TNI3K_PONAB
ID TNI3K_PONAB Reviewed; 618 AA.
AC Q5RF15;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Serine/threonine-protein kinase TNNI3K;
DE EC=2.7.11.1;
DE AltName: Full=TNNI3-interacting kinase;
GN Name=TNNI3K {ECO:0000250|UniProtKB:Q59H18};
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:0000312|EMBL:CAH89642.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart {ECO:0000312|EMBL:CAH89642.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR857346; CAH89642.1; -; mRNA.
DR RefSeq; NP_001127180.2; NM_001133708.2.
DR AlphaFoldDB; Q5RF15; -.
DR SMR; Q5RF15; -.
DR STRING; 9601.ENSPPYP00000001439; -.
DR eggNOG; KOG0192; Eukaryota.
DR InParanoid; Q5RF15; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; PF12796; Ank_2; 3.
DR Pfam; PF13637; Ank_4; 1.
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..618
FT /note="Serine/threonine-protein kinase TNNI3K"
FT /id="PRO_0000086759"
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..618
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT COILED 21..51
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 618 AA; 68942 MW; C390E834DE3F3690 CRC64;
MGNYKSRPTQ TCTDEWKKKV SESYVITIER LEDDLKIKEK ELTELRNIFG SDEAFSKVNL
NYHTENGLSL LHLCCICGGN KSHIRTLMLK GLRPSRLTRN GFTALHLAVY KDNAELITSL
LHGGADIQQV GYGGLTALHI ATIAGHLEAA DVLLQHGANV NIQDAVFFTP LHIAAYYGHE
QVTRLLLKFG ADVNVSGEVG DRPLHLASAK GFLNIAKLLM EEGSKADVNA QDNEDHVPLH
FCSRFGHHDI VKYLLQNDLE VQPHVVNIYG DTPLHLACYN GKFEVAKEII QISGTESLTK
ENIFSETAFH SACTYGKSID LVKFLLDQNV ININHQGRDG HTGLHSACYH GHIHLVQFLL
DNGADMNLVA CDPSRSSGEK DEQTCLMWAY EKGHDAIVTL LKHYKRPQDE LPCNEYSQPG
GDGSYVSVPS PLGKIKSMTK EKADILLLRA GLPSHFHLQL SEIEFHEIIG SGSFGKVYKG
RCRNKIVAIK RYRANTYCSK SDVDMFCREV SILCQLNHPC VIQFVGACLN DPSQFAIVTQ
YISGGSLFSL LHEQKRILDL QSKLIIAVDV ARGMEYLHNL TQPIIHRDLN RSLKYLSAFC
CCPNHLFLTA HTIYLLAP
