FAKD4_MOUSE
ID FAKD4_MOUSE Reviewed; 630 AA.
AC Q91YM4; O89082; Q3TKZ4; Q6ZQ19; Q8C6D1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=FAST kinase domain-containing protein 4;
DE AltName: Full=Protein TBRG4;
DE AltName: Full=Transforming growth factor beta regulator 4;
DE Flags: Precursor;
GN Name=Tbrg4; Synonyms=Kiaa0948;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Blastocyst, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 216-371 (ISOFORMS 1/2).
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA Chu C.C., Paul W.E.;
RT "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT representational difference analysis.";
RL Mol. Immunol. 35:487-502(1998).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=20869947; DOI=10.1016/j.bbrc.2010.09.075;
RA Simarro M., Gimenez-Cassina A., Kedersha N., Lazaro J.B., Adelmant G.O.,
RA Marto J.A., Rhee K., Tisdale S., Danial N., Benarafa C., Orduna A.,
RA Anderson P.;
RT "Fast kinase domain-containing protein 3 is a mitochondrial protein
RT essential for cellular respiration.";
RL Biochem. Biophys. Res. Commun. 401:440-446(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in processing of mitochondrial RNA precursors
CC and in stabilization of a subset of mature mitochondrial RNA species,
CC such as MT-CO1, MT-CO2, MT-CYB, MT-CO3, MT-ND3, MT-ND5 and MT-ATP8/6.
CC May play a role in cell cycle progression.
CC {ECO:0000250|UniProtKB:Q969Z0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q969Z0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91YM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91YM4-2; Sequence=VSP_022461;
CC -!- TISSUE SPECIFICITY: Expression detected in spleen, testis, colon,
CC heart, smooth muscle, kidney, brain, lung, liver, brown and white
CC adipose tissue with highest expression in testis, heart, smooth muscle
CC and brown adipose tissue. {ECO:0000269|PubMed:20869947}.
CC -!- SIMILARITY: Belongs to the FAST kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC36538.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC36037.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC98055.1; Type=Erroneous initiation; Evidence={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; AK129245; BAC98055.1; ALT_INIT; mRNA.
DR EMBL; AK075897; BAC36037.1; ALT_INIT; mRNA.
DR EMBL; AK166760; BAE38999.1; -; mRNA.
DR EMBL; AK168088; BAE40061.1; -; mRNA.
DR EMBL; AL603787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016483; AAH16483.1; -; mRNA.
DR EMBL; BC031155; AAH31155.1; -; mRNA.
DR EMBL; BC031910; AAH31910.1; -; mRNA.
DR EMBL; U89434; AAC36538.1; ALT_SEQ; mRNA.
DR CCDS; CCDS24423.1; -. [Q91YM4-1]
DR RefSeq; NP_001123929.1; NM_001130457.1. [Q91YM4-1]
DR RefSeq; NP_598772.1; NM_134011.2. [Q91YM4-1]
DR RefSeq; XP_006514670.1; XM_006514607.3. [Q91YM4-1]
DR RefSeq; XP_006514671.1; XM_006514608.3.
DR AlphaFoldDB; Q91YM4; -.
DR SMR; Q91YM4; -.
DR BioGRID; 203983; 2.
DR IntAct; Q91YM4; 5.
DR STRING; 10090.ENSMUSP00000000394; -.
DR iPTMnet; Q91YM4; -.
DR PhosphoSitePlus; Q91YM4; -.
DR SwissPalm; Q91YM4; -.
DR EPD; Q91YM4; -.
DR MaxQB; Q91YM4; -.
DR PaxDb; Q91YM4; -.
DR PeptideAtlas; Q91YM4; -.
DR PRIDE; Q91YM4; -.
DR ProteomicsDB; 267709; -. [Q91YM4-1]
DR ProteomicsDB; 267710; -. [Q91YM4-2]
DR Antibodypedia; 13534; 185 antibodies from 28 providers.
DR DNASU; 21379; -.
DR Ensembl; ENSMUST00000000394; ENSMUSP00000000394; ENSMUSG00000000384. [Q91YM4-1]
DR Ensembl; ENSMUST00000156969; ENSMUSP00000114256; ENSMUSG00000000384. [Q91YM4-1]
DR Ensembl; ENSMUST00000189268; ENSMUSP00000140835; ENSMUSG00000000384. [Q91YM4-1]
DR GeneID; 21379; -.
DR KEGG; mmu:21379; -.
DR UCSC; uc007hyz.2; mouse. [Q91YM4-1]
DR CTD; 9238; -.
DR MGI; MGI:1100868; Tbrg4.
DR VEuPathDB; HostDB:ENSMUSG00000000384; -.
DR eggNOG; ENOG502QTRE; Eukaryota.
DR GeneTree; ENSGT01030000234607; -.
DR HOGENOM; CLU_029448_0_0_1; -.
DR InParanoid; Q91YM4; -.
DR OMA; EPVFTPY; -.
DR OrthoDB; 1209476at2759; -.
DR PhylomeDB; Q91YM4; -.
DR TreeFam; TF324885; -.
DR BioGRID-ORCS; 21379; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Tbrg4; mouse.
DR PRO; PR:Q91YM4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91YM4; protein.
DR Bgee; ENSMUSG00000000384; Expressed in ectoplacental cone and 252 other tissues.
DR ExpressionAtlas; Q91YM4; baseline and differential.
DR Genevisible; Q91YM4; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0035770; C:ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0090615; P:mitochondrial mRNA processing; ISS:UniProtKB.
DR GO; GO:0000963; P:mitochondrial RNA processing; IBA:GO_Central.
DR GO; GO:0016071; P:mRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; ISS:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013579; FAST_2.
DR InterPro; IPR010622; FAST_Leu-rich.
DR InterPro; IPR013584; RAP.
DR Pfam; PF06743; FAST_1; 1.
DR Pfam; PF08368; FAST_2; 1.
DR Pfam; PF08373; RAP; 1.
DR SMART; SM00952; RAP; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51286; RAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..630
FT /note="FAST kinase domain-containing protein 4"
FT /id="PRO_0000273027"
FT DOMAIN 560..618
FT /note="RAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00619"
FT VAR_SEQ 77..107
FT /note="ASRPEQLLELLGSDHSLHHNHAALILIRLSY -> D (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022461"
FT CONFLICT 166
FT /note="V -> L (in Ref. 2; BAC36037)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="T -> I (in Ref. 2; BAC36037)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="F -> S (in Ref. 5; AAC36538)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="A -> V (in Ref. 5; AAC36538)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="P -> S (in Ref. 5; AAC36538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 630 AA; 71513 MW; 22BD82426988C195 CRC64;
MAVRLMKRCT CLLREATRLV PTVAPVGRLR LAGVSCKTLT SSVSSPSSGS LAELLGKEQV
FTPYPEHQEL DFLIEKASRP EQLLELLGSD HSLHHNHAAL ILIRLSYLLS EKPKEKALLA
EDARFQRLVK LVDSQITCVW HGTLVKLLRS LYTLVLPQIS KELQSVEQEV RWRLRRLKYK
HLVFLAESCA SFMKEQHSQE LLAELLMHLE RRWTEINDSR TLVTMMTMAG HLSESLMNHL
EDKCLELVEQ FGPDELRKVL VTLAAQSRRS VPLLRAISYH LVQKPFPMTK GMLLDLAYAY
GKLSFHQTQV SQRLAADLLP FIPSMTPGEV ARCAKSFAFL KWLNLPLFEA FTQHLLSRVQ
DVSLSHVCSV LLAFARLNFH PEQEEDQFFS MVHEKLDPVL GSLEPALQVD LVWALCVLQH
VHETELHTVL HPGLHARFLE SKSPKDQSTF QKLVHINTTA LLEHPEYKGP FLPASAVAPI
PSPSNKKMTP LQKELQETLK ALLGNTDKGS LEVATQYGWV LDAEVLLDAD GHFLPLRNFV
APHLAQPVGN QPLPPGAKRI AFLRWEFPNF NSRSKDLLGR FVLARRHVLA AGFLVVDVPY
YEWLDLKSEW QKSAYLKDKM RKAMAEELAK
