TLK2_DANRE
ID TLK2_DANRE Reviewed; 697 AA.
AC Q1ECX4; A8WGJ6; Q90ZY7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Serine/threonine-protein kinase tousled-like 2 {ECO:0000250|UniProtKB:Q86UE8};
DE EC=2.7.11.1;
DE AltName: Full=PKU-alpha {ECO:0000312|EMBL:AAK52417.1};
DE AltName: Full=Tousled-like kinase 2 {ECO:0000312|ZFIN:ZDB-GENE-060623-36};
GN Name=tlk2 {ECO:0000312|ZFIN:ZDB-GENE-060623-36}; ORFNames=zgc:136697;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK52417.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Chou C.-M., Lee I.-L., Leu J.-H., Huang C.-J.;
RT "The zebrafish homolog of the human pKU-alpha protein kinase.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK52417.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=AB {ECO:0000312|EMBL:AAI54738.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Negative regulator of amino acid starvation-induced
CC autophagy. {ECO:0000250}.
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:Q86UE8};
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:Q86UE8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q86UE8};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86UE8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|Ref.1};
CC IsoId=Q1ECX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1ECX4-2; Sequence=VSP_053052;
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; AF265344; AAK52417.1; -; mRNA.
DR EMBL; BC117634; AAI17635.1; -; mRNA.
DR EMBL; BC154737; AAI54738.1; -; mRNA.
DR EMBL; BC171502; AAI71502.1; -; mRNA.
DR RefSeq; NP_001103887.1; NM_001110417.1.
DR RefSeq; XP_005163931.1; XM_005163874.3.
DR AlphaFoldDB; Q1ECX4; -.
DR SMR; Q1ECX4; -.
DR STRING; 7955.ENSDARP00000003372; -.
DR PaxDb; Q1ECX4; -.
DR PRIDE; Q1ECX4; -.
DR Ensembl; ENSDART00000006490; ENSDARP00000003372; ENSDARG00000010779. [Q1ECX4-1]
DR Ensembl; ENSDART00000141937; ENSDARP00000114778; ENSDARG00000010779. [Q1ECX4-1]
DR GeneID; 407732; -.
DR KEGG; dre:407732; -.
DR CTD; 11011; -.
DR ZFIN; ZDB-GENE-060623-36; tlk2.
DR eggNOG; KOG1151; Eukaryota.
DR GeneTree; ENSGT00950000182984; -.
DR HOGENOM; CLU_000288_85_1_1; -.
DR InParanoid; Q1ECX4; -.
DR OMA; NERWAVN; -.
DR OrthoDB; 693214at2759; -.
DR PhylomeDB; Q1ECX4; -.
DR TreeFam; TF315233; -.
DR PRO; PR:Q1ECX4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000010779; Expressed in early embryo and 28 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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 InterPro; IPR027086; TLK2.
DR PANTHER; PTHR22974:SF20; PTHR22974:SF20; 2.
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 Alternative splicing; ATP-binding; Coiled coil; Kinase; Nucleotide-binding;
KW Nucleus; Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..697
FT /note="Serine/threonine-protein kinase tousled-like 2"
FT /id="PRO_0000367033"
FT DOMAIN 388..666
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 25..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 265..294
FT /evidence="ECO:0000255"
FT COILED 336..373
FT /evidence="ECO:0000255"
FT COMPBIAS 28..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 518
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 394..402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 345
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_053052"
FT CONFLICT 40
FT /note="C -> R (in Ref. 1; AAK52417)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="S -> N (in Ref. 1; AAK52417)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="K -> M (in Ref. 1; AAK52417)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="W -> R (in Ref. 1; AAK52417 and 2; AAI54738)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="I -> M (in Ref. 1; AAK52417 and 2; AAI54738)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="E -> G (in Ref. 1; AAK52417)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="L -> P (in Ref. 1; AAK52417)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 697 AA; 79305 MW; 907B93FFE169E2E4 CRC64;
MMEELHSLDP RRQELLEARF TGVGVAKGSG HNESSNQSLC SVGSLSDKEL ETPEKKSNDQ
RTRKRKGDPF DSQGKGGGRG HKISDYFEFA GGSGTGTSPA RGIPPVARSS PQHSLSNPPA
AVQQGSPSSI SSVNTDHSHT STSHKPASIH TQHRASQSEL TMEKLAALES SKSSDLEKKE
GRIDDLLRVN CDLRRQIDEQ QKMLEWCKER LNKCVTMSKK LLIEKSKQEK IACREKSMQD
RLRLGHFTTV RHGASFTEQW TDGYAFQNLV KQQERVNGQR EEIERQRKLL IKKKPPSASQ
TPPPNLEPNK RKSKSNGAEN EMLSLAEYHE QEEIFKLRLG HLKKEEAEIQ VELERLERVR
NLHIRELKRI HNEDNSQFKD HPTLNDRYLL LHLLGRGGFS EVYKAFDLTE QRYVAVKIHQ
LNKNWRDEKK ENYHKHACRE YRIHKELDHP RIVKLYDYFS LDTDSFCTVL EYCEGNDLDF
YLKQHKLMSE KEARSIIMQV VNALKYLNEI RPPIIHYDLK PGNILLVNGT ACGEIKITDF
GLSKIMDDDN YGVDGMELTS QGAGTYWYLP PECFVVGKEP PKISNKVDVW SVGVIFYQCL
YGKKPFGHNQ SQQDILQENT ILKATEVQFP PKPGVSPEAK AFIRRCLVYR KEDRIDVHQL
ASDPYLLPHI RKSVAATGNS SMAVASTSNS SNSSASN
