ID RRF2M_MOUSE Reviewed; 779 AA.
AC Q8R2Q4; B2RR55; Q8BXS5;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=Ribosome-releasing factor 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03059};
DE Short=RRF2mt {ECO:0000255|HAMAP-Rule:MF_03059};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03059};
DE AltName: Full=Elongation factor G 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03059};
DE Short=EF-G2mt {ECO:0000255|HAMAP-Rule:MF_03059};
DE Short=mEF-G 2 {ECO:0000255|HAMAP-Rule:MF_03059};
GN Name=Gfm2; Synonyms=Efg2;
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 3).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC and 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: Mitochondrial GTPase that mediates the disassembly of
CC ribosomes from messenger RNA at the termination of mitochondrial
CC protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis
CC follows the ribosome disassembly and probably occurs on the ribosome
CC large subunit. Not involved in the GTP-dependent ribosomal
CC translocation step during translation elongation. {ECO:0000255|HAMAP-
CC Rule:MF_03059}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03059};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03059}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8R2Q4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R2Q4-2; Sequence=VSP_038195;
CC Name=3;
CC IsoId=Q8R2Q4-3; Sequence=VSP_038196;
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03059}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03059}.
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DR EMBL; AK044371; BAC31889.1; -; mRNA.
DR EMBL; BC027341; AAH27341.1; -; mRNA.
DR EMBL; BC138233; AAI38234.1; -; mRNA.
DR EMBL; BC145208; AAI45209.1; -; mRNA.
DR CCDS; CCDS26708.2; -. [Q8R2Q4-1]
DR CCDS; CCDS70490.1; -. [Q8R2Q4-3]
DR CCDS; CCDS70491.1; -. [Q8R2Q4-2]
DR RefSeq; NP_001139515.1; NM_001146043.2.
DR RefSeq; NP_001258392.1; NM_001271463.1. [Q8R2Q4-1]
DR RefSeq; NP_001258393.1; NM_001271464.1. [Q8R2Q4-3]
DR RefSeq; NP_001258394.1; NM_001271465.1. [Q8R2Q4-2]
DR RefSeq; NP_796240.3; NM_177266.5. [Q8R2Q4-1]
DR RefSeq; XP_006517752.1; XM_006517689.3. [Q8R2Q4-1]
DR RefSeq; XP_006517753.1; XM_006517690.3. [Q8R2Q4-1]
DR AlphaFoldDB; Q8R2Q4; -.
DR SMR; Q8R2Q4; -.
DR BioGRID; 236307; 9.
DR STRING; 10090.ENSMUSP00000125656; -.
DR iPTMnet; Q8R2Q4; -.
DR PhosphoSitePlus; Q8R2Q4; -.
DR EPD; Q8R2Q4; -.
DR MaxQB; Q8R2Q4; -.
DR PaxDb; 10090-ENSMUSP00000125656; -.
DR PeptideAtlas; Q8R2Q4; -.
DR ProteomicsDB; 299894; -. [Q8R2Q4-1]
DR ProteomicsDB; 299895; -. [Q8R2Q4-2]
DR ProteomicsDB; 299896; -. [Q8R2Q4-3]
DR Pumba; Q8R2Q4; -.
DR Antibodypedia; 44237; 165 antibodies from 23 providers.
DR DNASU; 320806; -.
DR Ensembl; ENSMUST00000022170.8; ENSMUSP00000022170.8; ENSMUSG00000021666.17. [Q8R2Q4-2]
DR Ensembl; ENSMUST00000042084.13; ENSMUSP00000048373.7; ENSMUSG00000021666.17. [Q8R2Q4-3]
DR Ensembl; ENSMUST00000161639.8; ENSMUSP00000125656.2; ENSMUSG00000021666.17. [Q8R2Q4-1]
DR GeneID; 320806; -.
DR KEGG; mmu:320806; -.
DR UCSC; uc007rnu.2; mouse. [Q8R2Q4-1]
DR UCSC; uc011zdh.1; mouse. [Q8R2Q4-2]
DR UCSC; uc011zdi.1; mouse. [Q8R2Q4-3]
DR AGR; MGI:2444783; -.
DR CTD; 84340; -.
DR MGI; MGI:2444783; Gfm2.
DR VEuPathDB; HostDB:ENSMUSG00000021666; -.
DR eggNOG; KOG0464; Eukaryota.
DR GeneTree; ENSGT00550000074890; -.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q8R2Q4; -.
DR OMA; GPQFTFP; -.
DR OrthoDB; 148165at2759; -.
DR PhylomeDB; Q8R2Q4; -.
DR TreeFam; TF314848; -.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 320806; 19 hits in 74 CRISPR screens.
DR ChiTaRS; Gfm2; mouse.
DR PRO; PR:Q8R2Q4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8R2Q4; Protein.
DR Bgee; ENSMUSG00000021666; Expressed in hindlimb stylopod muscle and 243 other cell types or tissues.
DR ExpressionAtlas; Q8R2Q4; baseline and differential.
DR Genevisible; Q8R2Q4; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0032790; P:ribosome disassembly; ISS:UniProtKB.
DR CDD; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR CDD; cd04092; mtEFG2_II_like; 1.
DR CDD; cd01693; mtEFG2_like_IV; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_03059; mEF_G_2; 1.
DR InterPro; IPR030851; EFG2.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTP-binding; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..779
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000007451"
FT DOMAIN 68..353
FT /note="tr-type G"
FT BINDING 77..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 141..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 195..198
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT VAR_SEQ 50..51
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038195"
FT VAR_SEQ 284..310
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038196"
FT CONFLICT 245
FT /note="L -> V (in Ref. 2; AAH27341)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="K -> T (in Ref. 2; AAH27341)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="H -> R (in Ref. 2; AAH27341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 779 AA; 86109 MW; D9AA1D5775027207 CRC64;
MFTKWRIFAV NHQRTFSVHL NTMCYCKIKA NLKRLKTQLP LTRNYSSAPG IAGSDVKSLH
SVINPPVAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG
ITIQSAAVTL DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW
RQADKHKIPR ICFLNKMDKT GASFNYAVES IREKLKAKPL ILQLPIGEAR TFQGVVDVVN
KEKLLWNSNS DDGKDFERMP LSEASDRELL KETIEARNSL IEQVADLDDE FADLVLGEFS
ENFDLVPAEK LQAAVHRVTL AQAAVPVLCG SALKNKGVQP LLDAVTTYLP SPEEREDRFL
QWYEGDLCAL AFKVLHDKQR GPLVFLRIYS GTLTPQLAVH NINRNCTERM SRLLLPFADQ
HVEIPSLTAG NIALTVGLKQ TATGDTIVSS KSSALAAARR AGRGEREHGK KREAESLLLA
GVEVPEPVFF CTIEPPSVAK QPDLDHALER LQREDPSLKV KLDPDSGQTV LCGMGELHIE
IIHDRIKREY GLETYLGPLQ VAYRETILNS VRATDTLDRV LGDKRHLVSA ELEVRPAEEP
CAVAKIEYAD CVGEDLLQAS REAIESAVHS ACLQGPLLGS PVQDVAMTLH SLMIHPGTST
TMVTACISRC MQKALKKADK QVLEPLMSLE VTVSREYLSP VLADLAQRRG NIQEIQTRQD
NRVVLGFVPL AEIMGYSTVL RTLTSGSATF ALELSTYQAM SPQDQSALLN QRSGLAHVL
//
