ID RRF2M_HUMAN Reviewed; 779 AA.
AC Q969S9; A0AR28; Q8N6D8; Q8WYI0; Q9H6Z1;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 186.
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:0000269|PubMed:19716793};
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};
DE AltName: Full=Elongation factor G2;
DE Short=hEFG2;
GN Name=GFM2 {ECO:0000255|HAMAP-Rule:MF_03059};
GN Synonyms=EFG2 {ECO:0000255|HAMAP-Rule:MF_03059}; ORFNames=MSTP027;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11735030; DOI=10.1007/s00439-001-0610-5;
RA Hammarsund M., Wilson W., Corcoran M., Merup M., Einhorn S., Grander D.,
RA Sangfelt O.;
RT "Identification and characterization of two novel human mitochondrial
RT elongation factor genes, hEFG2 and hEFG1, phylogenetically conserved
RT through evolution.";
RL Hum. Genet. 109:542-550(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Zheng M., Xie Y., Mao Y.;
RT "Cloning of elongation factor G isoform.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Aorta;
RA Xu Y.Y., Sun L.Z., Wu Q.Y., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L.,
RA Ye J., Sheng H., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Sun Y.H.,
RA Jiang Y.X., Zhao X.W., Liu S., Liu L.S., Ding J.F., Gao R.L., Qiang B.Q.,
RA Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP HIS-425; GLY-594 AND GLY-735.
RC TISSUE=Brain, and Skin;
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 [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19716793; DOI=10.1016/j.molcel.2009.06.028;
RA Tsuboi M., Morita H., Nozaki Y., Akama K., Ueda T., Ito K., Nierhaus K.H.,
RA Takeuchi N.;
RT "EF-G2mt is an exclusive recycling factor in mammalian mitochondrial
RT protein synthesis.";
RL Mol. Cell 35:502-510(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP INVOLVEMENT IN COXPD39.
RX PubMed=26016410; DOI=10.1038/jhg.2015.57;
RA Fukumura S., Ohba C., Watanabe T., Minagawa K., Shimura M., Murayama K.,
RA Ohtake A., Saitsu H., Matsumoto N., Tsutsumi H.;
RT "Compound heterozygous GFM2 mutations with Leigh syndrome complicated by
RT arthrogryposis multiplex congenita.";
RL J. Hum. Genet. 60:509-513(2015).
RN [11]
RP VARIANT COXPD39 GLU-576.
RX PubMed=22700954; DOI=10.1126/scitranslmed.3003544;
RA Dixon-Salazar T.J., Silhavy J.L., Udpa N., Schroth J., Bielas S.,
RA Schaffer A.E., Olvera J., Bafna V., Zaki M.S., Abdel-Salam G.H.,
RA Mansour L.A., Selim L., Abdel-Hadi S., Marzouki N., Ben-Omran T.,
RA Al-Saana N.A., Sonmez F.M., Celep F., Azam M., Hill K.J., Collazo A.,
RA Fenstermaker A.G., Novarino G., Akizu N., Garimella K.V., Sougnez C.,
RA Russ C., Gabriel S.B., Gleeson J.G.;
RT "Exome sequencing can improve diagnosis and alter patient management.";
RL Sci. Transl. Med. 4:138RA78-138RA78(2012).
RN [12]
RP VARIANTS COXPD39 SER-92 AND GLN-190, AND INVOLVEMENT IN COXPD39.
RX PubMed=29075935; DOI=10.1007/s10048-017-0526-4;
RA Glasgow R.I.C., Thompson K., Barbosa I.A., He L., Alston C.L.,
RA Deshpande C., Simpson M.A., Morris A.A.M., Neu A., Loebel U., Hall J.,
RA Prokisch H., Haack T.B., Hempel M., McFarland R., Taylor R.W.;
RT "Novel GFM2 variants associated with early-onset neurological presentations
RT of mitochondrial disease and impaired expression of OXPHOS subunits.";
RL Neurogenetics 18:227-235(2017).
RN [13] {ECO:0007744|PDB:7NSH}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 45-779 IN COMPLEX WITH
RP NON-HYDROLYZABLE ANALOG OF GTP; MRRF AND MITOCHONDRIAL RIBOSOME.
RX PubMed=33878294; DOI=10.1016/j.molcel.2021.03.042;
RA Kummer E., Schubert K.N., Schoenhut T., Scaiola A., Ban N.;
RT "Structural basis of translation termination, rescue, and recycling in
RT mammalian mitochondria.";
RL Mol. Cell 81:2566-2582(2021).
CC -!- FUNCTION: Mitochondrial GTPase that mediates the disassembly of
CC ribosomes from messenger RNA at the termination of mitochondrial
CC protein biosynthesis (PubMed:19716793, PubMed:33878294). Acts in
CC collaboration with MRRF (PubMed:19716793, PubMed:33878294). Promotes
CC mitochondrial ribosome recycling by dissolution of intersubunit
CC contacts (PubMed:33878294). GTP hydrolysis follows the ribosome
CC disassembly and probably occurs on the ribosome large subunit
CC (PubMed:19716793). Not involved in the GTP-dependent ribosomal
CC translocation step during translation elongation (PubMed:19716793).
CC {ECO:0000269|PubMed:19716793, ECO:0000269|PubMed:33878294}.
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;
CC Evidence={ECO:0000269|PubMed:19716793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:19716793};
CC -!- INTERACTION:
CC Q969S9; Q8N9N5: BANP; NbExp=3; IntAct=EBI-2371750, EBI-744695;
CC Q969S9; P14373: TRIM27; NbExp=3; IntAct=EBI-2371750, EBI-719493;
CC Q969S9; Q9C026: TRIM9; NbExp=3; IntAct=EBI-2371750, EBI-720828;
CC Q969S9; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-2371750, EBI-2799833;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03059}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q969S9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969S9-2; Sequence=VSP_001363;
CC Name=3;
CC IsoId=Q969S9-3; Sequence=VSP_038194;
CC Name=4;
CC IsoId=Q969S9-4; Sequence=VSP_038192, VSP_038193;
CC Name=5;
CC IsoId=Q969S9-5; Sequence=VSP_038190, VSP_038191;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11735030}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 39 (COXPD39)
CC [MIM:618397]: An autosomal recessive disorder due to mitochondrial
CC dysfunction and characterized by global developmental delay, axial
CC hypotonia, dystonia, dysarthria, impaired intellectual development with
CC poor speech, and deficiencies of the mitochondrial respiratory chain
CC enzyme complexes. Neuroimaging shows abnormalities in the putamen and
CC caudate nuclei, along with subcortical white matter involvement.
CC {ECO:0000269|PubMed:22700954, ECO:0000269|PubMed:26016410,
CC ECO:0000269|PubMed:29075935}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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; AF367997; AAK53401.1; -; mRNA.
DR EMBL; AY453587; AAS49035.1; -; mRNA.
DR EMBL; AK025314; BAB15109.1; -; mRNA.
DR EMBL; AF111808; AAL39010.1; -; mRNA.
DR EMBL; CH471084; EAW95744.1; -; Genomic_DNA.
DR EMBL; BC015712; AAH15712.1; -; mRNA.
DR EMBL; BC030612; AAH30612.1; -; mRNA.
DR CCDS; CCDS4023.1; -. [Q969S9-1]
DR CCDS; CCDS4024.1; -. [Q969S9-2]
DR CCDS; CCDS47232.1; -. [Q969S9-5]
DR RefSeq; NP_001268231.1; NM_001281302.1.
DR RefSeq; NP_115756.2; NM_032380.4. [Q969S9-1]
DR RefSeq; NP_733781.1; NM_170681.2. [Q969S9-5]
DR RefSeq; NP_733792.1; NM_170691.2. [Q969S9-2]
DR RefSeq; XP_016865475.1; XM_017009986.1. [Q969S9-1]
DR PDB; 7L20; EM; 3.15 A; w=62-779.
DR PDB; 7NSH; EM; 3.20 A; BC=45-779.
DR PDBsum; 7L20; -.
DR PDBsum; 7NSH; -.
DR AlphaFoldDB; Q969S9; -.
DR EMDB; EMD-12567; -.
DR EMDB; EMD-23121; -.
DR SMR; Q969S9; -.
DR BioGRID; 124062; 181.
DR DIP; DIP-53437N; -.
DR IntAct; Q969S9; 22.
DR MINT; Q969S9; -.
DR STRING; 9606.ENSP00000427004; -.
DR CarbonylDB; Q969S9; -.
DR GlyGen; Q969S9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q969S9; -.
DR PhosphoSitePlus; Q969S9; -.
DR SwissPalm; Q969S9; -.
DR BioMuta; GFM2; -.
DR DMDM; 28201798; -.
DR EPD; Q969S9; -.
DR jPOST; Q969S9; -.
DR MassIVE; Q969S9; -.
DR MaxQB; Q969S9; -.
DR PaxDb; 9606-ENSP00000296805; -.
DR PeptideAtlas; Q969S9; -.
DR ProteomicsDB; 75837; -. [Q969S9-1]
DR ProteomicsDB; 75838; -. [Q969S9-2]
DR ProteomicsDB; 75839; -. [Q969S9-3]
DR ProteomicsDB; 75840; -. [Q969S9-4]
DR ProteomicsDB; 75841; -. [Q969S9-5]
DR Pumba; Q969S9; -.
DR Antibodypedia; 44237; 165 antibodies from 23 providers.
DR DNASU; 84340; -.
DR Ensembl; ENST00000296805.8; ENSP00000296805.3; ENSG00000164347.18. [Q969S9-1]
DR Ensembl; ENST00000345239.6; ENSP00000296804.3; ENSG00000164347.18. [Q969S9-2]
DR Ensembl; ENST00000427854.6; ENSP00000405808.2; ENSG00000164347.18. [Q969S9-5]
DR Ensembl; ENST00000509430.5; ENSP00000427004.1; ENSG00000164347.18. [Q969S9-1]
DR GeneID; 84340; -.
DR KEGG; hsa:84340; -.
DR MANE-Select; ENST00000296805.8; ENSP00000296805.3; NM_032380.5; NP_115756.2.
DR UCSC; uc003kdh.2; human. [Q969S9-1]
DR AGR; HGNC:29682; -.
DR CTD; 84340; -.
DR DisGeNET; 84340; -.
DR GeneCards; GFM2; -.
DR HGNC; HGNC:29682; GFM2.
DR HPA; ENSG00000164347; Low tissue specificity.
DR MalaCards; GFM2; -.
DR MIM; 606544; gene.
DR MIM; 618397; phenotype.
DR neXtProt; NX_Q969S9; -.
DR OpenTargets; ENSG00000164347; -.
DR Orphanet; 565624; Combined oxidative phosphorylation defect type 39.
DR PharmGKB; PA134949527; -.
DR VEuPathDB; HostDB:ENSG00000164347; -.
DR eggNOG; KOG0464; Eukaryota.
DR GeneTree; ENSGT00550000074890; -.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q969S9; -.
DR OMA; GPQFTFP; -.
DR OrthoDB; 148165at2759; -.
DR PhylomeDB; Q969S9; -.
DR TreeFam; TF314848; -.
DR PathwayCommons; Q969S9; -.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; Q969S9; -.
DR BioGRID-ORCS; 84340; 123 hits in 1157 CRISPR screens.
DR ChiTaRS; GFM2; human.
DR GenomeRNAi; 84340; -.
DR Pharos; Q969S9; Tbio.
DR PRO; PR:Q969S9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q969S9; Protein.
DR Bgee; ENSG00000164347; Expressed in left ventricle myocardium and 189 other cell types or tissues.
DR ExpressionAtlas; Q969S9; baseline and differential.
DR Genevisible; Q969S9; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IDA:UniProtKB.
DR GO; GO:0070126; P:mitochondrial translational termination; TAS:Reactome.
DR GO; GO:0032790; P:ribosome disassembly; IDA: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 3D-structure; Alternative splicing; Disease variant; GTP-binding;
KW Hydrolase; Mitochondrion; Nucleotide-binding;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome.
FT CHAIN 1..779
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000007450"
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 ECO:0000305|PubMed:33878294, ECO:0007744|PDB:7NSH"
FT BINDING 141..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059,
FT ECO:0000305|PubMed:33878294, ECO:0007744|PDB:7NSH"
FT BINDING 195..198
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059,
FT ECO:0000305|PubMed:33878294, ECO:0007744|PDB:7NSH"
FT VAR_SEQ 361..407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_001363"
FT VAR_SEQ 504..513
FT /note="DLEHALKCLQ -> GINGLSVSTN (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038190"
FT VAR_SEQ 514..779
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038191"
FT VAR_SEQ 530..531
FT /note="TV -> IP (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_038192"
FT VAR_SEQ 532..709
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_038193"
FT VAR_SEQ 608..609
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038194"
FT VARIANT 64
FT /note="N -> S (in dbSNP:rs957680)"
FT /id="VAR_053983"
FT VARIANT 92
FT /note="Y -> S (in COXPD39; dbSNP:rs1554042187)"
FT /evidence="ECO:0000269|PubMed:29075935"
FT /id="VAR_082193"
FT VARIANT 190
FT /note="R -> Q (in COXPD39; dbSNP:rs761283105)"
FT /evidence="ECO:0000269|PubMed:29075935"
FT /id="VAR_082194"
FT VARIANT 300
FT /note="S -> C (in dbSNP:rs16872235)"
FT /id="VAR_053984"
FT VARIANT 425
FT /note="P -> H (in dbSNP:rs17852780)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060200"
FT VARIANT 576
FT /note="D -> E (in COXPD39; uncertain significance; may
FT affect splicing)"
FT /evidence="ECO:0000269|PubMed:22700954"
FT /id="VAR_082195"
FT VARIANT 594
FT /note="E -> G (in dbSNP:rs17856872)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060201"
FT VARIANT 735
FT /note="E -> G (in dbSNP:rs17856871)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060202"
FT VARIANT 774
FT /note="R -> Q (in dbSNP:rs1048167)"
FT /id="VAR_053985"
FT CONFLICT 59
FT /note="L -> I (in Ref. 6; AAH30612)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="G -> V (in Ref. 2; AAS49035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 779 AA; 86601 MW; 856B4E26FD9DD94E CRC64;
MLTNLRIFAM SHQTIPSVYI NNICCYKIRA SLKRLKPHVP LGRNCSSLPG LIGNDIKSLH
SIINPPIAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG
ITIQSAAVTF DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW
RQADKHNIPR ICFLNKMDKT GASFKYAVES IREKLKAKPL LLQLPIGEAK TFKGVVDVVM
KEKLLWNCNS NDGKDFERKP LLEMNDPELL KETTEARNAL IEQVADLDDE FADLVLEEFS
ENFDLLPAEK LQTAIHRVTL AQTAVPVLCG SALKNKGIQP LLDAVTMYLP SPEERNYEFL
QWYKDDLCAL AFKVLHDKQR GPLVFMRIYS GTIKPQLAIH NINGNCTERI SRLLLPFADQ
HVEIPSLTAG NIALTVGLKH TATGDTIVSS KSSALAAARR AEREGEKKHR QNNEAERLLL
AGVEIPEPVF FCTIEPPSLS KQPDLEHALK CLQREDPSLK VRLDPDSGQT VLCGMGELHI
EIIHDRIKRE YGLETYLGPL QVAYRETILN SVRATDTLDR TLGDKRHLVT VEVEARPIET
SSVMPVIEFE YAESINEGLL KVSQEAIENG IHSACLQGPL LGSPIQDVAI TLHSLTIHPG
TSTTMISACV SRCVQKALKK ADKQVLEPLM NLEVTVARDY LSPVLADLAQ RRGNIQEIQT
RQDNKVVIGF VPLAEIMGYS TVLRTLTSGS ATFALELSTY QAMNPQDQNT LLNRRSGLT
//
