ID   FAKD2_RAT               Reviewed;         679 AA.
AC   Q5M7V7;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=FAST kinase domain-containing protein 2, mitochondrial;
DE   Flags: Precursor;
GN   Name=Fastkd2;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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: Plays an important role in assembly of the mitochondrial
CC       large ribosomal subunit. As a component of a functional protein-RNA
CC       module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and
CC       16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA
CC       abundance and is required for intra-mitochondrial translation. May play
CC       a role in mitochondrial apoptosis. {ECO:0000250|UniProtKB:Q9NYY8}.
CC   -!- SUBUNIT: Monomer. Found in a complex with GRSF1, DDX28, DHX30 and
CC       FASTKD5. Associates with the 16S mitochondrial rRNA (16S mt-rRNA).
CC       Forms a regulatory protein-RNA complex, consisting of RCC1L, NGRN,
CC       RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA.
CC       {ECO:0000250|UniProtKB:Q9NYY8}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q9NYY8}. Mitochondrion matrix, mitochondrion
CC       nucleoid {ECO:0000250|UniProtKB:Q9NYY8}. Note=Localizes to
CC       mitochondrial RNA granules found in close proximity to the
CC       mitochondrial nucleoids. {ECO:0000250|UniProtKB:Q9NYY8}.
CC   -!- SIMILARITY: Belongs to the FAST kinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC088416; AAH88416.1; -; mRNA.
DR   RefSeq; NP_001009673.1; NM_001009673.1.
DR   AlphaFoldDB; Q5M7V7; -.
DR   STRING; 10116.ENSRNOP00000017281; -.
DR   PaxDb; Q5M7V7; -.
DR   PeptideAtlas; Q5M7V7; -.
DR   PRIDE; Q5M7V7; -.
DR   GeneID; 301463; -.
DR   KEGG; rno:301463; -.
DR   CTD; 22868; -.
DR   RGD; 1307883; Fastkd2.
DR   eggNOG; ENOG502QVSD; Eukaryota.
DR   HOGENOM; CLU_025270_0_0_1; -.
DR   InParanoid; Q5M7V7; -.
DR   PhylomeDB; Q5M7V7; -.
DR   PRO; PR:Q5M7V7; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; Q5M7V7; RN.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; ISS:UniProtKB.
DR   GO; GO:0000963; P:mitochondrial RNA processing; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IBA:GO_Central.
DR   GO; GO:0006396; P:RNA processing; ISS:UniProtKB.
DR   InterPro; IPR010622; FAST_Leu-rich.
DR   InterPro; IPR013584; RAP.
DR   Pfam; PF06743; FAST_1; 1.
DR   Pfam; PF08373; RAP; 1.
DR   SMART; SM00952; RAP; 1.
DR   PROSITE; PS51286; RAP; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; Mitochondrion nucleoid; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; RNA-binding; rRNA-binding; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..679
FT                   /note="FAST kinase domain-containing protein 2,
FT                   mitochondrial"
FT                   /id="PRO_0000050786"
FT   DOMAIN          607..664
FT                   /note="RAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00619"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYY8"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYY8"
SQ   SEQUENCE   679 AA;  77767 MW;  643E7B03953FDF4A CRC64;
     MNNRAHTFLW GIRQFRTSIP RSRALRTYSL VFCKPEVIHS KRNPRNHLLN GFDEGLQPSV
     RYLFQDIFIS KSVAGCTQTR GIIHAAGFKL DRILCPRRLS FDAKHSFVSD GTSDHDLMKT
     NFHHTSTEDV LTKKMRPTPV NYKKLAQECN SLSDVLDTFS KAPTFPGSNY FLAMWIIAKR
     ISEDKRRFEK QLMFSHPAFN QLCEQMMREA KIMRYDHLLF SLNAIVKLGV PQNSLMVQTL
     LRTIQERISE CDERCLSILS TALVTMEPCM NVNALRAGLR ILVDQQVWNI NDIFTLQTVM
     RCIGKDMKAL KELGRFSVLN SRHMFEVLAA MDHRSVVLLN ECSKIVIDNI HGCPFKVLIS
     ILQSCRDLRY QNEDLFKSIA DYVATTFDIW KLKHVIFFLL SFETLGFRPP GLMDKLLEKV
     VQEPGSLTVK NIVSVLHVYS SLNHVHNVQN REFLEALASA LTGCLHQISS ESLLNAVHSF
     CMMNYFPLAP INQLIKENII HELLTSGDTE KNIHKLHVLN TCLKLDESTY KCIHIPLPQL
     PLTASHPNEK LAEVLSRLLE GDGCFSRNVQ LPHNYHIDFE IRMDTNRTQV FSFSEGDASS
     ATNMQRVAVL CVPKSAYCLN SNHLRGLMAM KIRHLNVMGF HVILIHNWEL KKLKMEDAVT
     FVRKKIYSDE ALATTDESV