Identification |
BMDB Protein ID
| BMDBP01179 |
Secondary Accession Numbers
| |
Name
| cGMP-dependent protein kinase 1 |
Synonyms
|
Not Available
|
Gene Name
| PRKG1 |
Protein Type
| Enzyme |
Biological Properties |
General Function
| Involved in ATP binding |
Specific Function
| Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle (By similarity). |
Pathways
|
- Ion Channels and Their Functional Role in Vascular Endothelium
|
Reactions
| Not Available |
GO Classification
|
Not Available
|
Cellular Location
|
Not Available
|
Gene Properties |
Chromosome Location
| 26 |
Locus
| Not Available |
SNPs
| PRKG1 |
Gene Sequence
|
>2016 bp
ATGAGCGAGCTGGAGGAAGACTTTGCCAAGATTCTCATGCTCAAGGAGGAGAGGATCAAA
GAGCTGGAGAAGCGGCTGTCAGAGAAGGAGGAAGAAATCCAGGAGCTGAAGAGGAAACTC
CATAAATGCCAGTCAGTGCTGCCCGTGCCCTCGACCCACATCGGCCCCCGGACCACCCGG
GCACAGGGCATCTCGGCCGAGCCGCAGACCTACAGGTCCTTCCACGACCTCCGACAGGCA
TTCCGGAAGTTCACCAAATCCGAAAGGTCCAAGGATCTCATAAAGGAGGCCATCCTTGAC
AATGACTTTATGAAGAACTTGGAGCTGTCACAGATCCAAGAGATTGTGGATTGTATGTAC
CCAGTGGAGTACGGCAAAGACAGCTGCATCATCAAAGAAGGAGATGTGGGGTCACTGGTG
TATGTCATGGAAGATGGTAAGGTTGAAGTTACAAAAGAAGGCGTGAAGCTGTGCACAATG
GGTCCTGGTAAAGTGTTTGGAGAGTTGGCTATCCTTTACAACTGTACCCGGACGGCGACC
GTCAAAACTCTTGTAAATGTGAAACTCTGGGCCATTGATCGACAATGTTTTCAGACGATA
ATGATGAGGACAGGACTTATCAAGCATACCGAGTATATGGAATTTTTAAAAAGCGTTCCA
ACATTCCAGAGCCTTCCTGAAGAGATCCTCAGTAAGCTTGCTGACGTCCTTGAAGAGACC
CACTATGAAAATGGGGAATATATCATCAGGCAAGGTGCAAGAGGGGACACCTTCTTTATC
ATCAGTAAAGGAAAGGTTAATGTCACTCGTGAAGACTCGCCCAATGAAGACCCAGTCTTT
CTTAGAACCTTAGGAAAAGGAGATTGGTTTGGAGAGAAAGCCTTGCAGGGGGAAGATGTG
AGAACAGCGAATGTAATTGCGGCAGAAGCTGTAACCTGCCTTGTGATCGACAGAGACTCT
TTCAAACATTTGATTGGAGGATTAGATGATGTTTCTAATAAAGCATATGAAGATGCAGAA
GCTAAGGCAAAATATGAAGCTGAAGCTGCTTTCTTCGCCAACCTGAAGCTGTCTGATTTC
AACATCATTGACACCCTTGGAGTTGGAGGTTTCGGACGCGTAGAACTGGTCCAGTTAAAA
AGTGAAGAATCCAAAACCTTTGCAATGAAGATTCTCAAGAAACGGCACATCGTGGATACA
AGACAGCAGGAACACATCCGCTCGGAGAAGCAGATCATGCAGGGGGCCCATTCGGACTTC
ATAGTGAGATTATACAGAACATTTAAGGACAGCAAATATTTGTATATGTTGATGGAAGCT
TGCCTAGGTGGAGAGCTCTGGACCATTCTCAGGGATCGGGGGTCATTTGAAGATTCTACA
ACCAGATTTTATACAGCATGTGTGGTAGAAGCTTTTGCCTATCTGCATTCCAAAGGAATC
ATTTACAGGGACCTCAAGCCTGAAAATCTCATCCTAGATCACCGAGGTTATGCCAAACTG
GTTGATTTTGGCTTTGCAAAGAAAATAGGATTTGGAAAGAAAACATGGACTTTTTGTGGG
ACTCCAGAATATGTAGCCCCAGAGATCATCCTGAACAAAGGCCATGACATTTCAGCCGAC
TATTGGTCACTGGGAATCCTCATGTATGAGCTTCTGACTGGCAGCCCACCTTTCTCAGGC
CCAGATCCTATGAAAACCTATAACATCATATTGAGGGGGATTGACATGATAGAGTTTCCA
AAGAAGATTGCCAAAAATGCTGCTAATTTAATTAAAAAACTATGCAGGGATAATCCATCA
GAAAGATTAGGGAATTTGAAAAACGGAGTGAAAGACATTCAAAAGCACAAATGGTTTGAG
GGCTTTAATTGGGAAGGCTTAAGAAAAGGCACCTTGACACCTCCTATAATACCAAGTGTT
GCATCACCCACAGACACAAGCAATTTTGACAGTTTCCCTGAGGACAATGATGAACCGCCA
CCTGATGACAACTCAGGATGGGACATAGACTTCTAA
|
Protein Properties |
Number of Residues
| 671 |
Molecular Weight
| 76419.0 |
Theoretical pI
| 5.99 |
Pfam Domain Function
|
Not Available |
Signals
|
|
Transmembrane Regions
|
Not Available
|
Protein Sequence
|
>cGMP-dependent protein kinase 1, alpha isozyme
MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTR
AQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMY
PVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTAT
VKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEET
HYENGEYIIRQGARGDTFFIISKGKVNVTREDSPNEDPVFLRTLGKGDWFGEKALQGEDV
RTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDF
NIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDF
IVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGI
IYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISAD
YWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPS
ERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDSFPEDNDEPP
PDDNSGWDIDF
|
External Links |
GenBank ID Protein
| CAA34214.1 |
UniProtKB/Swiss-Prot ID
| P00516 |
UniProtKB/Swiss-Prot Entry Name
| KGP1_BOVIN |
PDB IDs
|
|
GenBank Gene ID
| X16086 |
GeneCard ID
| PRKG1 |
GenAtlas ID
| Not Available |
HGNC ID
| Not Available |
References |
General References
| Not Available |