8Z9V

Amyloid beta and TTR

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001523	biological_process	retinoid metabolic process
A	0005179	molecular_function	hormone activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0006144	biological_process	purine nucleobase metabolic process
A	0007165	biological_process	signal transduction
A	0032991	cellular_component	protein-containing complex
A	0035578	cellular_component	azurophil granule lumen
A	0042562	molecular_function	hormone binding
A	0042802	molecular_function	identical protein binding
A	0044877	molecular_function	protein-containing complex binding
A	0070062	cellular_component	extracellular exosome
A	0140313	molecular_function	molecular sequestering activity
b	0001523	biological_process	retinoid metabolic process
b	0005179	molecular_function	hormone activity
b	0005515	molecular_function	protein binding
b	0005576	cellular_component	extracellular region
b	0005615	cellular_component	extracellular space
b	0005737	cellular_component	cytoplasm
b	0006144	biological_process	purine nucleobase metabolic process
b	0007165	biological_process	signal transduction
b	0032991	cellular_component	protein-containing complex
b	0035578	cellular_component	azurophil granule lumen
b	0042562	molecular_function	hormone binding
b	0042802	molecular_function	identical protein binding
b	0044877	molecular_function	protein-containing complex binding
b	0070062	cellular_component	extracellular exosome
b	0140313	molecular_function	molecular sequestering activity
e	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
b	LYS15-VAL30

---

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

Chain	Residue	Details
b	TYR105-SER117

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	25
Details	Peptide: {"description":"P3(42)","featureId":"PRO_0000000095"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	23
Details	Peptide: {"description":"P3(40)","featureId":"PRO_0000000096"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10413512","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11274207","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10413512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11274207","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26898943","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11274207","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26898943","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Cleavage; by ACE","evidences":[{"source":"PubMed","id":"11604391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16154999","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Cleavage; by alpha-secretase","evidences":[{"source":"PubMed","id":"11851430","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Site: {"description":"Cleavage; by theta-secretase","evidences":[{"source":"PubMed","id":"16816112","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Site: {"description":"Implicated in free radical propagation","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Site: {"description":"Susceptible to oxidation","evidences":[{"source":"PubMed","id":"10535332","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Site: {"description":"Cleavage; by gamma-secretase; site 1","evidences":[{"source":"PubMed","id":"11851430","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (HexNAc...) tyrosine; partial","evidences":[{"source":"PubMed","id":"22576872","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
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

---

site_id	SWS_FT_FI14
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

---

site_id	SWS_FT_FI15
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

---

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P02767","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
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

---