2YG2

Structure of apolioprotein M in complex with Sphingosine 1-Phosphate

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
B	SCOP2 Family	ApoM domain-like	8045815	4004704	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Lipocalins	8052635	3001332	SCOP2 (2022-06-29)
A	SCOP2B Superfamily	Lipocalins	8052635	3001332	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)
B	ApoM	e2yg2B1	A: beta barrels	X: Lipocalins/Streptavidin	H: Lipocalins (From Topology)	T: Lipocalins	F: ApoM	ECOD (1.6)
A	ApoM	e2yg2A1	A: beta barrels	X: Lipocalins/Streptavidin	H: Lipocalins (From Topology)	T: Lipocalins	F: ApoM	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.40.128.20	Mainly Beta	Beta Barrel	Lipocalin	Calycin beta-barrel core domain	CATH (4.3.0)
A	2.40.128.20	Mainly Beta	Beta Barrel	Lipocalin	Calycin beta-barrel core domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF11032	ApoM domain (ApoM)	ApoM domain	ApoM is a 25 kDa plasma protein associated with high-density lipoproteins (HDLs). ApoM is important in the formation of pre-ss-HDL and also in increasing cholesterol efflux from macrophage foam cells [1]. Lipoproteins consist of lipids solubilized by ...	ApoM is a 25 kDa plasma protein associated with high-density lipoproteins (HDLs). ApoM is important in the formation of pre-ss-HDL and also in increasing cholesterol efflux from macrophage foam cells [1]. Lipoproteins consist of lipids solubilized by apolipoproteins. ApoM lacks an external amphipathic motif and is uniquely secreted to plasma without cleavage of its terminal signal peptide [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	APOLIPOPROTEIN M	antioxidant activity binding phospholipid binding lipid binding lipid transporter activity transporter activity	plasma lipoprotein particle organization multicellular organismal process regulation of biological process protein-containing complex organization protein-lipid complex organization biological regulation regulation of plasma lipoprotein particle levels cellular component organization cellular component biogenesis cellular component assembly high-density lipoprotein particle assembly protein-containing complex assembly cellular process plasma lipoprotein particle assembly plasma lipoprotein particle organization multicellular organismal process regulation of biological process protein-containing complex organization protein-lipid complex organization biological regulation regulation of plasma lipoprotein particle levels cellular component organization cellular component biogenesis cellular component assembly high-density lipoprotein particle assembly protein-containing complex assembly cellular process plasma lipoprotein particle assembly protein-lipid complex assembly cellular component organization or biogenesis high-density lipoprotein particle clearance plasma lipoprotein particle clearance transport organic substance transport reverse cholesterol transport lipid localization lipid transport organic hydroxy compound transport establishment of localization localization macromolecule localization cholesterol transport sterol transport cholesterol efflux organic substance metabolic process organonitrogen compound metabolic process lipoprotein metabolic process metabolic process primary metabolic process protein metabolic process macromolecule metabolic process protein-containing complex remodeling plasma lipoprotein particle remodeling high-density lipoprotein particle remodeling protein-lipid complex remodeling regulation of cellular component organization regulation of cellular process negative regulation of biological process regulation of plasma lipoprotein oxidation negative regulation of cellular process regulation of multicellular organismal process negative regulation of cellular component organization negative regulation of plasma lipoprotein oxidation negative regulation of multicellular organismal process plasma lipoprotein particle oxidation sterol homeostasis chemical homeostasis homeostatic process cholesterol homeostasis lipid homeostasis	discoidal high-density lipoprotein particle protein-containing complex extracellular region plasma lipoprotein particle high-density lipoprotein particle extracellular space cellular anatomical entity lipoprotein particle protein-lipid complex low-density lipoprotein particle spherical high-density lipoprotein particle very-low-density lipoprotein particle triglyceride-rich plasma lipoprotein particle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR012674	Calycin	Homologous Superfamily
A, B	IPR022734	Apolipoprotein M	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: O95445	rheumatoid arthritis autism spectrum disorder cutaneous lupus erythematosus laryngeal squamous cell carcinoma malignant ependymoma nephrosclerosis psoriatic arthritis systemic lupus erythematosus cancer Hashimoto thyroiditis lung adenocarcinoma medulloblastoma osteosarcoma Crohn disease hypertensive disorder rheumatoid arthritis autism spectrum disorder cutaneous lupus erythematosus laryngeal squamous cell carcinoma malignant ependymoma nephrosclerosis psoriatic arthritis systemic lupus erythematosus cancer Hashimoto thyroiditis lung adenocarcinoma medulloblastoma osteosarcoma Crohn disease hypertensive disorder lung carcinoma membranous glomerulonephritis pancreatic ductal adenocarcinoma squamous cell lung carcinoma

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.