TNI3K_MOUSE
ID TNI3K_MOUSE Reviewed; 834 AA.
AC Q5GIG6; B2RTJ7; Q5GIG5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 144.
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:0000312|MGI:MGI:2443276}; Synonyms=Cark;
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] {ECO:0000305, ECO:0000312|EMBL:AAS98608.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=KM {ECO:0000312|EMBL:AAS98608.1};
RA Chen C., Zhen Y., Liu Y., Xun L., Chen J., Zhang L., Hui R.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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 TISSUE=Brain;
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5GIG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5GIG6-2; Sequence=VSP_051886, VSP_051887;
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; AY526095; AAS98608.1; -; mRNA.
DR EMBL; AY526096; AAS98609.1; -; mRNA.
DR EMBL; AC125097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139368; AAI39369.1; -; mRNA.
DR EMBL; BC139394; AAI39395.1; -; mRNA.
DR CCDS; CCDS17928.1; -. [Q5GIG6-1]
DR RefSeq; NP_796040.3; NM_177066.5. [Q5GIG6-1]
DR AlphaFoldDB; Q5GIG6; -.
DR SMR; Q5GIG6; -.
DR STRING; 10090.ENSMUSP00000070561; -.
DR GuidetoPHARMACOLOGY; 2247; -.
DR iPTMnet; Q5GIG6; -.
DR PhosphoSitePlus; Q5GIG6; -.
DR PaxDb; Q5GIG6; -.
DR PRIDE; Q5GIG6; -.
DR ProteomicsDB; 258934; -. [Q5GIG6-1]
DR ProteomicsDB; 258935; -. [Q5GIG6-2]
DR DNASU; 435766; -.
DR Ensembl; ENSMUST00000064076; ENSMUSP00000070561; ENSMUSG00000040086. [Q5GIG6-1]
DR Ensembl; ENSMUST00000143410; ENSMUSP00000122478; ENSMUSG00000040086. [Q5GIG6-2]
DR GeneID; 435766; -.
DR KEGG; mmu:435766; -.
DR UCSC; uc008rus.2; mouse. [Q5GIG6-1]
DR CTD; 51086; -.
DR MGI; MGI:2443276; Tnni3k.
DR VEuPathDB; HostDB:ENSMUSG00000040086; -.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00940000159131; -.
DR HOGENOM; CLU_017658_0_0_1; -.
DR InParanoid; Q5GIG6; -.
DR OMA; IHFVGAC; -.
DR OrthoDB; 173077at2759; -.
DR PhylomeDB; Q5GIG6; -.
DR TreeFam; TF317710; -.
DR BioGRID-ORCS; 435766; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Tnni3k; mouse.
DR PRO; PR:Q5GIG6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q5GIG6; protein.
DR Bgee; ENSMUSG00000040086; Expressed in myocardium of ventricle and 12 other tissues.
DR Genevisible; Q5GIG6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
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:0031013; F:troponin I binding; ISO:MGI.
DR GO; GO:0086069; P:bundle of His cell to Purkinje myocyte communication; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:1903779; P:regulation of cardiac conduction; IMP:BHF-UCL.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
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; 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 Alternative splicing; ANK repeat; ATP-binding; Coiled coil; Cytoplasm;
KW Kinase; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..834
FT /note="Serine/threonine-protein kinase TNNI3K"
FT /id="PRO_0000086758"
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..229
FT /note="ANK 5"
FT REPEAT 233..262
FT /note="ANK 6"
FT REPEAT 268..297
FT /note="ANK 7"
FT REPEAT 303..334
FT /note="ANK 8"
FT REPEAT 338..367
FT /note="ANK 9"
FT REPEAT 380..409
FT /note="ANK 10"
FT DOMAIN 462..722
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 815..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..49
FT /evidence="ECO:0000255"
FT ACT_SITE 587
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 468..476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 489
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"
FT VAR_SEQ 670..675
FT /note="AAAAAD -> GKTRVL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_051886"
FT VAR_SEQ 676..834
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_051887"
FT CONFLICT 659
FT /note="T -> I (in Ref. 1; AAS98608/AAS98609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 92575 MW; AC8581BFA7B05216 CRC64;
MGNYKSRPTQ TCSDEWKKKV SESYAIIIER LEDDLQIKEN EFQELRHIFG SDEAFSEVSL
NYRTERGLSL LHLCCACGGN KSHIRALMLK GLRPSRLTRN GFPALHLAVY KDSLELITSL
LHSGADVQQA GYGGLTALHI AAIAGHPEAV EVLLQHGANV NVQDAVFFTP LHIAAYYGHE
QVTSVLLKFG ADVNVSGEVG DRPLHLASAK GFFNIVKLLV EGNKADVNAQ DNEDHVPLHF
CSRFGHHNIV SYLLQSDLEV QPHVINIYGD TPLHLACYNG NFEVAKEIVH VTGTESLTKE
NIFSETAFHS ACTYGKNIDL VKFLLDQNAV NINHRGRDGH TGLHSACYHG HIRLVQFLLD
NGADMNLVAC DPSRSSGEKD EQTCLMWAYE KGHDAIVTLL KHYKRPQDEL PCNEYSQPGG
DGSYVSVPSP LGKIKSMTKE KADVLLLRAE LPSRFHLQLS EIEFHEIIGS GSFGKVYKGR
CRNKIVAIKR YRANTYCSKS DVDMFCREVS ILCQLNHPCV VQFVGACLDD PSQFAIVTQY
ISGGSLFSLL HEQKRILDLQ SKLIIAVDVA KGMEYLHSLT QPIIHRDLNS HNILLYEDGH
AVVADFGESR FLQSLDEDNM TKQPGNLRWM APEVFTQCTR YTIKADVFSY ALCLWELLTG
EIPFAHLKPA AAAADMAYHH IRPPIGYSIP KPISSLLMRG WNACPEGRPE FSEVVRKLEE
CLCNVELMSP ASSNSSGSLS PSSSSDCLLS RGGPGRSHVA ALRSRFELEY ALNARSYTGW
PQSVGTHTNP GLSLEEMNRG AQYSAVDKYG YVSDPMSPMH LHSRRNSGSF EDGN
