3JC2

The structure of the mammalian Sec61 channel opened by a signal sequence

Functional Information from GO Data

Chain	GOid	namespace	contents
1	0005048	molecular_function	signal sequence binding
1	0005784	cellular_component	Sec61 translocon complex
1	0005789	cellular_component	endoplasmic reticulum membrane
1	0006613	biological_process	cotranslational protein targeting to membrane
1	0006616	biological_process	SRP-dependent cotranslational protein targeting to membrane, translocation
1	0008320	molecular_function	protein transmembrane transporter activity
1	0015031	biological_process	protein transport
1	0016020	cellular_component	membrane
1	0031204	biological_process	post-translational protein targeting to membrane, translocation
1	0039019	biological_process	pronephric nephron development
1	0043022	molecular_function	ribosome binding
1	0045047	biological_process	protein targeting to ER
1	0045048	biological_process	protein insertion into ER membrane
2	0005543	molecular_function	phospholipid binding
2	0005789	cellular_component	endoplasmic reticulum membrane
2	0006605	biological_process	protein targeting
2	0006886	biological_process	intracellular protein transport
2	0008320	molecular_function	protein transmembrane transporter activity
2	0015031	biological_process	protein transport
2	0016020	cellular_component	membrane
2	0022406	biological_process	membrane docking
2	0031204	biological_process	post-translational protein targeting to membrane, translocation
2	0043022	molecular_function	ribosome binding
2	0045047	biological_process	protein targeting to ER
2	0071261	cellular_component	Ssh1 translocon complex

Functional Information from PROSITE/UniProt

site_id	PS00755
Number of Residues	20
Details	SECY_1 Protein secY signature 1. TLMeLGIsPIVtSGLIMQLL

Chain	Residue	Details
1	THR75-LEU94

---

site_id	PS00756
Number of Residues	19
Details	SECY_2 Protein secY signature 2. LLdElLQkgyGLGSGiSLF

Chain	Residue	Details
1	LEU164-PHE182

---

site_id	PS01067
Number of Residues	29
Details	SECE_SEC61G Protein secE/sec61-gamma signature. FvKDsIrlVkRctKPdrkEfqkiaMATAI

Chain	Residue	Details
2	PHE14-ILE42

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	204
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	85
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	49
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60059","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---