NUAK2_PONAB
ID NUAK2_PONAB Reviewed; 628 AA.
AC Q5R7G9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=NUAK family SNF1-like kinase 2;
DE EC=2.7.11.1;
GN Name=NUAK2 {ECO:0000250|UniProtKB:Q9H093};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAH92291.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:CAH92291.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Stress-activated kinase involved in tolerance to glucose
CC starvation. Induces cell-cell detachment by increasing F-actin
CC conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via
CC NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required
CC for the increased motility and invasiveness of CD95-activated tumor
CC cells. Phosphorylates LATS1 and LATS2. Plays a key role in neural tube
CC closure during embryonic development through LATS2 phosphorylation and
CC regulation of the nuclear localization of YAP1 a critical downstream
CC regulatory target in the Hippo signaling pathway.
CC {ECO:0000250|UniProtKB:Q9H093}.
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 Evidence={ECO:0000250|UniProtKB:Q9H093};
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; Evidence={ECO:0000250|UniProtKB:Q9H093};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9H093};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-208.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-
CC related adapter-alpha (STRADA) pseudo kinase and CAB39.
CC Autophosphorylation is also possible at Thr-208.
CC {ECO:0000250|UniProtKB:Q9H093}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR860148; CAH92291.1; -; mRNA.
DR RefSeq; NP_001126340.1; NM_001132868.2.
DR AlphaFoldDB; Q5R7G9; -.
DR SMR; Q5R7G9; -.
DR STRING; 9601.ENSPPYP00000000331; -.
DR Ensembl; ENSPPYT00000000348; ENSPPYP00000000331; ENSPPYG00000000307.
DR GeneID; 100173321; -.
DR KEGG; pon:100173321; -.
DR CTD; 81788; -.
DR eggNOG; KOG0611; Eukaryota.
DR GeneTree; ENSGT00940000158422; -.
DR HOGENOM; CLU_000288_63_42_1; -.
DR InParanoid; Q5R7G9; -.
DR OrthoDB; 1127668at2759; -.
DR TreeFam; TF324572; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0035330; P:regulation of hippo signaling; ISS:UniProtKB.
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 Acetylation; Apoptosis; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..628
FT /note="NUAK family SNF1-like kinase 2"
FT /id="PRO_0000247758"
FT DOMAIN 53..303
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 355..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O60285,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 59..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O60285,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H093,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H093"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H093"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H093"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H093"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H093"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H093"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZN4"
SQ SEQUENCE 628 AA; 69624 MW; 5C0DEFFBF7BF5C21 CRC64;
MESLVFARRS GPTPSAAELA RPLAEGLIKS PKPLMKKQAV KRHHHKHNLR HRYEFLETLG
KGTYGKVKKA RESSGRLVAI KSIRKDKIKD EQDLMHIRRE IEIMSSLNHP HIIAIHEVFE
NSSKIVIVME YASRGDLYDY ISERQQLSER EARHFFRQIV SAVHYCHQNR VVHRDLKLEN
ILLDANGNIK IADFGLSNLY HQGKFLQTFC GSPLYASPEI VNGKPYTGPE VDSWSLGVLL
YILVHGTMPF DGHDHKILVK QISNGAYREP PKPSDACGLI RWLLMVNPTR RATLEDVASH
WWVNWGYATR VGEQEAPHEG GHPGSDSARA SMADWLRRSS RPLLENGAKV CSFFKQHAPG
GGSTTPGLER QHSLKKSRKE NDMAQSLHSD TADDTAHRPG KSNLKLPKGI LKKKVSASAE
GAQEDPPELS PIPVSPGQAA PPLPKKGILK KPRQRESGYY SSPEPSESGE LLDVGDVFVS
GDPKEQKPPQ ASGLLLHRKG ILKLNGKFSQ TALELAAPTT FGSLDELAPP RPLARASRPS
GAVSEDSILS SESFDQLDLP ERLPEPPLRG CVSVDNLTGL EEPPSEGPGS CLRRWRQDPL
GDSCFSLTDC QEVTATYRQA LRVCSKLT
