5TOD | pdb_00005tod

Transmembrane protein 24 SMP domain

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth F]	SCOP2B Superfamily	Aha1/BPI domain-like	8101163	3001851	SCOP2B (2022-06-29)
B [auth A]	SCOP2 Family	C2CD2L SMP domain-like	8101162	4007814	SCOP2 (2022-06-29)
B [auth A]	SCOP2 Superfamily	Aha1/BPI domain-like	8101163	3001851	SCOP2 (2022-06-29)
C [auth B]	SCOP2B Superfamily	Aha1/BPI domain-like	8101163	3001851	SCOP2B (2022-06-29)
D [auth C]	SCOP2B Superfamily	Aha1/BPI domain-like	8101163	3001851	SCOP2B (2022-06-29)
E [auth D]	SCOP2B Superfamily	Aha1/BPI domain-like	8101163	3001851	SCOP2B (2022-06-29)
F [auth E]	SCOP2B Superfamily	Aha1/BPI domain-like	8101163	3001851	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth F]	EUF08572	e5todF1	A: a+b complex topology	X: Aha1/BPI domain-like (From Topology)	H: Aha1/BPI domain-like (From Topology)	T: Aha1/BPI domain-like	F: EUF08572	ECOD (1.6)
B [auth A]	EUF08572	e5todA1	A: a+b complex topology	X: Aha1/BPI domain-like (From Topology)	H: Aha1/BPI domain-like (From Topology)	T: Aha1/BPI domain-like	F: EUF08572	ECOD (1.6)
C [auth B]	EUF08572	e5todB1	A: a+b complex topology	X: Aha1/BPI domain-like (From Topology)	H: Aha1/BPI domain-like (From Topology)	T: Aha1/BPI domain-like	F: EUF08572	ECOD (1.6)
D [auth C]	EUF08572	e5todC1	A: a+b complex topology	X: Aha1/BPI domain-like (From Topology)	H: Aha1/BPI domain-like (From Topology)	T: Aha1/BPI domain-like	F: EUF08572	ECOD (1.6)
E [auth D]	EUF08572	e5todD1	A: a+b complex topology	X: Aha1/BPI domain-like (From Topology)	H: Aha1/BPI domain-like (From Topology)	T: Aha1/BPI domain-like	F: EUF08572	ECOD (1.6)
F [auth E]	EUF08572	e5todE1	A: a+b complex topology	X: Aha1/BPI domain-like (From Topology)	H: Aha1/BPI domain-like (From Topology)	T: Aha1/BPI domain-like	F: EUF08572	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E]	PF18696	Synaptotagmin-like, mitochondrial and lipid-binding domain (SMP_C2CD2L)	Synaptotagmin-like, mitochondrial and lipid-binding domain	This is a lipid transport domain found in phospholipid transfer proteins such as C2CD2L-like (also known as TMEM24). The TMEM24-SMP domain is shown to bind glycerolipids with a preference for phosphatidylinositol (PI).The bound PI is then transferred ...	This is a lipid transport domain found in phospholipid transfer proteins such as C2CD2L-like (also known as TMEM24). The TMEM24-SMP domain is shown to bind glycerolipids with a preference for phosphatidylinositol (PI).The bound PI is then transferred to the plasma membrane (PM) where it is converted to phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to replenish pools of this lipid hydrolyzed during glucose-stimulated signaling. PI(4,5)P2 is required for Ca2+-dependent exocytosis hence, the SMP domain of TMEM24 is essential for sustaining the intracellular Ca2+ oscillations that trigger bursts of insulin granule release and hence insulin secretion. The SMP domain belongs to a superfamily of lipid/hydrophobic ligand-binding domains called TULIP for (tubular lipid-binding proteins) it adopts TULIP fold with two alpha helices and a highly curved antiparallel beta sheet forming a cornucopia-like structure [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E]	Transmembrane protein 24	binding phospholipid binding lipid binding phosphatidylinositol binding phospholipid transfer activity lipid transporter activity lipid transfer activity phosphatidylinositol transfer activity transporter activity phospholipid transporter activity amide binding protein binding peptide hormone binding hormone binding binding phospholipid binding lipid binding phosphatidylinositol binding phospholipid transfer activity lipid transporter activity lipid transfer activity phosphatidylinositol transfer activity transporter activity phospholipid transporter activity amide binding protein binding peptide hormone binding hormone binding insulin binding	protein localization cellular response to stimulus positive regulation of cell communication regulation of localization establishment of protein localization nitrogen compound transport regulation of cellular process response to stimulus positive regulation of establishment of protein localization cell communication localization carbohydrate homeostasis cellular macromolecule localization establishment of localization in cell positive regulation of insulin secretion involved in cellular response to glucose stimulus protein localization cellular response to stimulus positive regulation of cell communication regulation of localization establishment of protein localization nitrogen compound transport regulation of cellular process response to stimulus positive regulation of establishment of protein localization cell communication localization carbohydrate homeostasis cellular macromolecule localization establishment of localization in cell positive regulation of insulin secretion involved in cellular response to glucose stimulus positive regulation of insulin secretion regulation of biological quality regulation of peptide hormone secretion regulation of biological process regulation of hormone levels positive regulation of peptide hormone secretion establishment of protein localization to extracellular region intracellular glucose homeostasis protein secretion establishment of localization cellular response to oxygen-containing compound regulation of protein secretion regulation of secretion cellular response to carbohydrate stimulus chemical homeostasis response to glucose response to chemical glucose homeostasis positive regulation of protein localization insulin secretion involved in cellular response to glucose stimulus cellular localization regulation of hormone secretion regulation of protein localization regulation of peptide secretion transport signaling homeostatic process positive regulation of biological process positive regulation of secretion by cell hormone secretion protein localization to extracellular region positive regulation of protein transport peptide secretion regulation of secretion by cell secretion by cell positive regulation of hormone secretion response to monosaccharide response to carbohydrate positive regulation of secretion amide transport signal release cellular response to hexose stimulus intracellular chemical homeostasis cellular response to monosaccharide stimulus positive regulation of cellular process positive regulation of peptide secretion regulation of signaling regulation of transport secretion regulation of peptide transport biological regulation regulation of establishment of protein localization export from cell cell-cell signaling response to oxygen-containing compound cellular response to glucose stimulus regulation of protein transport positive regulation of protein secretion peptide transport response to hexose cellular response to chemical stimulus cellular homeostasis positive regulation of transport protein transport regulation of cellular localization regulation of insulin secretion peptide hormone secretion macromolecule localization regulation of insulin secretion involved in cellular response to glucose stimulus hormone transport regulation of cell communication cellular process insulin secretion positive regulation of signaling	cell periphery cellular anatomical structure plasma membrane membrane endoplasmic reticulum-plasma membrane contact site organelle membrane contact site organelle membrane-bounded organelle cell cortex intracellular anatomical structure cortical endoplasmic reticulum organelle subcompartment intracellular membrane-bounded organelle endomembrane system cell periphery cellular anatomical structure plasma membrane membrane endoplasmic reticulum-plasma membrane contact site organelle membrane contact site organelle membrane-bounded organelle cell cortex intracellular anatomical structure cortical endoplasmic reticulum organelle subcompartment intracellular membrane-bounded organelle endomembrane system endoplasmic reticulum subcompartment intracellular organelle endoplasmic reticulum cytoplasm endoplasmic reticulum tubular network nuclear outer membrane-endoplasmic reticulum membrane network organelle membrane endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E]	IPR039934	C2 domain-containing protein 2-like	Family
A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E]	IPR000008	C2 domain	Domain
A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E]	IPR035892	C2 domain superfamily	Homologous Superfamily
A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E]	IPR040885	Synaptotagmin-like, mitochondrial and lipid-binding domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], A [auth F], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E]	Pharos: O14523	atypical teratoid rhabdoid tumor malignant ependymoma medulloblastoma psoriasis glioblastoma malignant glioma osteosarcoma tuberculosis heart disease malignant mesothelioma pilocytic astrocytoma

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.