Q6RW13 · ATRAP_HUMAN
- ProteinType-1 angiotensin II receptor-associated protein
- GeneAGTRAP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids159 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Appears to be a negative regulator of type-1 angiotensin II receptor-mediated signaling by regulating receptor internalization as well as mechanism of receptor desensitization such as phosphorylation. Induces also a decrease in cell proliferation and angiotensin II-stimulated transcriptional activity.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cell cortex | |
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | plasma membrane | |
Molecular Function | angiotensin type II receptor activity | |
Molecular Function | identical protein binding | |
Biological Process | regulation of blood pressure | |
Biological Process | response to hypoxia |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameType-1 angiotensin II receptor-associated protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6RW13
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Golgi apparatus membrane ; Multi-pass membrane protein
Cytoplasmic vesicle membrane ; Multi-pass membrane protein
Note: Present in perinuclear vesicular membranes, Endoplasmic reticulum, Golgi and endocytic vesicles.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-23 | Extracellular | ||||
Sequence: MELPAVNLKVILLGHWLLTTWGC | ||||||
Transmembrane | 24-44 | Helical | ||||
Sequence: IVFSGSYAWANFTILALGVWA | ||||||
Topological domain | 45-55 | Cytoplasmic | ||||
Sequence: VAQRDSIDAIS | ||||||
Transmembrane | 56-76 | Helical | ||||
Sequence: MFLGGLLATIFLDIVHISIFY | ||||||
Topological domain | 77-86 | Extracellular | ||||
Sequence: PRVSLTDTGR | ||||||
Transmembrane | 87-107 | Helical | ||||
Sequence: FGVGMAILSLLLKPLSCCFVY | ||||||
Topological domain | 108-159 | Cytoplasmic | ||||
Sequence: HMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPADPFAVPEGRSQDARGY |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_023075 | 143 | in dbSNP:rs17875960 | |||
Sequence: A → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 186 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000064735 | 1-159 | UniProt | Type-1 angiotensin II receptor-associated protein | |||
Sequence: MELPAVNLKVILLGHWLLTTWGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGLLATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLSCCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPADPFAVPEGRSQDARGY | |||||||
Modified residue | 126 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 127 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 127 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 131 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 133 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 135 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 138 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 153 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 153 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous but more abundant in kidney, heart, pancreas and thyroid.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with RACK1, and with the C-terminal region of AGTR1.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 110-122 | Interaction with AGTR1 | ||||
Sequence: YRERGGELLVHTG | ||||||
Region | 140-159 | Disordered | ||||
Sequence: EAPADPFAVPEGRSQDARGY |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q6RW13-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length159
- Mass (Da)17,419
- Last updated2004-07-05 v1
- Checksum7E1D5C7E79AE6BC5
Q6RW13-2
- Name2
- Differences from canonical
- 115-121: Missing
Q6RW13-3
- Name3
- Differences from canonical
- 21-159: WGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGLLATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLSCCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPADPFAVPEGRSQDARGY → CFWRHFSAKPRLETIELTCALCKLRSAAHRATAGLHCILRLLCLGQLHHPGLGRVGCGSAGLHRRHKHVSGWLAGHHLPGHRAHQHLLPAGQPHGHGPLWRGHGHPQLAAQAALLLLRLPHVPGARG
Q6RW13-5
- Name5
- Differences from canonical
- 21-159: WGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGLLATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLSCCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPADPFAVPEGRSQDARGY → CFWRHFSAKPRLETIELTCALCKLRSAAHRATAGLHCILRLLCLGQLHHPGLGRVGCGSAGLHRRHKHVSGWLAGHHLPGHRAHQHLLPAGQPHGHGPLWRGHGHPQLAAQAALLLLRLPHVPGARGFPWVFSGP
Q6RW13-4
- Name4
- Differences from canonical
- 10-159: VILLGHWLLTTWGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGLLATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLSCCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPADPFAVPEGRSQDARGY → GLHCILRLLCLGQLHHPGLGRVGCGSAGLHRRHKHVSGWLAGHHLPGHRAHQHLLPAGQPHGHGPLWRGHGHPQLAAQAALLLLRLPHVPGARGFPWVFSGP
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_039291 | 10-159 | in isoform 4 | |||
Sequence: VILLGHWLLTTWGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGLLATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLSCCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPADPFAVPEGRSQDARGY → GLHCILRLLCLGQLHHPGLGRVGCGSAGLHRRHKHVSGWLAGHHLPGHRAHQHLLPAGQPHGHGPLWRGHGHPQLAAQAALLLLRLPHVPGARGFPWVFSGP | ||||||
Alternative sequence | VSP_039290 | 21-159 | in isoform 3 | |||
Sequence: WGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGLLATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLSCCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPADPFAVPEGRSQDARGY → CFWRHFSAKPRLETIELTCALCKLRSAAHRATAGLHCILRLLCLGQLHHPGLGRVGCGSAGLHRRHKHVSGWLAGHHLPGHRAHQHLLPAGQPHGHGPLWRGHGHPQLAAQAALLLLRLPHVPGARG | ||||||
Alternative sequence | VSP_040406 | 21-159 | in isoform 5 | |||
Sequence: WGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGLLATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLSCCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPADPFAVPEGRSQDARGY → CFWRHFSAKPRLETIELTCALCKLRSAAHRATAGLHCILRLLCLGQLHHPGLGRVGCGSAGLHRRHKHVSGWLAGHHLPGHRAHQHLLPAGQPHGHGPLWRGHGHPQLAAQAALLLLRLPHVPGARGFPWVFSGP | ||||||
Alternative sequence | VSP_014839 | 115-121 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 158 | in Ref. 2; AAF89547 | ||||
Sequence: G → R | ||||||
Sequence conflict | 159 | in Ref. 1; AAL26806 | ||||
Sequence: Y → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF312374 EMBL· GenBank· DDBJ | AAL26806.1 EMBL· GenBank· DDBJ | mRNA | ||
AF165187 EMBL· GenBank· DDBJ | AAF89547.1 EMBL· GenBank· DDBJ | mRNA | ||
CA866314 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AY488088 EMBL· GenBank· DDBJ | AAR25556.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL953897 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471130 EMBL· GenBank· DDBJ | EAW71702.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC017328 EMBL· GenBank· DDBJ | AAH17328.1 EMBL· GenBank· DDBJ | mRNA | ||
BE782705 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |