2KR6

Solution structure of presenilin-1 CTF subunit

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016020	cellular_component	membrane
A	0016485	biological_process	protein processing
A	0042500	molecular_function	aspartic endopeptidase activity, intramembrane cleaving

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	TRANSMEM: Helical => ECO:0000269|PubMed:26280335

Chain	Residue	Details
A	LEU381-SER401
A	ILE408-PHE428
A	PRO433-VAL453

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site_id	SWS_FT_FI2
Number of Residues	18
Details	TOPO_DOM: Lumenal => ECO:0000269|PubMed:26280335

Chain	Residue	Details
A	GLY402-THR407
A	GLN454-ILE467

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site_id	SWS_FT_FI3
Number of Residues	3
Details	TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:26280335

Chain	Residue	Details
A	LYS429-LEU432

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site_id	SWS_FT_FI4
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:10206644, ECO:0000305|PubMed:10899933, ECO:0000305|PubMed:15341515, ECO:0000305|PubMed:30598546, ECO:0000305|PubMed:30630874

Chain	Residue	Details
A	ASP385

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site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Cleavage; alternate => ECO:0000269|PubMed:9173929

Chain	Residue	Details
A	MET292

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Cleavage => ECO:0000269|PubMed:9173929

Chain	Residue	Details
A	MET298

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site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Cleavage; by caspase => ECO:0000269|PubMed:9485372

Chain	Residue	Details
A	ASP345

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:14576165

Chain	Residue	Details
A	SER310

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site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:14576165

Chain	Residue	Details
A	SER346

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site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER367

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