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{
    "metadata": {
        "accession": "IPR042694",
        "entry_id": null,
        "type": "domain",
        "go_terms": null,
        "source_database": "interpro",
        "member_databases": {
            "cdd": {
                "cd07672": "The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR031160",
            "name": "F-BAR domain",
            "type": "Domain",
            "children": [
                {
                    "accession": "IPR034934",
                    "name": "F-BAR and double SH3 domains protein 2, F-BAR domain",
                    "type": "Domain",
                    "children": []
                },
                {
                    "accession": "IPR035494",
                    "name": "FNBP1L, F-BAR domain",
                    "type": "Domain",
                    "children": []
                },
                {
                    "accession": "IPR037449",
                    "name": "Formin-binding protein 1, F-BAR domain",
                    "type": "Domain",
                    "children": []
                },
                {
                    "accession": "IPR037451",
                    "name": "SLIT-ROBO Rho GTPase-activating protein 1, F-BAR domain",
                    "type": "Domain",
                    "children": []
                },
                {
                    "accession": "IPR037452",
                    "name": "Tyrosine-protein kinase Fer, F-BAR domain",
                    "type": "Domain",
                    "children": []
                },
                {
                    "accession": "IPR037453",
                    "name": "PACSIN2, F-BAR domain",
                    "type": "Domain",
                    "children": []
                },
                {
                    "accession": "IPR037454",
                    "name": "PACSIN1, F-BAR",
                    "type": "Domain",
                    "children": []
                },
                {
                    "accession": "IPR037957",
                    "name": "GAS7, F-BAR domain",
                    "type": "Domain",
                    "children": []
                },
                {
                    "accession": "IPR042694",
                    "name": "Proline-serine-threonine phosphatase-interacting protein 2, F-BAR domain",
                    "type": "Domain",
                    "children": []
                },
                {
                    "accession": "IPR049581",
                    "name": "Slit-Robo GTPase Activating Protein 3, F-BAR domain",
                    "type": "Domain",
                    "children": []
                },
                {
                    "accession": "IPR054713",
                    "name": "GMIP/FCHO2-like, FCH domain",
                    "type": "Domain",
                    "children": [
                        {
                            "accession": "IPR030122",
                            "name": "F-BAR domain only protein 2, F-BAR domain",
                            "type": "Domain",
                            "children": []
                        },
                        {
                            "accession": "IPR042735",
                            "name": "FCHO1, F-BAR domain",
                            "type": "Domain",
                            "children": []
                        }
                    ]
                }
            ]
        },
        "name": {
            "name": "Proline-serine-threonine phosphatase-interacting protein 2, F-BAR domain",
            "short": "PSTPIP2_F-BAR"
        },
        "description": [
            {
                "text": "<p>F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization [[cite:PUB00043263]]. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2) is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility [[cite:PUB00071674]]. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease [[cite:PUB00071675]]. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules [[cite:PUB00043263]].</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00043263": {
                "PMID": 17540576,
                "ISBN": null,
                "volume": "15",
                "issue": "7",
                "year": 2007,
                "title": "Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature.",
                "URL": null,
                "raw_pages": "839-52",
                "medline_journal": "Structure",
                "ISO_journal": "Structure",
                "authors": [
                    "Henne WM",
                    "Kent HM",
                    "Ford MG",
                    "Hegde BG",
                    "Daumke O",
                    "Butler PJ",
                    "Mittal R",
                    "Langen R",
                    "Evans PR",
                    "McMahon HT."
                ],
                "DOI_URL": "http://dx.doi.org/10.1016/j.str.2007.05.002"
            },
            "PUB00071675": {
                "PMID": 16397132,
                "ISBN": null,
                "volume": "107",
                "issue": "8",
                "year": 2006,
                "title": "Mutation of mouse Mayp/Pstpip2 causes a macrophage autoinflammatory disease.",
                "URL": null,
                "raw_pages": "3350-8",
                "medline_journal": "Blood",
                "ISO_journal": "Blood",
                "authors": [
                    "Grosse J",
                    "Chitu V",
                    "Marquardt A",
                    "Hanke P",
                    "Schmittwolf C",
                    "Zeitlmann L",
                    "Schropp P",
                    "Barth B",
                    "Yu P",
                    "Paffenholz R",
                    "Stumm G",
                    "Nehls M",
                    "Stanley ER."
                ],
                "DOI_URL": "http://dx.doi.org/10.1182/blood-2005-09-3556"
            },
            "PUB00071674": {
                "PMID": 15788569,
                "ISBN": null,
                "volume": "16",
                "issue": "6",
                "year": 2005,
                "title": "The PCH family member MAYP/PSTPIP2 directly regulates F-actin bundling and enhances filopodia formation and motility in macrophages.",
                "URL": null,
                "raw_pages": "2947-59",
                "medline_journal": "Mol Biol Cell",
                "ISO_journal": "Mol. Biol. Cell",
                "authors": [
                    "Chitu V",
                    "Pixley FJ",
                    "Macaluso F",
                    "Larson DR",
                    "Condeelis J",
                    "Yeung YG",
                    "Stanley ER."
                ],
                "DOI_URL": "http://dx.doi.org/10.1091/mbc.E04-10-0914"
            }
        },
        "set_info": null,
        "overlaps_with": [
            {
                "accession": "IPR027267",
                "name": "AH/BAR domain superfamily",
                "type": "homologous_superfamily"
            }
        ],
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 0,
            "interactions": 0,
            "matches": 269,
            "pathways": 0,
            "proteins": 269,
            "proteomes": 187,
            "sets": 0,
            "structural_models": {
                "alphafold": 237,
                "bfvd": 0
            },
            "structures": 0,
            "taxa": 668
        },
        "entry_annotations": {},
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": null
    }
}