation and immunofluorescence.\",\n      \"method\": \"Immunoprecipitation; immunofluorescence microscopy\",\n      \"journal\": \"Infection and immunity\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — immunoprecipitation and co-localization by IFA, single lab, two orthogonal methods\",\n      \"pmids\": [\"14742548\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium yoelii\", \"strain\": \"17XL\"}\n      ]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"In P. falciparum, MSRP2 undergoes sequential proteolytic cleavages producing 28- and 25-kDa forms; unlike MSP7, MSRP2 is absent from merozoites and the 25-kDa form (MSRP2(25)) is soluble and secreted upon merozoite egress.\",\n      \"method\": \"Western blot with anti-MSRP2 antibodies; immunoblot analysis of merozoite fractions and supernatants\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct protein detection with specific antibodies and fractionation, single lab\",\n      \"pmids\": [\"20472690\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"PfSUB1, a subtilisin-like serine protease, proteolytically processes MSRP2 (MSP7-related protein-2) in P. falciparum, as determined by bioinformatic and proteomic analysis of the late asexual blood stage proteome.\",\n      \"method\": \"Proteomics; bioinformatic analysis of SUB1 cleavage sites\",\n      \"journal\": \"Infection and immunity\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — proteomics plus bioinformatics, single lab, established cleavage substrate\",\n      \"pmids\": [\"21220481\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"P. berghei MSRP2 (PbMSRP2) directly interacts with mouse P-selectin, as shown by a systematic extracellular protein interaction screen and biochemical characterization; this interaction was mapped to involvement of the P-selectin C-type lectin and EGF-like domains.\",\n      \"method\": \"Extracellular protein interaction screen (AVEXIS); biochemical binding assays\",\n      \"journal\": \"Malaria journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — interaction screen plus biochemical follow-up, single lab, two methods\",\n      \"pmids\": [\"26045295\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"Members of the MSRP family in P. falciparum, unexpectedly, were identified as PEXEL/HT-negative exported proteins (PNEPs) that are exported into the host erythrocyte, indicating unanticipated export functions for MSRPs beyond the merozoite surface.\",\n      \"method\": \"Reporter export assays; indirect immunofluorescence in P. falciparum\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, MSRP family members identified as PNEPs but MSRP2 specifically not individually characterized in the abstract\",\n      \"pmids\": [\"23950716\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Deletion of msrp2 (along with msp7 and msrp1) in a P. berghei triple-mutant produced no detectable impairment of life cycle progression, indicating MSRP2 is not individually required for parasite development through the life cycle.\",\n      \"method\": \"Targeted gene disruption; life cycle analysis of triple knockout parasites\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — negative result from a triple mutant; contribution of MSRP2 alone not separable\",\n      \"pmids\": [\"26222913\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"PBANKA_1349000 (MSRP2) is an MSP7-like protein whose P. yoelii ortholog is expressed on the schizont/merozoite surface and interacts with the N-terminal region of MSP-1 (shown by yeast two-hybrid and in vitro binding); in P. falciparum, MSRP2 undergoes sequential proteolytic processing by PfSUB1 generating 28- and 25-kDa forms, with the mature 25-kDa form secreted as a soluble protein upon merozoite egress rather than remaining on the merozoite surface; P. berghei MSRP2 additionally interacts with host P-selectin; deletion of msrp2 in a P. berghei triple mutant causes no detectable life-cycle defect.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"MSRP2 (PBANKA_1349000) is an MSP7-like protein of malaria parasites associated with the schizont/merozoite surface and with the MSP-1 complex during blood-stage development [#0, #1]. In the P. yoelii ortholog, MSRP2 interacts with the amino-terminal region of MSP-1, co-localizes with the N-terminal portion of MSP-1 and with MSP-7 on the schizont surface, and is released into culture supernatants [#0, #1]. In P. falciparum, MSRP2 diverges from MSP7 in fate: it is absent from mature merozoites and is instead sequentially proteolytically processed into 28- and 25-kDa forms, with the mature 25-kDa species being soluble and secreted upon merozoite egress [#2]; this processing is attributed to the subtilisin-like serine protease PfSUB1 [#3]. In P. berghei, MSRP2 additionally binds host mouse P-selectin through the receptor's C-type lectin and EGF-like domains [#4]. No individual functional requirement has been assigned to MSRP2: deletion of msrp2 within a P. berghei triple mutant produced no detectable life-cycle defect [#6], and the biological consequence of its MSP-1 association, secretion, and P-selectin binding has not been resolved in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2002,\n      \"claim\": \"Establishing that MSRP2 physically engages the MSP-1 machinery answered whether this MSP7-like protein belongs to the merozoite surface protein complex rather than acting independently.\",\n      \"evidence\": \"Yeast two-hybrid screen and in vitro binding assays with the P. yoelii MSP-1 N-terminus\",\n      \"pmids\": [\"12477792\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Binding interface on MSRP2 not mapped\", \"Functional consequence of the MSP-1 interaction not tested\", \"Shown only for the P. yoelii ortholog\"],\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}, {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2004,\n      \"claim\": \"Localizing MSRP2 to the schizont surface alongside MSP-1 and MSP-7 and detecting its release established where and when it acts during blood-stage development.\",\n      \"evidence\": \"Immunoprecipitation and immunofluorescence co-localization in P. yoelii 17XL\",\n      \"pmids\": [\"14742548\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism and timing of release not defined\", \"Whether release reflects processing not addressed here\", \"Single ortholog studied\"],\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"17XL\"}]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Showing that P. falciparum MSRP2 is processed into a soluble secreted 25-kDa form and is absent from merozoites distinguished its fate from the surface-retained MSP7, reframing MSRP2 as a secreted rather than surface-anchored protein.\",\n      \"evidence\": \"Western blot with anti-MSRP2 antibodies and fractionation of P. falciparum 3D7 merozoites and egress supernatants\",\n      \"pmids\": [\"20472690\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Function of the secreted 25-kDa form unknown\", \"Fate of the 28-kDa intermediate not resolved\", \"Divergence from MSP7 fate not explained mechanistically\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Identifying PfSUB1 as the protease that cleaves MSRP2 connected its processing to the egress protease cascade, giving a molecular basis for the sequential cleavage observed.\",\n      \"evidence\": \"Proteomic and bioinformatic analysis of SUB1 cleavage sites in the P. falciparum late asexual proteome\",\n      \"pmids\": [\"21220481\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Cleavage not reconstituted with purified enzyme and substrate\", \"Order and sites of the two cleavages not resolved\", \"Contribution of other proteases not excluded\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Demonstrating that P. berghei MSRP2 binds host P-selectin raised the possibility of a host-interaction role distinct from its intra-parasite MSP-1 association.\",\n      \"evidence\": \"AVEXIS extracellular interaction screen with biochemical mapping to P-selectin C-type lectin and EGF-like domains in P. berghei\",\n      \"pmids\": [\"26045295\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"In vivo relevance of P-selectin binding not shown\", \"Whether the secreted or surface form mediates binding unclear\", \"Affinity and physiological setting undefined\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Deleting msrp2 tested whether it is required for parasite development; the absence of a phenotype in a triple mutant indicated no individually essential life-cycle role under the conditions tested.\",\n      \"evidence\": \"Targeted gene disruption and life-cycle analysis of a P. berghei msp7/msrp1/msrp2 triple knockout\",\n      \"pmids\": [\"26222913\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Contribution of MSRP2 alone cannot be separated from the triple deletion\", \"Possible redundancy with family members not resolved\", \"Subtle or condition-specific phenotypes not excluded\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown what biological function MSRP2 serves given its secretion, MSP-1 association, and P-selectin binding, and whether these roles are conserved or divergent across Plasmodium species.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No single-gene knockout phenotype defined\", \"No mechanistic link between MSP-1 binding, secretion, and P-selectin binding\", \"Species divergence in fate (surface vs secreted) not reconciled\"],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [0, 4]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0009986\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0005576\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0051701\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"complexes\": [\n      \"MSP-1 surface complex (association via MSP-1 N-terminus; co-localizes with MSP-1 N-terminus and MSP-7)\"\n    ],\n    \"partners\": [\n      \"MSP-1 (amino-terminal region) [#0, #1]\",\n      \"MSP-7 (co-localization) [#1]\",\n      \"PfSUB1 (protease that processes MSRP2) [#3]\",\n      \"Host P-selectin (C-type lectin and EGF-like domains) [#4]\"\n    ],\n    \"other_free_text\": [\n      \"In P. falciparum, MSRP2 is sequentially cleaved into 28- and 25-kDa forms; the 25-kDa form is soluble and secreted at egress and, unlike MSP7, is absent from merozoites [#2, #3].\",\n      \"MSRP family members in P. falciparum were identified as PEXEL/HT-negative exported proteins, but MSRP2 was not individually characterized in that report (Low confidence) [#5].\",\n      \"Deletion of msrp2 within a P. berghei triple mutant caused no detectable life-cycle defect; the individual requirement for MSRP2 could not be separated [#6].\"\n    ]\n  }\n}","audit_flag":{"gene":"PBANKA_1349000","tier":"IDENTITY_CHECK","verdict":"identity unverified","subtype":"names_other_cards","uniprot_band":"","rules_fired":"R12","issue":"No cited paper names this card; 5 of 7 cited papers name other catalogue genes (PF3D7_0930300, PF3D7_0507500, PF3D7_1410400). The summary may describe one of those genes."},"strains":[{"strain":"PbANKA","gene_id":"PBANKA_1349000","name":null,"product":"MSP7-like protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1266300","name":null,"product":"MSP7-like protein","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"MSP7A","evaluation":null}