ID G1TXD8_RABIT Unreviewed; 870 AA.
AC G1TXD8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000552};
DE EC=2.7.11.13 {ECO:0000256|PIRNR:PIRNR000552};
GN Name=PRKD2 {ECO:0000313|Ensembl:ENSOCUP00000021739.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000021739.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000021739.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000021739.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000021739.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13; Evidence={ECO:0000256|PIRNR:PIRNR000552};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000552};
CC -!- ACTIVITY REGULATION: Activated by DAG and phorbol esters.
CC {ECO:0000256|PIRNR:PIRNR000552}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000552}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000256|ARBA:ARBA00008582}.
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DR AlphaFoldDB; G1TXD8; -.
DR SMR; G1TXD8; -.
DR STRING; 9986.ENSOCUP00000021739; -.
DR PaxDb; 9986-ENSOCUP00000021739; -.
DR Ensembl; ENSOCUT00000021630.3; ENSOCUP00000021739.2; ENSOCUG00000026784.3.
DR eggNOG; KOG4236; Eukaryota.
DR GeneTree; ENSGT00950000183024; -.
DR HOGENOM; CLU_009772_1_0_1; -.
DR InParanoid; G1TXD8; -.
DR TreeFam; TF314320; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000026784; Expressed in blood and 19 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
DR GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0070232; P:regulation of T cell apoptotic process; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR CDD; cd20840; C1_PKD2_rpt1; 1.
DR CDD; cd01239; PH_PKD; 1.
DR CDD; cd14082; STKc_PKD; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR PANTHER; PTHR22968:SF12; SERINE_THREONINE-PROTEIN KINASE D2; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000552; PKC_mu_nu_D2; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000552};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000552};
KW Kinase {ECO:0000256|PIRNR:PIRNR000552};
KW Magnesium {ECO:0000256|PIRNR:PIRNR000552};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000552};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000552};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000552};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000552};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 136..186
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 258..308
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 548..804
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 671
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-1"
FT BINDING 554..562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-2"
FT BINDING 577
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 870 AA; 95712 MW; ACCA68BAAFB58C96 CRC64;
MAAAPSHPAG LPGFPGPGSP PPPGGLDPQS PPPLLSAVPG PGVSFHIQIG LTREFVLLPA
ASELAHVKQL ACSIVDQKFP ECGFYGLYDK ILLFKHDPTS ANLLQLVRSA GDIQEGDLVE
VVLSASATFE DFQIRPHALT VHSYRAPAFC DHCGEMLFGL VRQGLKCDGC GLNYHKRCAF
SIPNNCSGAR KRRLSSTSLA SGHSVRLGSS ESLPCTAEEL SRSTTDLLPR RPPSSSASFY
TGRPIELDKM LLSKVKVPHT FLVHSYTRPT VCQACKKLLK GLFRQGLQCK DCKFNCHKRC
ASRVPNECLG EALLNGDVPM EEATDFSEAD KSALAEEPDD AGVDSGVVPG SHSESALQAG
EEEEGEGGKA QSDSVFPSVK WEERMSPRTC QAGTSFYHGS SKNNERAKRH YWRLDCKCIT
LFQNDTTNRY YKWGCPEIPL SEILTVEPAQ NFSFVPPGTN PHCFEIITAN ATYFVGETPG
GAPGAPHGQG AETARGWETA IRQALMPVIL QDAASTPGHA PHRQASLSIS VSNSQIQENV
DIAAVYQIFP DEVLGSGQFG VVYGGKHRKT SRDVAVKVID KLRFPTKQES QLRNEVAILQ
SLRHPGIVNL ECMFETPEKV FVVMEKLHGD MLEMILSSEK GRLPERLTKF LITQILVALR
HLHFKNIVHC DLKPENVLLA SADPFPQVKL CDFGFARIIG EKSFRRSVVG TPAYLAPEVL
LNQGYNRSLD MWSVGVIMYV SLSGTFPFNE DEDINDQIQN AAFMYPASPW SCISAGAIDL
INNLLQVKMR KRYSVDKSLS HSWLQEYQTW LDLRELEGKM GERYITHESD DARWEQFVAE
QPLPGPGELG SAWVPQDHEM QGLAERVSVL
//
