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7EWP

Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:1:1 ratio

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0006091biological_processgeneration of precursor metabolites and energy
A0007186biological_processG protein-coupled receptor signaling pathway
A0008218biological_processbioluminescence
A0016020cellular_componentmembrane
B0004930molecular_functionG protein-coupled receptor activity
B0006091biological_processgeneration of precursor metabolites and energy
B0007186biological_processG protein-coupled receptor signaling pathway
B0008218biological_processbioluminescence
B0016020cellular_componentmembrane
C0001965molecular_functionG-protein alpha-subunit binding
C0001975biological_processresponse to amphetamine
C0003924molecular_functionGTPase activity
C0005096molecular_functionGTPase activator activity
C0005635cellular_componentnuclear envelope
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0007186biological_processG protein-coupled receptor signaling pathway
C0008277biological_processregulation of G protein-coupled receptor signaling pathway
C0009968biological_processnegative regulation of signal transduction
C0031681molecular_functionG-protein beta-subunit binding
C0032991cellular_componentprotein-containing complex
C0035556biological_processintracellular signal transduction
C0043005cellular_componentneuron projection
C0043547biological_processpositive regulation of GTPase activity
C0045471biological_processresponse to ethanol
C0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
C1901381biological_processpositive regulation of potassium ion transmembrane transport
D0003924molecular_functionGTPase activity
D0005096molecular_functionGTPase activator activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005834cellular_componentheterotrimeric G-protein complex
D0005886cellular_componentplasma membrane
D0007165biological_processsignal transduction
D0007186biological_processG protein-coupled receptor signaling pathway
D0007212biological_processG protein-coupled dopamine receptor signaling pathway
D0016020cellular_componentmembrane
D0030159molecular_functionsignaling receptor complex adaptor activity
D0031682molecular_functionG-protein gamma-subunit binding
D0036367biological_processlight adaption
D0043547biological_processpositive regulation of GTPase activity
D0051087molecular_functionprotein-folding chaperone binding
D0098793cellular_componentpresynapse
D1901386biological_processnegative regulation of voltage-gated calcium channel activity
D1902773cellular_componentGTPase activator complex
D1990603biological_processdark adaptation
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. IVSSsqDgKVIVWDS
ChainResidueDetails
DILE78-SER92
DILE168-VAL182
DLEU298-VAL312

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49803
ChainResidueDetails
CSER229
AVAL548-ASP576
ALEU634-TRP642
BALA24-ARG417
BVAL548-ASP576
BLEU634-TRP642

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O54829
ChainResidueDetails
CSER241
BLEU418-TYR439

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O54829
ChainResidueDetails
CTHR243
ALYS502-ARG525
ATYR598-ARG611
BHIS440-GLY451
BLYS502-ARG525
BTYR598-ARG611

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10862767
ChainResidueDetails
CSER434
BLEU452-PHE474

site_idSWS_FT_FI5
Number of Residues6
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0000305, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
AGLU475-THR478
BGLU475-THR478

site_idSWS_FT_FI6
Number of Residues44
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
APHE479-LEU501
BPHE479-LEU501

site_idSWS_FT_FI7
Number of Residues42
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
AVAL526-SER547
BVAL526-SER547

site_idSWS_FT_FI8
Number of Residues40
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
AARG577-CYS597
BARG577-CYS597

site_idSWS_FT_FI9
Number of Residues42
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
ATYR612-VAL633
BTYR612-VAL633

site_idSWS_FT_FI10
Number of Residues42
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
AMET643-ILE664
BMET643-ILE664

site_idSWS_FT_FI11
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:36996198
ChainResidueDetails
ASER172
AARG173
AGLU271
AASP307
BSER172
BARG173
BGLU271
BASP307

site_idSWS_FT_FI12
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8C419
ChainResidueDetails
ASER694
ASER705
ASER708
BSER694
BSER705
BSER708

site_idSWS_FT_FI13
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN98
BASN333
AASN143
AASN215
AASN274
AASN333
BASN98
BASN143
BASN215
BASN274

site_idSWS_FT_FI14
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18655026
ChainResidueDetails
ALYS774
BLYS774

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PDB entries from 2024-07-17

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