TNI3K_RAT
ID TNI3K_RAT Reviewed; 835 AA.
AC Q7TQP6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Serine/threonine-protein kinase TNNI3K;
DE EC=2.7.11.1;
DE AltName: Full=Cardiac ankyrin repeat kinase;
DE AltName: Full=TNNI3-interacting kinase;
GN Name=Tnni3k {ECO:0000250|UniProtKB:Q59H18};
GN Synonyms=Cark {ECO:0000312|RGD:727908};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAP72031.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jeyaseelan R.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in cardiac physiology.
CC {ECO:0000250|UniProtKB:Q59H18}.
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:Q59H18};
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:Q59H18};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q59H18};
CC -!- SUBUNIT: Interacts with TNNI3, ACTC, ACTA1, MYBPC3, AIP, FABP3 and
CC HADHB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Expressed at lower levels in the cytoplasm. {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q59H18}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; AY303692; AAP72031.1; -; mRNA.
DR RefSeq; NP_861434.1; NM_181769.1.
DR AlphaFoldDB; Q7TQP6; -.
DR SMR; Q7TQP6; -.
DR STRING; 10116.ENSRNOP00000031479; -.
DR ChEMBL; CHEMBL4802010; -.
DR iPTMnet; Q7TQP6; -.
DR PhosphoSitePlus; Q7TQP6; -.
DR PaxDb; Q7TQP6; -.
DR PRIDE; Q7TQP6; -.
DR GeneID; 295531; -.
DR KEGG; rno:295531; -.
DR CTD; 51086; -.
DR RGD; 727908; Tnni3k.
DR eggNOG; KOG0192; Eukaryota.
DR InParanoid; Q7TQP6; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q7TQP6; -.
DR PRO; PR:Q7TQP6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISS:BHF-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0031013; F:troponin I binding; ISO:RGD.
DR GO; GO:0086069; P:bundle of His cell to Purkinje myocyte communication; ISS:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:1903779; P:regulation of cardiac conduction; ISS:BHF-UCL.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISS:BHF-UCL.
DR GO; GO:0002027; P:regulation of heart rate; ISS:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 10.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; ATP-binding; Coiled coil; Cytoplasm; Kinase; Lipoprotein;
KW Magnesium; Metal-binding; Myristate; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..835
FT /note="Serine/threonine-protein kinase TNNI3K"
FT /id="PRO_0000086760"
FT REPEAT 66..96
FT /note="ANK 1"
FT REPEAT 100..129
FT /note="ANK 2"
FT REPEAT 133..162
FT /note="ANK 3"
FT REPEAT 166..195
FT /note="ANK 4"
FT REPEAT 199..228
FT /note="ANK 5"
FT REPEAT 234..263
FT /note="ANK 6"
FT REPEAT 269..298
FT /note="ANK 7"
FT REPEAT 304..335
FT /note="ANK 8"
FT REPEAT 339..368
FT /note="ANK 9"
FT REPEAT 381..410
FT /note="ANK 10"
FT DOMAIN 463..723
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT COILED 21..50
FT /evidence="ECO:0000255"
FT ACT_SITE 588
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 469..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 835 AA; 92732 MW; 35A022D1011615D3 CRC64;
MGNYKSRPTQ TCSDEWKKKV SESYAIIIER LEDNLQIKEN EFQELRHIFG SDEAFSEVSL
NYRTERGLSL LHLCCVCGGN KSHIRALMLK GLRPSRLTRN GFPALHLAVY KDSPELITSL
LHSGADVQQV GYGGLTALHI AAIAGHPEAA EVLLQHGANV NVQDAVFFTP LHIAAYYGHE
QVTSVLLKFG ADVNVSGEVG DRPLHLASAK GFFNIVKLLV EEGSKADVNA QDNEDHVPLH
FCSRFGHHNI VSYLLQSDLE VQPHVINIYG DTPLHLACYN GNFEVAKEIV QVTGTESLTK
ENIFSETAFH SACTYGKNID LVKFLLDQNA VNINHRGRDG HTGLHSACYH GHIRLVQFLL
DNGADMNLVA CDPSRSSGEK DEQTCLMWAY EKGHDAIVTL LKHYKRPQEE LPCNEYSQPG
GDGSYVSVPS PLGKIKSMTK EKADVLLLRA ELPSRFHLQL SEIEFHEIIG SGSFGKVYKG
RCRNKIVAIK RYRANTYCSK SDVDMFCREV SILCQLNHPC VVQFVGACLD DPSQFAIVTQ
YISGGSLFSL LHEQKRILDL QSKLIIAVDV AKGMEYLHSL TQPIIHRDLN SHNILLYEDG
HAVVADFGES RFLQSLDEDN MTKQPGNLRW MAPEVFTQCT RYTIKADVFS YSLCLWELLT
GEIPFAHLKP AAAAADMAYH HIRPPIGYSI PKPISSLLIR GWNACPEGRP EFSEVVSKLE
ECLCNVELMS PASSNSSGSL SPSSSSDCLL SRGGPGRSHV AALRSRFELE YALNARSYAG
WSQSVGTHSN PGLSLEEMNR STQYSTVDKY GYVSDPMSLT HLHSRQDDSN FEDSN
