UniProt ID | CRFR1_RAT | |
---|---|---|
UniProt AC | P35353 | |
Protein Name | Corticotropin-releasing factor receptor 1 | |
Gene Name | Crhr1 | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 415 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein. Endosome. Agonist-binding promotes endocytosis.. |
|
Protein Description | G-protein coupled receptor for CRH (corticotropin-releasing factor) and UCN (urocortin). Has high affinity for CRH and UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels. Inhibits the activity of the calcium channel CACNA1H. Required for normal embryonic development of the adrenal gland and for normal hormonal responses to stress. Plays a role in the response to anxiogenic stimuli.. | |
Protein Sequence | MGRRPQLRLVKALLLLGLNPVSTSLQDQRCENLSLTSNVSGLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVRYNTTNNGYRECLANGSWAARVNYSECQEILNEEKKSKVHYHVAVIINYLGHCISLVALLVAFVLFLRLRSIRCLRNIIHWNLISAFILRNATWFVVQLTVSPEVHQSNVAWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTYSTDRLRKWMFVCIGWGVPFPIIVAWAIGKLHYDNEKCWFGKRPGVYTDYIYQGPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDEVSRVVFIYFNSFLESFQGFFVSVFYCFLNSEVRSAIRKRWRRWQDKHSIRARVARAMSIPTSPTRVSFHSIKQSTAV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
38 | N-linked_Glycosylation | ENLSLTSNVSGLQCN CCCCCCCCCCCCCCC | 27.09 | 11567096 | |
45 | N-linked_Glycosylation | NVSGLQCNASVDLIG CCCCCCCCCEEEEEE | 23.45 | 11567096 | |
78 | N-linked_Glycosylation | FFYGVRYNTTNNGYR CEEEEEEECCCCCHH | 29.84 | 11567096 | |
90 | N-linked_Glycosylation | GYRECLANGSWAARV CHHHHHHCCCEEEEE | 31.89 | 11567096 | |
98 | N-linked_Glycosylation | GSWAARVNYSECQEI CCEEEEECHHHHHHH | 29.12 | 11567096 | |
301 | Phosphorylation | LMTKLRASTTSETIQ HHHHHHCCCCHHHHH | 26.28 | - | |
396 | Phosphorylation | ARVARAMSIPTSPTR HHHHHHHCCCCCCCE | 25.16 | 28432305 | |
399 | Phosphorylation | ARAMSIPTSPTRVSF HHHHCCCCCCCEEEE | 45.74 | 28432305 | |
400 | Phosphorylation | RAMSIPTSPTRVSFH HHHCCCCCCCEEEEE | 20.94 | 28432305 | |
402 | Phosphorylation | MSIPTSPTRVSFHSI HCCCCCCCEEEEECC | 43.39 | 28432305 | |
405 | Phosphorylation | PTSPTRVSFHSIKQS CCCCCEEEEECCCCC | 17.60 | 28432305 | |
408 | Phosphorylation | PTRVSFHSIKQSTAV CCEEEEECCCCCCCC | 29.48 | 17913459 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
301 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
301 | S | Phosphorylation |
| - |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CRFR1_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of CRFR1_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Functional and protein chemical characterization of the N-terminaldomain of the rat corticotropin-releasing factor receptor 1."; Hofmann B.A., Sydow S., Jahn O., van Werven L., Liepold T., Eckart K.,Spiess J.; Protein Sci. 10:2050-2062(2001). Cited for: DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-38; ASN-45; ASN-78; ASN-90AND ASN-98. |