FASTK_MOUSE
ID FASTK_MOUSE Reviewed; 511 AA.
AC Q9JIX9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Fas-activated serine/threonine kinase;
DE Short=FAST kinase;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q14296};
DE EC=2.7.11.8 {ECO:0000250|UniProtKB:Q14296};
GN Name=Fastk;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Van Raay T.J., Rao M.S.;
RT "A mouse homolog of the human Fas-activated serine/threonine kinase (FAST
RT kinase).";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, RNA-BINDING, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25704814; DOI=10.1016/j.celrep.2015.01.063;
RA Jourdain A.A., Koppen M., Rodley C.D., Maundrell K., Gueguen N.,
RA Reynier P., Guaras A.M., Enriquez J.A., Anderson P., Simarro M.,
RA Martinou J.C.;
RT "A mitochondria-specific isoform of FASTK is present in mitochondrial RNA
RT granules and regulates gene expression and function.";
RL Cell Rep. 10:1110-1121(2015).
CC -!- FUNCTION: Phosphorylates the splicing regulator TIA1, thereby promoting
CC the inclusion of FAS exon 6, which leads to an mRNA encoding a pro-
CC apoptotic form of the receptor (By similarity). Required for the
CC biogenesis of some mitochondrial-encoded mRNAs, specifically stabilizes
CC ND6 (NADH dehydrogenase complex subunit 6) mRNA, and regulates its
CC levels. {ECO:0000250|UniProtKB:Q14296, ECO:0000269|PubMed:25704814}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[Fas-activated protein] = ADP + H(+) + O-
CC phospho-L-seryl-[Fas-activated protein]; Xref=Rhea:RHEA:15881,
CC Rhea:RHEA-COMP:13713, Rhea:RHEA-COMP:13714, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; EC=2.7.11.8;
CC Evidence={ECO:0000250|UniProtKB:Q14296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[Fas-activated protein] = ADP + H(+) + O-
CC phospho-L-threonyl-[Fas-activated protein]; Xref=Rhea:RHEA:53920,
CC Rhea:RHEA-COMP:13715, Rhea:RHEA-COMP:13716, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.8;
CC Evidence={ECO:0000250|UniProtKB:Q14296};
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:Q14296};
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:Q14296};
CC -!- SUBUNIT: Interacts with TIA1; the interactions leads to TIA1
CC phosphorylation (By similarity). Interacts with TIAR (By similarity).
CC {ECO:0000250|UniProtKB:Q14296}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:25704814}. Note=Colocalizes with mitochondrial RNA
CC granules. {ECO:0000269|PubMed:25704814}.
CC -!- DOMAIN: The RAP domain is essential for RNA-binding.
CC {ECO:0000269|PubMed:25704814}.
CC -!- PTM: Autophosphorylated on serine/threonine residues. Activated by
CC dephosphorylation (By similarity). {ECO:0000250|UniProtKB:Q14296}.
CC -!- DISRUPTION PHENOTYPE: 60% decrease in mitochondrial NADH dehydrogenase
CC activity. {ECO:0000269|PubMed:25704814}.
CC -!- SIMILARITY: Belongs to the FAST protein kinase family. {ECO:0000305}.
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DR EMBL; AF168682; AAF89660.1; -; mRNA.
DR AlphaFoldDB; Q9JIX9; -.
DR STRING; 10090.ENSMUSP00000030800; -.
DR iPTMnet; Q9JIX9; -.
DR PhosphoSitePlus; Q9JIX9; -.
DR PaxDb; Q9JIX9; -.
DR PRIDE; Q9JIX9; -.
DR ProteomicsDB; 275588; -.
DR MGI; MGI:1913837; Fastk.
DR eggNOG; ENOG502QXK7; Eukaryota.
DR InParanoid; Q9JIX9; -.
DR BRENDA; 2.7.11.8; 3474.
DR ChiTaRS; Fastk; mouse.
DR PRO; PR:Q9JIX9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JIX9; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0035770; C:ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033867; F:Fas-activated serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000963; P:mitochondrial RNA processing; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; ISO:MGI.
DR InterPro; IPR013579; FAST_2.
DR InterPro; IPR010622; FAST_Leu-rich.
DR InterPro; IPR013584; RAP.
DR InterPro; IPR015715; Ser/Thr_kinase_FAST.
DR PANTHER; PTHR21228:SF4; PTHR21228:SF4; 1.
DR Pfam; PF06743; FAST_1; 1.
DR Pfam; PF08368; FAST_2; 1.
DR Pfam; PF08373; RAP; 1.
DR SMART; SM00952; RAP; 1.
DR PROSITE; PS51286; RAP; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Kinase; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; RNA-binding;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..511
FT /note="Fas-activated serine/threonine kinase"
FT /id="PRO_0000087197"
FT DOMAIN 439..497
FT /note="RAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00619"
SQ SEQUENCE 511 AA; 57726 MW; 77C421F7E94ACB9C CRC64;
MLRILLSAQT SPARLSGLLL IPPVQPCCLG PSKSGDRPFG GGPVQGLQRL LEQARSPGEL
LRWLSQNPTK VRAHHYPVAL RRLGQLLVSQ PRPSPVEQAT LQDLSQLIIR NCPSFDVHTI
HVCLHLAVLL GFPSDGPLLC ALEQERRSRL PPKPPSPHRP AIYGGQRLEV ALSCPRFLQY
PRQHLIRSLA EARPEELTPH VMVLLAQHLA RHRLREPQLL EAIAHFLVVQ EAQLNSKVVQ
KLVLPFGRLN YMPLEQQFMP CLERILAREA GVAPLATVNI LMSLCQLQCL PFRALQFVFS
PSFINHINGT PPSLIVRRYL SLLDTAVELE LPGYQGPRLP QRQRVPIFPQ PLITDRARCK
YSHKDMVAEG LRQLLGEENY RQNLTVPPGY CTDFLLCVSS SGAVLPMRTQ DPFLPYPPRS
CQQDQANFNS TTQDPAQRVV LMLRERWHFC RDGRVLLGSR ALRERHLGLM GYQLLPLPFE
ELESQRGLPQ LKSYLRQKLQ ALGFRWGPEG G
