EKS-BOT-00165

Eukaryotic Protein Kinase & Protein Phosphatase Database

Tag

Content

EKPD ID

EKS-BOT-00165

Classification

Group/Family	Score	E-Value	Start	End	Domain Length
AGC/PKG	509.2	2.0E-153	361	619	259

Status

Reviewed

Ensembl Protein

ENSBTAP00000024490

UniProt Accession

P00516; P21136;

Protein Name

cGMP-dependent protein kinase 1

Protein Synonyms/Alias

cGK 1; cGK1; cGMP-dependent protein kinase I; cGKI;

Gene Name

PRKG1

Gene Synonyms/Alias

PRKG1; PRKG1B, PRKGR1A, PRKGR1B;

Ensembl Information

Ensembl Gene ID	Ensembl Protein ID	Ensembl Transcript ID
ENSBTAG00000018404	ENSBTAP00000024490	ENSBTAT00000024490
ENSBTAG00000018404	ENSBTAP00000030518	ENSBTAT00000030539

Organism

Bos taurus

Functional Description

Serine/threonine protein kinasethat acts as key mediatorof 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. Smoth 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).

Protein Length

671

Protein Sequence
(FASTA)

MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP STHIGPRTTR 60

AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD NDFMKNLELS QIQEIVDCMY 120

PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV TKEGVKLCTM GPGKVFGELA ILYNCTRTAT 180

VKTLVNVKLW AIDRQCFQTI MMRTGLIKHT EYMEFLKSVP TFQSLPEEIL SKLADVLEET 240

HYENGEYIIR QGARGDTFFI ISKGKVNVTR EDSPNEDPVF LRTLGKGDWF GEKALQGEDV 300

RTANVIAAEA VTCLVIDRDS FKHLIGGLDD VSNKAYEDAE AKAKYEAEAA FFANLKLSDF 360

NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT RQQEHIRSEK QIMQGAHSDF 420

IVRLYRTFKD SKYLYMLMEA CLGGELWTIL RDRGSFEDST TRFYTACVVE AFAYLHSKGI 480

IYRDLKPENL ILDHRGYAKL VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD 540

YWSLGILMYE LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS 600

ERLGNLKNGV KDIQKHKWFE GFNWEGLRKG TLTPPIIPSV ASPTDTSNFD SFPEDNDEPP 660

PDDNSGWDID F 671

Nucleotide Sequence
(FASTA)

ATGAGCGAGC TGGAGGAAGA CTTTGCCAAG ATTCTCATGC TCAAGGAGGA GAGGATCAAA 60

GAGCTGGAGA AGCGGCTGTC AGAGAAGGAG GAAGAAATCC AGGAGCTGAA GAGGAAACTC 120

CATAAATGCC AGTCAGTGCT GCCCGTGCCC TCGACCCACA TCGGCCCCCG GACCACCCGG 180

GCACAGGGCA TCTCGGCCGA GCCGCAGACC TACAGGTCCT TCCACGACCT CCGACAGGCA 240

TTCCGGAAGT TCACCAAATC CGAAAGGTCC AAGGATCTCA TAAAGGAGGC CATCCTTGAC 300

AATGACTTTA TGAAGAACTT GGAGCTGTCA CAGATCCAAG AGATTGTGGA TTGTATGTAC 360

CCAGTGGAGT ACGGCAAAGA CAGCTGCATC ATCAAAGAAG GAGATGTGGG GTCACTGGTG 420

TATGTCATGG AAGATGGTAA GGTTGAAGTT ACAAAAGAAG GCGTGAAGCT GTGCACAATG 480

GGTCCTGGTA AAGTGTTTGG AGAGTTGGCT ATCCTTTACA ACTGTACCCG GACGGCGACC 540

GTCAAAACTC TTGTAAATGT GAAACTCTGG GCCATTGATC GACAATGTTT TCAGACGATA 600

ATGATGAGGA CAGGACTTAT CAAGCATACC GAGTATATGG AATTTTTAAA AAGCGTTCCA 660

ACATTCCAGA GCCTTCCTGA AGAGATCCTC AGTAAGCTTG CTGACGTCCT TGAAGAGACC 720

CACTATGAAA ATGGGGAATA TATCATCAGG CAAGGTGCAA GAGGGGACAC CTTCTTTATC 780

ATCAGTAAAG GAAAGGTTAA TGTCACTCGT GAAGACTCGC CCAATGAAGA CCCAGTCTTT 840

CTTAGAACCT TAGGAAAAGG AGATTGGTTT GGAGAGAAAG CCTTGCAGGG GGAAGATGTG 900

AGAACAGCGA ATGTAATTGC GGCAGAAGCT GTAACCTGCC TTGTGATCGA CAGAGACTCT 960

TTCAAACATT TGATTGGAGG ATTAGATGAT GTTTCTAATA AAGCATATGA AGATGCAGAA 1020

GCTAAAGCAA AATATGAAGC TGAAGCTGCT TTCTTCGCCA ACCTGAAGCT GTCTGATTTC 1080

AACATCATTG ACACCCTTGG AGTTGGAGGT TTCGGACGAG TAGAACTGGT CCAGTTAAAA 1140

AGTGAAGAAT CCAAAACCTT TGCAATGAAG ATTCTCAAGA AACGCCACAT CGTGGATACA 1200

AGACAGCAGG AACACATCCG CTCGGAGAAG CAGATCATGC AGGGGGCCCA TTCGGACTTC 1260

ATAGTGAGAT TATACAGAAC ATTTAAGGAC AGCAAATATT TGTATATGTT GATGGAAGCT 1320

TGCCTAGGTG GAGAGCTCTG GACCATTCTC AGGGATCGGG GGTCATTTGA AGATTCTACA 1380

ACCAGATTTT ATACAGCATG TGTGGTAGAA GCTTTTGCCT ATCTGCATTC CAAAGGAATC 1440

ATTTACAGGG ACCTCAAGCC TGAAAATCTC ATCCTAGATC ACCGAGGTTA TGCCAAACTG 1500

GTTGATTTTG GCTTTGCAAA GAAAATAGGA TTTGGAAAGA AAACATGGAC TTTTTGTGGG 1560

ACTCCAGAAT ATGTAGCCCC AGAGATCATC CTGAACAAAG GCCATGACAT TTCAGCCGAC 1620

TATTGGTCAC TGGGAATCCT CATGTATGAG CTTCTGACTG GCAGCCCACC TTTCTCAGGC 1680

CCAGATCCTA TGAAAACCTA TAACATCATA TTGAGGGGGA TTGACATGAT AGAGTTTCCA 1740

AAGAAGATTG CCAAAAATGC TGCTAATTTA ATTAAAAAAC TATGCAGGGA TAATCCATCA 1800

GAAAGATTAG GGAATTTGAA AAACGGAGTG AAAGACATTC AAAAGCACAA ATGGTTTGAG 1860

GGCTTTAATT GGGAAGGCTT AAGAAAAGGC ACCTTGACAC CTCCTATAAT ACCAAGTGTT 1920

GCATCACCCA CAGACACAAG CAATTTTGAC AGTTTCCCTG AGGACAATGA CGAACCGCCA 1980

CCTGATGACA ACTCAGGATG GGACATAGAC TTCTAA 2016

Domain Profile

S: 2     kviatlgvggfgrvelvkvksdeskafalkilkkkhivdtkqqehvlsekrileeaksdf  61

         ++i+tlgvggfgrvelv++ks+esk+fa+kilkk+hivdt+qqeh++sek+i++ a+sdf

Q: 361   NIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDF  420

         79**********************************************************

S: 62    ivklyrtfkdekyvyllleaclggelwtilrdrgsfddktakfivacvvealeylhskni  121

         iv+lyrtfkd+ky+y+l+eaclggelwtilrdrgsf+d+t++f++acvvea++ylhsk+i

Q: 421   IVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGI  480

         ************************************************************

S: 122   iyrdlkpenllldeegylklvdfgfakklksgkktwtfcgtpeyvapeiilnkghdlsvd  181

         iyrdlkpenl+ld++gy+klvdfgfakk++ gkktwtfcgtpeyvapeiilnkghd+s+d

Q: 481   IYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISAD  540

         ************************************************************

S: 182   ywalgilvyelltgkppfsgvdplktynlilkgidklelprkitkeaedlikklcrdnpa  241

         yw+lgil+yelltg+ppfsg+dp+ktyn+il+gid++e+p+ki+k+a++likklcrdnp+

Q: 541   YWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPS  600

         ************************************************************

S: 242   erlgylkggikdikkhkwf  260

         erlg+lk+g+kdi+khkwf

Q: 601   ERLGNLKNGVKDIQKHKWF  619

         ******************9

Domain Sequence
(FASTA)

NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT RQQEHIRSEK QIMQGAHSDF 60

IVRLYRTFKD SKYLYMLMEA CLGGELWTIL RDRGSFEDST TRFYTACVVE AFAYLHSKGI 120

IYRDLKPENL ILDHRGYAKL VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD 180

YWSLGILMYE LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS 240

ERLGNLKNGV KDIQKHKWF 259

Keyword

3D-structure; Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding; cGMP; cGMP-binding; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase.

Sequence Source

Ensembl

Orthology

Ortholog group

Ailuropoda melanoleuca"; ?>Caenorhabditis elegans"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Choloepus hoffmanni"; ?>Ciona intestinalis"; ?>Ciona savignyi"; ?>Danio rerio"; ?>Drosophila melanogaster"; ?>Equus caballus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Tursiops truncatus"; ?>Vicugna pacos"; ?>Xiphophorus maculatus"; ?>

Gene Ontology

GO:0005829	; C:cytosol
GO:0005524	; F:ATP binding
GO:0005246	; F:calcium channel regulator activity
GO:0030553	; F:cGMP binding
GO:0004692	; F:cGMP-dependent protein kinase activity
GO:0090331	; P:negative regulation of platelet aggregation
GO:0043087	; P:regulation of GTPase activity

KEGG

bta:282004

;

InterPros

IPR000961	; AGC-kinase_C.
IPR016232	; cGMP-dependent_protein_kinase.
IPR002374	; cGMP_dep_kinase.
IPR018490	; cNMP-bd-like.
IPR018488	; cNMP-bd_CS.
IPR000595	; cNMP-bd_dom.
IPR011009	; Kinase-like_dom.
IPR000719	; Prot_kinase_cat_dom.
IPR017441	; Protein_kinase_ATP_BS.
IPR014710	; RmlC-like_jellyroll.
IPR002290	; Ser/Thr_dual-sp_kinase_dom.
IPR008271	; Ser/Thr_kinase_AS.

Pfam

PF00027	; cNMP_binding; 2.
PF00069	; Pkinase; 1.

SMARTs

SM00100	; cNMP; 2.
SM00133	; S_TK_X; 1.
SM00220	; S_TKc; 1.

Prosites

PS51285	; AGC_KINASE_CTER; 1.
PS00888	; CNMP_BINDING_1; 2.
PS00889	; CNMP_BINDING_2; 2.
PS50042	; CNMP_BINDING_3; 2.
PS00107	; PROTEIN_KINASE_ATP; 1.
PS50011	; PROTEIN_KINASE_DOM; 1.
PS00108	; PROTEIN_KINASE_ST; 1.

Prints

PR00104

; CGMPKINASE.

Created Date

20-Feb-2013