8DO1

Cryo-EM structure of the human Sec61 complex inhibited by ipomoeassin F

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005048	molecular_function	signal sequence binding
A	0005262	molecular_function	calcium channel activity
A	0005515	molecular_function	protein binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005784	cellular_component	Sec61 translocon complex
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006613	biological_process	cotranslational protein targeting to membrane
A	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
A	0006616	biological_process	SRP-dependent cotranslational protein targeting to membrane, translocation
A	0006620	biological_process	post-translational protein targeting to endoplasmic reticulum membrane
A	0007029	biological_process	endoplasmic reticulum organization
A	0008320	molecular_function	protein transmembrane transporter activity
A	0015031	biological_process	protein transport
A	0016020	cellular_component	membrane
A	0031204	biological_process	post-translational protein targeting to membrane, translocation
A	0034341	biological_process	response to type II interferon
A	0039019	biological_process	pronephric nephron development
A	0043022	molecular_function	ribosome binding
A	0045047	biological_process	protein targeting to ER
A	0045048	biological_process	protein insertion into ER membrane
A	0070588	biological_process	calcium ion transmembrane transport
B	0005515	molecular_function	protein binding
B	0005783	cellular_component	endoplasmic reticulum
B	0005784	cellular_component	Sec61 translocon complex
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005829	cellular_component	cytosol
B	0006605	biological_process	protein targeting
B	0006886	biological_process	intracellular protein transport
B	0008320	molecular_function	protein transmembrane transporter activity
B	0015031	biological_process	protein transport
B	0016020	cellular_component	membrane
B	0031204	biological_process	post-translational protein targeting to membrane, translocation
B	0043022	molecular_function	ribosome binding
B	0045047	biological_process	protein targeting to ER
B	0071261	cellular_component	Ssh1 translocon complex
C	0003723	molecular_function	RNA binding
C	0005085	molecular_function	guanyl-nucleotide exchange factor activity
C	0005515	molecular_function	protein binding
C	0005783	cellular_component	endoplasmic reticulum
C	0005784	cellular_component	Sec61 translocon complex
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0005829	cellular_component	cytosol
C	0006616	biological_process	SRP-dependent cotranslational protein targeting to membrane, translocation
C	0006886	biological_process	intracellular protein transport
C	0015031	biological_process	protein transport
C	0016020	cellular_component	membrane
C	0030970	biological_process	retrograde protein transport, ER to cytosol
C	0031204	biological_process	post-translational protein targeting to membrane, translocation
C	0031205	cellular_component	endoplasmic reticulum Sec complex
C	0036503	biological_process	ERAD pathway
C	0043022	molecular_function	ribosome binding
C	0044322	cellular_component	endoplasmic reticulum quality control compartment
C	0048408	molecular_function	epidermal growth factor binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR75-LEU94

---

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

Chain	Residue	Details
A	LEU164-PHE182

---

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

Chain	Residue	Details
B	PHE14-ILE42

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	242
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	76
Details	Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	96
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---