7Q3I

Human Transthyretin expressed in Vibrio natriegens

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0001523	biological_process	retinoid metabolic process
AAA	0005179	molecular_function	hormone activity
AAA	0005515	molecular_function	protein binding
AAA	0005576	cellular_component	extracellular region
AAA	0005615	cellular_component	extracellular space
AAA	0005737	cellular_component	cytoplasm
AAA	0006144	biological_process	purine nucleobase metabolic process
AAA	0007165	biological_process	signal transduction
AAA	0032991	cellular_component	protein-containing complex
AAA	0035578	cellular_component	azurophil granule lumen
AAA	0042562	molecular_function	hormone binding
AAA	0042802	molecular_function	identical protein binding
AAA	0044877	molecular_function	protein-containing complex binding
AAA	0070062	cellular_component	extracellular exosome
AAA	0140313	molecular_function	molecular sequestering activity
BBB	0001523	biological_process	retinoid metabolic process
BBB	0005179	molecular_function	hormone activity
BBB	0005515	molecular_function	protein binding
BBB	0005576	cellular_component	extracellular region
BBB	0005615	cellular_component	extracellular space
BBB	0005737	cellular_component	cytoplasm
BBB	0006144	biological_process	purine nucleobase metabolic process
BBB	0007165	biological_process	signal transduction
BBB	0032991	cellular_component	protein-containing complex
BBB	0035578	cellular_component	azurophil granule lumen
BBB	0042562	molecular_function	hormone binding
BBB	0042802	molecular_function	identical protein binding
BBB	0044877	molecular_function	protein-containing complex binding
BBB	0070062	cellular_component	extracellular exosome
BBB	0140313	molecular_function	molecular sequestering activity

Functional Information from PROSITE/UniProt

site_id	PS00768
Number of Residues	16
Details	TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV

Chain	Residue	Details
AAA	LYS15-VAL30

---

site_id	PS00769
Number of Residues	13
Details	TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS

Chain	Residue	Details
AAA	TYR105-SER117

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11418763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ICT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Sulfocysteine","evidences":[{"source":"PubMed","id":"17175208","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2H4E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"4-carboxyglutamate; in a patient with Moyamoya disease","evidences":[{"source":"PubMed","id":"18221012","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P02767","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19167329","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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