Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6I7S

Microsomal triglyceride transfer protein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0003756	molecular_function	protein disulfide isomerase activity
A	0003779	molecular_function	actin binding
A	0004656	molecular_function	procollagen-proline 4-dioxygenase activity
A	0005178	molecular_function	integrin binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0005925	cellular_component	focal adhesion
A	0006457	biological_process	protein folding
A	0006888	biological_process	endoplasmic reticulum to Golgi vesicle-mediated transport
A	0009897	cellular_component	external side of plasma membrane
A	0015035	molecular_function	protein-disulfide reductase activity
A	0016222	cellular_component	procollagen-proline 4-dioxygenase complex
A	0016853	molecular_function	isomerase activity
A	0016972	molecular_function	thiol oxidase activity
A	0018401	biological_process	peptidyl-proline hydroxylation to 4-hydroxy-L-proline
A	0019899	molecular_function	enzyme binding
A	0030027	cellular_component	lamellipodium
A	0030070	biological_process	insulin processing
A	0032991	cellular_component	protein-containing complex
A	0034663	cellular_component	endoplasmic reticulum chaperone complex
A	0034975	biological_process	protein folding in endoplasmic reticulum
A	0034976	biological_process	response to endoplasmic reticulum stress
A	0035722	biological_process	interleukin-12-mediated signaling pathway
A	0038155	biological_process	interleukin-23-mediated signaling pathway
A	0042470	cellular_component	melanosome
A	0044877	molecular_function	protein-containing complex binding
A	0045785	biological_process	positive regulation of cell adhesion
A	0046598	biological_process	positive regulation of viral entry into host cell
A	0046982	molecular_function	protein heterodimerization activity
A	0070062	cellular_component	extracellular exosome
A	0071456	biological_process	cellular response to hypoxia
A	0098761	biological_process	cellular response to interleukin-7
A	1900026	biological_process	positive regulation of substrate adhesion-dependent cell spreading
A	1902175	biological_process	regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
B	0003723	molecular_function	RNA binding
B	0003756	molecular_function	protein disulfide isomerase activity
B	0003779	molecular_function	actin binding
B	0004656	molecular_function	procollagen-proline 4-dioxygenase activity
B	0005178	molecular_function	integrin binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0005886	cellular_component	plasma membrane
B	0005925	cellular_component	focal adhesion
B	0006457	biological_process	protein folding
B	0006888	biological_process	endoplasmic reticulum to Golgi vesicle-mediated transport
B	0009897	cellular_component	external side of plasma membrane
B	0015035	molecular_function	protein-disulfide reductase activity
B	0016222	cellular_component	procollagen-proline 4-dioxygenase complex
B	0016853	molecular_function	isomerase activity
B	0016972	molecular_function	thiol oxidase activity
B	0018401	biological_process	peptidyl-proline hydroxylation to 4-hydroxy-L-proline
B	0019899	molecular_function	enzyme binding
B	0030027	cellular_component	lamellipodium
B	0030070	biological_process	insulin processing
B	0032991	cellular_component	protein-containing complex
B	0034663	cellular_component	endoplasmic reticulum chaperone complex
B	0034975	biological_process	protein folding in endoplasmic reticulum
B	0034976	biological_process	response to endoplasmic reticulum stress
B	0035722	biological_process	interleukin-12-mediated signaling pathway
B	0038155	biological_process	interleukin-23-mediated signaling pathway
B	0042470	cellular_component	melanosome
B	0044877	molecular_function	protein-containing complex binding
B	0045785	biological_process	positive regulation of cell adhesion
B	0046598	biological_process	positive regulation of viral entry into host cell
B	0046982	molecular_function	protein heterodimerization activity
B	0070062	cellular_component	extracellular exosome
B	0071456	biological_process	cellular response to hypoxia
B	0098761	biological_process	cellular response to interleukin-7
B	1900026	biological_process	positive regulation of substrate adhesion-dependent cell spreading
B	1902175	biological_process	regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
G	0005319	molecular_function	lipid transporter activity
G	0005515	molecular_function	protein binding
G	0005548	molecular_function	phospholipid transporter activity
G	0005783	cellular_component	endoplasmic reticulum
G	0005788	cellular_component	endoplasmic reticulum lumen
G	0005794	cellular_component	Golgi apparatus
G	0005829	cellular_component	cytosol
G	0006629	biological_process	lipid metabolic process
G	0006641	biological_process	triglyceride metabolic process
G	0006869	biological_process	lipid transport
G	0007623	biological_process	circadian rhythm
G	0008289	molecular_function	lipid binding
G	0009306	biological_process	protein secretion
G	0015914	biological_process	phospholipid transport
G	0015918	biological_process	sterol transport
G	0016323	cellular_component	basolateral plasma membrane
G	0031526	cellular_component	brush border membrane
G	0031528	cellular_component	microvillus membrane
G	0031982	cellular_component	vesicle
G	0034185	molecular_function	apolipoprotein binding
G	0034197	biological_process	triglyceride transport
G	0034374	biological_process	low-density lipoprotein particle remodeling
G	0034377	biological_process	plasma lipoprotein particle assembly
G	0034378	biological_process	chylomicron assembly
G	0034379	biological_process	very-low-density lipoprotein particle assembly
G	0042157	biological_process	lipoprotein metabolic process
G	0042632	biological_process	cholesterol homeostasis
G	0042953	biological_process	lipoprotein transport
G	0043235	cellular_component	receptor complex
G	0044877	molecular_function	protein-containing complex binding
G	0046982	molecular_function	protein heterodimerization activity
G	0051592	biological_process	response to calcium ion
G	0051649	biological_process	establishment of localization in cell
G	0120009	biological_process	intermembrane lipid transfer
G	0120013	molecular_function	lipid transfer activity
G	0120014	molecular_function	phospholipid transfer activity
G	0120019	molecular_function	phosphatidylcholine transfer activity
G	0120020	molecular_function	cholesterol transfer activity
G	0140344	molecular_function	triglyceride transfer activity
G	1902388	molecular_function	ceramide 1-phosphate transfer activity
G	1902389	biological_process	ceramide 1-phosphate transport
G	1904121	molecular_function	phosphatidylethanolamine transfer activity
H	0005319	molecular_function	lipid transporter activity
H	0005515	molecular_function	protein binding
H	0005548	molecular_function	phospholipid transporter activity
H	0005783	cellular_component	endoplasmic reticulum
H	0005788	cellular_component	endoplasmic reticulum lumen
H	0005794	cellular_component	Golgi apparatus
H	0005829	cellular_component	cytosol
H	0006629	biological_process	lipid metabolic process
H	0006641	biological_process	triglyceride metabolic process
H	0006869	biological_process	lipid transport
H	0007623	biological_process	circadian rhythm
H	0008289	molecular_function	lipid binding
H	0009306	biological_process	protein secretion
H	0015914	biological_process	phospholipid transport
H	0015918	biological_process	sterol transport
H	0016323	cellular_component	basolateral plasma membrane
H	0031526	cellular_component	brush border membrane
H	0031528	cellular_component	microvillus membrane
H	0031982	cellular_component	vesicle
H	0034185	molecular_function	apolipoprotein binding
H	0034197	biological_process	triglyceride transport
H	0034374	biological_process	low-density lipoprotein particle remodeling
H	0034377	biological_process	plasma lipoprotein particle assembly
H	0034378	biological_process	chylomicron assembly
H	0034379	biological_process	very-low-density lipoprotein particle assembly
H	0042157	biological_process	lipoprotein metabolic process
H	0042632	biological_process	cholesterol homeostasis
H	0042953	biological_process	lipoprotein transport
H	0043235	cellular_component	receptor complex
H	0044877	molecular_function	protein-containing complex binding
H	0046982	molecular_function	protein heterodimerization activity
H	0051592	biological_process	response to calcium ion
H	0051649	biological_process	establishment of localization in cell
H	0120009	biological_process	intermembrane lipid transfer
H	0120013	molecular_function	lipid transfer activity
H	0120014	molecular_function	phospholipid transfer activity
H	0120019	molecular_function	phosphatidylcholine transfer activity
H	0120020	molecular_function	cholesterol transfer activity
H	0140344	molecular_function	triglyceride transfer activity
H	1902388	molecular_function	ceramide 1-phosphate transfer activity
H	1902389	biological_process	ceramide 1-phosphate transport
H	1904121	molecular_function	phosphatidylethanolamine transfer activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CA A 601

Chain	Residue
A	ALA381
A	ASP383
A	LYS386
A	PHE446
A	PRO447

site_id	AC2
Number of Residues	3
Details	binding site for residue EDO A 602

Chain	Residue
A	LYS162
A	SER190
A	ASP199

site_id	AC3
Number of Residues	6
Details	binding site for residue EDO A 603

Chain	Residue
A	SER153
A	GLU154
A	PHE206
A	LYS207
A	LYS208
A	VAL150

site_id	AC4
Number of Residues	1
Details	binding site for residue EDO A 604

Chain	Residue
A	LYS276

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 605

Chain	Residue
A	LYS415
A	HOH714
G	LYS195

site_id	AC6
Number of Residues	1
Details	binding site for residue EDO A 606

Chain	Residue
A	GLY349

site_id	AC7
Number of Residues	5
Details	binding site for residue CA B 601

Chain	Residue
B	ALA381
B	ASP383
B	LYS386
B	PHE446
B	PRO447

site_id	AC8
Number of Residues	2
Details	binding site for residue PGE B 602

Chain	Residue
B	ALA118
B	ARG120

site_id	AC9
Number of Residues	5
Details	binding site for residue PGE B 603

Chain	Residue
B	TYR327
B	GLY349
G	LYS103
G	LYS105
G	LYS109

site_id	AD1
Number of Residues	6
Details	binding site for residue SO4 B 604

Chain	Residue
B	GLU322
B	GLU323
B	MET324
B	HOH708
H	ARG594
H	HIS603

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO B 605

Chain	Residue
B	VAL237
B	LYS276

site_id	AD3
Number of Residues	3
Details	binding site for residue EDO B 606

Chain	Residue
B	TYR49
B	CYS56
B	LYS81

site_id	AD4
Number of Residues	2
Details	binding site for residue EDO B 607

Chain	Residue
B	ASN419
G	LYS278

site_id	AD5
Number of Residues	3
Details	binding site for residue PEG B 608

Chain	Residue
B	GLU177
B	ALA178
B	LYS222

site_id	AD6
Number of Residues	3
Details	binding site for residue PEG B 609

Chain	Residue
B	HIS438
G	GLN95
H	HOH1039

site_id	AD7
Number of Residues	5
Details	binding site for residue PE5 G 901

Chain	Residue
G	SER646
G	SER662
G	ASN780
G	ALA809
G	PHE813

site_id	AD8
Number of Residues	4
Details	binding site for residue PGE G 902

Chain	Residue
G	GLU391
G	TYR395
G	VAL728
G	HOH1003

site_id	AD9
Number of Residues	1
Details	binding site for residue TRS G 903

Chain	Residue
G	VAL227

site_id	AE1
Number of Residues	3
Details	binding site for residue SO4 G 904

Chain	Residue
G	GLY850
G	ARG851
G	GLY852

site_id	AE2
Number of Residues	5
Details	binding site for residue SO4 G 905

Chain	Residue
G	GLU90
G	ASN91
G	PHE102
G	HOH1006
G	HOH1012

site_id	AE3
Number of Residues	4
Details	binding site for residue SO4 G 906

Chain	Residue
G	GLU536
G	LYS537
G	THR538
G	ARG644

site_id	AE4
Number of Residues	4
Details	binding site for residue SO4 G 907

Chain	Residue
G	SER39
G	ARG58
G	LYS255
G	HOH1016

site_id	AE5
Number of Residues	6
Details	binding site for residue SO4 G 908

Chain	Residue
G	SER768
G	LEU769
G	TRP770
H	ILE196
H	ALA197
H	ARG198

site_id	AE6
Number of Residues	4
Details	binding site for residue SO4 G 909

Chain	Residue
A	ARG300
G	GLN569
G	ARG610
G	SER611

site_id	AE7
Number of Residues	2
Details	binding site for residue SO4 G 910

Chain	Residue
G	ILE188
G	ALA190

site_id	AE8
Number of Residues	1
Details	binding site for residue EDO G 911

Chain	Residue
G	ARG623

site_id	AE9
Number of Residues	1
Details	binding site for residue EDO G 912

Chain	Residue
G	ARG121

site_id	AF1
Number of Residues	2
Details	binding site for residue EDO G 913

Chain	Residue
G	ASN140
G	GLU141

site_id	AF2
Number of Residues	2
Details	binding site for residue EDO G 914

Chain	Residue
G	SER296
G	LYS748

site_id	AF3
Number of Residues	2
Details	binding site for residue EDO G 915

Chain	Residue
G	ARG312
G	ASN352

site_id	AF4
Number of Residues	9
Details	binding site for residue EDO G 916

Chain	Residue
G	PHE399
G	ALA400
G	SER401
G	ILE732
G	LEU733
G	HOH1011
G	SER365
G	GLN367
G	ALA396

site_id	AF5
Number of Residues	4
Details	binding site for residue PEG G 918

Chain	Residue
G	GLN509
G	ASN549
G	HIS660
G	GLN663

site_id	AF6
Number of Residues	4
Details	binding site for residue PE5 H 901

Chain	Residue
H	SER646
H	SER662
H	ASN780
H	PHE813

site_id	AF7
Number of Residues	8
Details	binding site for residue PE4 H 902

Chain	Residue
H	LYS99
H	THR849
H	GLY850
H	ARG851
H	GLY852
H	VAL854
H	GLN856
H	HOH1055

site_id	AF8
Number of Residues	5
Details	binding site for residue PGE H 903

Chain	Residue
H	GLN509
H	ARG510
H	TYR511
H	ASP512
H	PHE651

site_id	AF9
Number of Residues	1
Details	binding site for residue PGE H 904

Chain	Residue
H	TYR554

site_id	AG1
Number of Residues	3
Details	binding site for residue PGE H 905

Chain	Residue
H	SER27
H	PHE226
H	VAL227

site_id	AG2
Number of Residues	4
Details	binding site for residue SO4 H 906

Chain	Residue
G	ARG32
G	ALA263
H	THR517
H	ASP518

site_id	AG3
Number of Residues	4
Details	binding site for residue SO4 H 907

Chain	Residue
H	GLN569
H	ARG610
H	SER611
H	HOH1005

site_id	AG4
Number of Residues	3
Details	binding site for residue SO4 H 908

Chain	Residue
H	GLN530
H	ARG540
H	PRO568

site_id	AG5
Number of Residues	2
Details	binding site for residue EDO H 909

Chain	Residue
H	THR705
H	HOH1040

site_id	AG6
Number of Residues	2
Details	binding site for residue EDO H 910

Chain	Residue
H	ARG312
H	ASN352

site_id	AG7
Number of Residues	3
Details	binding site for residue EDO H 911

Chain	Residue
H	PRO204
H	ASN205
H	GLN441

site_id	AG8
Number of Residues	1
Details	binding site for residue EDO H 912

Chain	Residue
H	TYR314

site_id	AG9
Number of Residues	2
Details	binding site for residue EDO H 913

Chain	Residue
H	THR165
H	ASN166

site_id	AH1
Number of Residues	5
Details	binding site for residue PEG H 914

Chain	Residue
H	TYR395
H	PHE399
H	LEU701
H	VAL728
H	GLY730

site_id	AH2
Number of Residues	1
Details	binding site for residue PEG H 915

Chain	Residue
H	MET692

site_id	AH3
Number of Residues	2
Details	binding site for residue PEG H 916

Chain	Residue
G	SER269
H	LYS859

site_id	AH4
Number of Residues	5
Details	binding site for residue PEG H 917

Chain	Residue
H	THR37
H	TYR38
H	SER39
H	SER61
H	LYS255

site_id	AH5
Number of Residues	1
Details	binding site for residue PEG H 918

Chain	Residue
H	GLY200

Functional Information from PROSITE/UniProt

site_id	PS00014
Number of Residues	4
Details	ER_TARGET Endoplasmic reticulum targeting sequence. KDEL

Chain	Residue	Details
A	LYS505-LEU508

site_id	PS00194
Number of Residues	19
Details	THIOREDOXIN_1 Thioredoxin family active site. LVeFYapWCGHCKaLapeY

Chain	Residue	Details
A	LEU45-TYR63
A	PHE389-TRP407

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Nucleophile

Chain	Residue	Details
A	CYS53
A	CYS56
B	CYS53
B	CYS56

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000250

Chain	Residue	Details
A	CYS397
A	CYS400
B	CYS397
B	CYS400

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Contributes to redox potential value

Chain	Residue	Details
A	GLY54
A	HIS55
B	GLY54
B	HIS55

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Lowers pKa of C-terminal Cys of first active site

Chain	Residue	Details
A	ARG120
B	ARG120

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Contributes to redox potential value => ECO:0000250

Chain	Residue	Details
A	GLY398
A	HIS399
B	GLY398
B	HIS399

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Lowers pKa of C-terminal Cys of second active site => ECO:0000250

Chain	Residue	Details
A	ARG461
B	ARG461

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P09103

Chain	Residue	Details
A	LYS200
B	LYS200

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P09103

Chain	Residue	Details
A	LYS222
A	LYS271
B	LYS222
B	LYS271

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:32149426

Chain	Residue	Details
A	SER331
A	SER427
B	SER331
B	SER427

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269\|PubMed:26091039, ECO:0000269\|PubMed:32149426

Chain	Residue	Details
A	SER357
B	SER357

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 191

Chain	Residue	Details
A	CYS53	nucleofuge, nucleophile, proton acceptor, proton donor
A	GLY54	activator, modifies pKa
A	HIS55	modifies pKa, proton acceptor, proton donor
A	CYS56

site_id	MCSA2
Number of Residues	4
Details	M-CSA 191

Chain	Residue	Details
B	CYS53	nucleofuge, nucleophile, proton acceptor, proton donor
B	GLY54	activator, modifies pKa
B	HIS55	modifies pKa, proton acceptor, proton donor
B	CYS56

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)