PDK1L_MOUSE
ID PDK1L_MOUSE Reviewed; 341 AA.
AC Q8QZR7; A2A9L0; Q3URF0; Q8BKB3;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Serine/threonine-protein kinase PDIK1L;
DE EC=2.7.11.1;
DE AltName: Full=PDLIM1-interacting kinase 1-like;
GN Name=Pdik1l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Brain cortex, Eye, Hippocampus, Spinal ganglion, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
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=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AK053750; BAC35506.1; -; mRNA.
DR EMBL; AK139413; BAE24001.1; -; mRNA.
DR EMBL; AK141566; BAE24738.1; -; mRNA.
DR EMBL; AK141823; BAE24845.1; -; mRNA.
DR EMBL; AK157013; BAE33930.1; -; mRNA.
DR EMBL; AK164975; BAE37986.1; -; mRNA.
DR EMBL; AL627314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027088; AAH27088.1; -; mRNA.
DR EMBL; BC058514; AAH58514.1; -; mRNA.
DR CCDS; CCDS18768.1; -.
DR RefSeq; NP_001157266.1; NM_001163794.1.
DR RefSeq; NP_666268.1; NM_146156.3.
DR AlphaFoldDB; Q8QZR7; -.
DR SMR; Q8QZR7; -.
DR STRING; 10090.ENSMUSP00000060381; -.
DR iPTMnet; Q8QZR7; -.
DR PhosphoSitePlus; Q8QZR7; -.
DR MaxQB; Q8QZR7; -.
DR PaxDb; Q8QZR7; -.
DR PRIDE; Q8QZR7; -.
DR ProteomicsDB; 289335; -.
DR Antibodypedia; 30559; 140 antibodies from 23 providers.
DR DNASU; 230809; -.
DR Ensembl; ENSMUST00000061234; ENSMUSP00000060381; ENSMUSG00000050890.
DR Ensembl; ENSMUST00000105876; ENSMUSP00000101502; ENSMUSG00000050890.
DR GeneID; 230809; -.
DR KEGG; mmu:230809; -.
DR UCSC; uc008vep.2; mouse.
DR CTD; 149420; -.
DR MGI; MGI:2385213; Pdik1l.
DR VEuPathDB; HostDB:ENSMUSG00000050890; -.
DR eggNOG; KOG0595; Eukaryota.
DR GeneTree; ENSGT00940000158412; -.
DR HOGENOM; CLU_026714_0_0_1; -.
DR InParanoid; Q8QZR7; -.
DR OMA; SMNARMK; -.
DR OrthoDB; 813266at2759; -.
DR TreeFam; TF105336; -.
DR BioGRID-ORCS; 230809; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Pdik1l; mouse.
DR PRO; PR:Q8QZR7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8QZR7; protein.
DR Bgee; ENSMUSG00000050890; Expressed in rostral migratory stream and 245 other tissues.
DR ExpressionAtlas; Q8QZR7; baseline and differential.
DR Genevisible; Q8QZR7; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..341
FT /note="Serine/threonine-protein kinase PDIK1L"
FT /id="PRO_0000086495"
FT DOMAIN 8..334
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 14..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 96..100
FT /note="LVETS -> VCVTA (in Ref. 1; BAC35506)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="Q -> P (in Ref. 1; BAE24738)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 38550 MW; DEBB705C8F9394E6 CRC64;
MVSSQPKYDL IREVGRGSYG VVYEAVIRKT SARVAVKKIR CHAPENVELA LREFWALSSI
KSQHPNVIHL EECILQKDGM VQKMSHGSNS SLYLQLVETS LKGEIAFDPR SAYYLWFVMD
FCDGGDMNEY LLSRKPNRKT NTSFMLQLSS ALAFLHKNQI IHRDLKPDNI LISQSRMDTS
DLEPTLKVAD FGLSKVCSAS GQNPEEPVSV NKCFLSTACG TDFYMAPEVW EGHYTAKADI
FALGIIIWAM LERITFIDTE TKKELLGSYV KQGTEIVPVG EALLENPKME LLIPVKKKSM
NGRMKQLIKE MLAANPQDRP DAFELELRLV QIAFKDSSWE T
