7VFI

Cryo-EM structure of the mouse TAPL (9mer-peptide bound)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005764	cellular_component	lysosome
A	0005765	cellular_component	lysosomal membrane
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006518	biological_process	peptide metabolic process
A	0015031	biological_process	protein transport
A	0015421	molecular_function	ABC-type oligopeptide transporter activity
A	0015440	molecular_function	ABC-type peptide transporter activity
A	0015833	biological_process	peptide transport
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0022857	molecular_function	transmembrane transporter activity
A	0035672	biological_process	oligopeptide transmembrane transport
A	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
A	0042803	molecular_function	protein homodimerization activity
A	0055085	biological_process	transmembrane transport
A	0140359	molecular_function	ABC-type transporter activity
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005764	cellular_component	lysosome
B	0005765	cellular_component	lysosomal membrane
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006518	biological_process	peptide metabolic process
B	0015031	biological_process	protein transport
B	0015421	molecular_function	ABC-type oligopeptide transporter activity
B	0015440	molecular_function	ABC-type peptide transporter activity
B	0015833	biological_process	peptide transport
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0022857	molecular_function	transmembrane transporter activity
B	0035672	biological_process	oligopeptide transmembrane transport
B	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
B	0042803	molecular_function	protein homodimerization activity
B	0055085	biological_process	transmembrane transport
B	0140359	molecular_function	ABC-type transporter activity

Functional Information from PROSITE/UniProt

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRVAMARAL

Chain	Residue	Details
A	LEU639-LEU653

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	160
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	566
Details	Domain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	472
Details	Domain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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