THG1_HUMAN
ID THG1_HUMAN Reviewed; 298 AA.
AC Q9NWX6; D3DQJ5; Q53G12; Q7L5R3; Q9H0S2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Probable tRNA(His) guanylyltransferase;
DE EC=2.7.7.79 {ECO:0000269|PubMed:21059936};
DE AltName: Full=Induced in high glucose-1 {ECO:0000303|PubMed:25008184};
DE Short=IHG-1 {ECO:0000303|PubMed:25008184};
DE AltName: Full=Interphase cytoplasmic foci protein 45;
DE AltName: Full=tRNA-histidine guanylyltransferase;
GN Name=THG1L; Synonyms=ICF45;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15459185; DOI=10.1074/jbc.m406737200;
RA Guo D., Hu K., Lei Y., Wang Y., Ma T., He D.;
RT "Identification and characterization of a novel cytoplasm protein ICF45
RT that is involved in cell cycle regulation.";
RL J. Biol. Chem. 279:53498-53505(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-232.
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].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-232.
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-232.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-232.
RC TISSUE=Brain, and Muscle;
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MFN1 AND MFN2.
RX PubMed=25008184; DOI=10.2337/db13-1256;
RA Hickey F.B., Corcoran J.B., Griffin B., Bhreathnach U., Mortiboys H.,
RA Reid H.M., Andrews D., Byrne S., Furlong F., Martin F., Godson C.,
RA Murphy M.;
RT "IHG-1 increases mitochondrial fusion and bioenergetic function.";
RL Diabetes 63:4314-4325(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM;
RP TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND
RP MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181;
RP LYS-216 AND ASN-227.
RX PubMed=21059936; DOI=10.1073/pnas.1010436107;
RA Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H.,
RA Jackman J.E., Doublie S.;
RT "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl
RT transferase, shares unexpected structural homology with canonical 5'-3' DNA
RT polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010).
RN [10]
RP INVOLVEMENT IN SCAR28, VARIANT SCAR28 ALA-55, CHARACTERIZATION OF VARIANT
RP SCAR28 ALA-55, AND FUNCTION.
RX PubMed=27307223; DOI=10.1007/s10048-016-0487-z;
RA Edvardson S., Elbaz-Alon Y., Jalas C., Matlock A., Patel K., Labbe K.,
RA Shaag A., Jackman J.E., Elpeleg O.;
RT "A mutation in the THG1L gene in a family with cerebellar ataxia and
RT developmental delay.";
RL Neurogenetics 17:219-225(2016).
RN [11]
RP VARIANT SCAR28 ALA-55.
RX PubMed=31168944; DOI=10.1002/ajmg.a.61196;
RA Walker M.A., Lerman-Sagie T., Swoboda K., Lev D., Blumkin L.;
RT "Refining the phenotype of the THG1L (p.Val55Ala mutation)-related
RT mitochondrial autosomal recessive congenital cerebellar ataxia.";
RL Am. J. Med. Genet. A 179:1575-1579(2019).
RN [12]
RP VARIANT PRO-294.
RX PubMed=30214071; DOI=10.1038/s41436-018-0140-3;
RA Shaheen R., Maddirevula S., Ewida N., Alsahli S., Abdel-Salam G.M.H.,
RA Zaki M.S., Tala S.A., Alhashem A., Softah A., Al-Owain M., Alazami A.M.,
RA Abadel B., Patel N., Al-Sheddi T., Alomar R., Alobeid E., Ibrahim N.,
RA Hashem M., Abdulwahab F., Hamad M., Tabarki B., Alwadei A.H., Alhazzani F.,
RA Bashiri F.A., Kentab A., Sahintuerk S., Sherr E., Fregeau B., Sogati S.,
RA Alshahwan S.A.M., Alkhalifi S., Alhumaidi Z., Temtamy S., Aglan M.,
RA Otaify G., Girisha K.M., Tulbah M., Seidahmed M.Z., Salih M.A.,
RA Abouelhoda M., Momin A.A., Saffar M.A., Partlow J.N., Arold S.T.,
RA Faqeih E., Walsh C., Alkuraya F.S.;
RT "Genomic and phenotypic delineation of congenital microcephaly.";
RL Genet. Med. 21:545-552(2019).
CC -!- FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and
CC RNase P cleavage. This step is essential for proper recognition of the
CC tRNA and for the fidelity of protein synthesis (Probable). Also
CC functions as a guanyl-nucleotide exchange factor/GEF for the MFN1 and
CC MFN2 mitofusins thereby regulating mitochondrial fusion
CC (PubMed:25008184, PubMed:27307223). By regulating both mitochondrial
CC dynamics and bioenergetic function, it contributes to cell survival
CC following oxidative stress (PubMed:25008184, PubMed:27307223).
CC {ECO:0000269|PubMed:25008184, ECO:0000269|PubMed:27307223,
CC ECO:0000305|PubMed:21059936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end ribonucleotide-tRNA(His) + ATP + GTP + H2O = a 5'-end
CC phospho-guanosine-ribonucleotide-tRNA(His) + AMP + 2 diphosphate +
CC H(+); Xref=Rhea:RHEA:54564, Rhea:RHEA-COMP:14193, Rhea:RHEA-
CC COMP:14917, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:141847, ChEBI:CHEBI:456215; EC=2.7.7.79;
CC Evidence={ECO:0000269|PubMed:21059936};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21059936};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:21059936};
CC -!- SUBUNIT: Homotetramer (PubMed:21059936). Interacts with MFN1 and MFN2;
CC functions as a guanyl-nucleotide exchange factor/GEF for MFN2 and also
CC probably MFN1 (PubMed:25008184). {ECO:0000269|PubMed:21059936,
CC ECO:0000269|PubMed:25008184}.
CC -!- INTERACTION:
CC Q9NWX6; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-746510, EBI-739832;
CC Q9NWX6; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-746510, EBI-741158;
CC Q9NWX6; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-746510, EBI-742388;
CC Q9NWX6; O00560: SDCBP; NbExp=3; IntAct=EBI-746510, EBI-727004;
CC Q9NWX6; P54274: TERF1; NbExp=2; IntAct=EBI-746510, EBI-710997;
CC Q9NWX6; Q9NWX6: THG1L; NbExp=4; IntAct=EBI-746510, EBI-746510;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15459185}.
CC Mitochondrion outer membrane {ECO:0000305|PubMed:25008184}.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues.
CC {ECO:0000269|PubMed:15459185}.
CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 28 (SCAR28)
CC [MIM:618800]: A form of spinocerebellar ataxia, a clinically and
CC genetically heterogeneous group of cerebellar disorders due to
CC degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCAR28 patients manifest mild motor
CC developmental delay, gait ataxia, and dysarthria. Some patients show
CC mildly impaired intellectual development. Disease onset is in early
CC childhood. {ECO:0000269|PubMed:27307223, ECO:0000269|PubMed:31168944}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01523.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH01852.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY463216; AAS21134.1; -; mRNA.
DR EMBL; AL136669; CAB66604.1; -; mRNA.
DR EMBL; AK000553; BAA91249.1; -; mRNA.
DR EMBL; AK021663; BAB13870.1; -; mRNA.
DR EMBL; CR533503; CAG38534.1; -; mRNA.
DR EMBL; AK223119; BAD96839.1; -; mRNA.
DR EMBL; CH471062; EAW61590.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61591.1; -; Genomic_DNA.
DR EMBL; BC001523; AAH01523.2; ALT_INIT; mRNA.
DR EMBL; BC001852; AAH01852.2; ALT_INIT; mRNA.
DR EMBL; BC023521; AAH23521.1; -; mRNA.
DR CCDS; CCDS4341.1; -.
DR RefSeq; NP_001304753.1; NM_001317824.1.
DR RefSeq; NP_001304754.1; NM_001317825.1.
DR RefSeq; NP_001304755.1; NM_001317826.1.
DR RefSeq; NP_060342.2; NM_017872.4.
DR PDB; 3OTB; X-ray; 2.95 A; A/B=30-298.
DR PDB; 3OTC; X-ray; 3.01 A; A/B=30-298.
DR PDB; 3OTD; X-ray; 2.28 A; A/B=30-298.
DR PDB; 3OTE; X-ray; 2.56 A; A/B=30-298.
DR PDB; 7CV1; X-ray; 4.00 A; A/B/C/D=30-298.
DR PDBsum; 3OTB; -.
DR PDBsum; 3OTC; -.
DR PDBsum; 3OTD; -.
DR PDBsum; 3OTE; -.
DR PDBsum; 7CV1; -.
DR AlphaFoldDB; Q9NWX6; -.
DR SMR; Q9NWX6; -.
DR BioGRID; 120311; 56.
DR DIP; DIP-59479N; -.
DR IntAct; Q9NWX6; 15.
DR MINT; Q9NWX6; -.
DR STRING; 9606.ENSP00000231198; -.
DR iPTMnet; Q9NWX6; -.
DR PhosphoSitePlus; Q9NWX6; -.
DR BioMuta; THG1L; -.
DR DMDM; 146325755; -.
DR EPD; Q9NWX6; -.
DR jPOST; Q9NWX6; -.
DR MassIVE; Q9NWX6; -.
DR MaxQB; Q9NWX6; -.
DR PaxDb; Q9NWX6; -.
DR PeptideAtlas; Q9NWX6; -.
DR PRIDE; Q9NWX6; -.
DR ProteomicsDB; 82998; -.
DR Antibodypedia; 28457; 92 antibodies from 23 providers.
DR DNASU; 54974; -.
DR Ensembl; ENST00000231198.12; ENSP00000231198.7; ENSG00000113272.14.
DR GeneID; 54974; -.
DR KEGG; hsa:54974; -.
DR MANE-Select; ENST00000231198.12; ENSP00000231198.7; NM_017872.5; NP_060342.2.
DR UCSC; uc003lxd.4; human.
DR CTD; 54974; -.
DR DisGeNET; 54974; -.
DR GeneCards; THG1L; -.
DR HGNC; HGNC:26053; THG1L.
DR HPA; ENSG00000113272; Low tissue specificity.
DR MalaCards; THG1L; -.
DR MIM; 618800; phenotype.
DR MIM; 618802; gene.
DR neXtProt; NX_Q9NWX6; -.
DR OpenTargets; ENSG00000113272; -.
DR PharmGKB; PA162405691; -.
DR VEuPathDB; HostDB:ENSG00000113272; -.
DR eggNOG; KOG2721; Eukaryota.
DR GeneTree; ENSGT00390000011705; -.
DR HOGENOM; CLU_044271_0_0_1; -.
DR InParanoid; Q9NWX6; -.
DR OMA; WKQHTEI; -.
DR OrthoDB; 1152974at2759; -.
DR PhylomeDB; Q9NWX6; -.
DR TreeFam; TF325119; -.
DR BRENDA; 2.7.7.79; 2681.
DR PathwayCommons; Q9NWX6; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q9NWX6; -.
DR BioGRID-ORCS; 54974; 578 hits in 1087 CRISPR screens.
DR ChiTaRS; THG1L; human.
DR EvolutionaryTrace; Q9NWX6; -.
DR GeneWiki; THG1L; -.
DR GenomeRNAi; 54974; -.
DR Pharos; Q9NWX6; Tbio.
DR PRO; PR:Q9NWX6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NWX6; protein.
DR Bgee; ENSG00000113272; Expressed in monocyte and 149 other tissues.
DR ExpressionAtlas; Q9NWX6; baseline and differential.
DR Genevisible; Q9NWX6; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:1990234; C:transferase complex; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IDA:BHF-UCL.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:BHF-UCL.
DR GO; GO:0016779; F:nucleotidyltransferase activity; EXP:Reactome.
DR GO; GO:0000049; F:tRNA binding; TAS:BHF-UCL.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR GO; GO:1990046; P:stress-induced mitochondrial fusion; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IDA:UniProtKB.
DR Gene3D; 3.30.70.3000; -; 1.
DR InterPro; IPR025845; Thg1_C_dom.
DR InterPro; IPR024956; tRNAHis_GuaTrfase_cat.
DR InterPro; IPR007537; tRNAHis_GuaTrfase_Thg1.
DR InterPro; IPR038469; tRNAHis_GuaTrfase_Thg1_sf.
DR PANTHER; PTHR12729; PTHR12729; 1.
DR Pfam; PF04446; Thg1; 1.
DR Pfam; PF14413; Thg1C; 1.
DR PIRSF; PIRSF028980; tRNAHis_guanylyltransferase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; GTP-binding; Magnesium; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Neurodegeneration; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..298
FT /note="Probable tRNA(His) guanylyltransferase"
FT /id="PRO_0000284984"
FT BINDING 58..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21059936"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21059936"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21059936"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21059936"
FT BINDING 104..105
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21059936"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21059936"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21059936"
FT VARIANT 55
FT /note="V -> A (in SCAR28; decreased mitochondrial fusion;
FT dbSNP:rs201920319)"
FT /evidence="ECO:0000269|PubMed:27307223,
FT ECO:0000269|PubMed:31168944"
FT /id="VAR_083901"
FT VARIANT 232
FT /note="L -> P (in dbSNP:rs2270812)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT /id="VAR_031871"
FT VARIANT 294
FT /note="L -> P (found in a patient with a severe
FT multisystemic growth disorder and cerebellar atrophy;
FT unknown pathological significance; dbSNP:rs1581444231)"
FT /evidence="ECO:0000269|PubMed:30214071"
FT /id="VAR_083902"
FT MUTAGEN 58
FT /note="D->A: Reduces activity by 99.5%."
FT /evidence="ECO:0000269|PubMed:21059936"
FT MUTAGEN 63
FT /note="H->A: Slightly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21059936"
FT MUTAGEN 104
FT /note="S->A: Slightly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21059936"
FT MUTAGEN 105
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21059936"
FT MUTAGEN 106
FT /note="E->A: Reduces activity by 95%."
FT /evidence="ECO:0000269|PubMed:21059936"
FT MUTAGEN 127
FT /note="T->A: Abolishes oligomerization. Loss of enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:21059936"
FT MUTAGEN 181
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21059936"
FT MUTAGEN 216
FT /note="K->A: Reduces activity by 98.5%."
FT /evidence="ECO:0000269|PubMed:21059936"
FT MUTAGEN 227
FT /note="N->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21059936"
FT CONFLICT 57
FT /note="L -> Q (in Ref. 5; BAD96839)"
FT /evidence="ECO:0000305"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:3OTD"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:3OTD"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:3OTD"
FT HELIX 77..93
FT /evidence="ECO:0007829|PDB:3OTD"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:3OTD"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3OTD"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:3OTD"
FT HELIX 122..139
FT /evidence="ECO:0007829|PDB:3OTD"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3OTD"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3OTD"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:3OTD"
FT HELIX 166..195
FT /evidence="ECO:0007829|PDB:3OTD"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:3OTD"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:3OTD"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3OTD"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:3OTD"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3OTD"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:3OTD"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3OTB"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:3OTD"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:3OTD"
SQ SEQUENCE 298 AA; 34831 MW; A6C941B75611C448 CRC64;
MWGACKVKVH DSLATISITL RRYLRLGATM AKSKFEYVRD FEADDTCLAH CWVVVRLDGR
NFHRFAEKHN FAKPNDSRAL QLMTKCAQTV MEELEDIVIA YGQSDEYSFV FKRKTNWFKR
RASKFMTHVA SQFASSYVFY WRDYFEDQPL LYPPGFDGRV VVYPSNQTLK DYLSWRQADC
HINNLYNTVF WALIQQSGLT PVQAQGRLQG TLAADKNEIL FSEFNINYNN ELPMYRKGTV
LIWQKVDEVM TKEIKLPTEM EGKKMAVTRT RTKPVPLHCD IIGDAFWKEH PEILDEDS
