GATC_HUMAN
ID GATC_HUMAN Reviewed; 136 AA.
AC O43716; B3KSU7; Q3B824; Q3KNR8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03149};
DE Short=Glu-AdT subunit C {ECO:0000255|HAMAP-Rule:MF_03149};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03149};
DE AltName: Full=Protein 15E1.2;
GN Name=GATC {ECO:0000255|HAMAP-Rule:MF_03149}; Synonyms=15E1.2;
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 [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19805282; DOI=10.1073/pnas.0907602106;
RA Nagao A., Suzuki T., Katoh T., Sakaguchi Y., Suzuki T.;
RT "Biogenesis of glutaminyl-mt tRNAGln in human mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16209-16214(2009).
RN [5]
RP INVOLVEMENT IN COXPD42, AND VARIANT COXPD42 ARG-78.
RX PubMed=30283131; DOI=10.1038/s41467-018-06250-w;
RA Friederich M.W., Timal S., Powell C.A., Dallabona C., Kurolap A.,
RA Palacios-Zambrano S., Bratkovic D., Derks T.G.J., Bick D., Bouman K.,
RA Chatfield K.C., Damouny-Naoum N., Dishop M.K., Falik-Zaccai T.C., Fares F.,
RA Fedida A., Ferrero I., Gallagher R.C., Garesse R., Gilberti M.,
RA Gonzalez C., Gowan K., Habib C., Halligan R.K., Kalfon L., Knight K.,
RA Lefeber D., Mamblona L., Mandel H., Mory A., Ottoson J., Paperna T.,
RA Pruijn G.J.M., Rebelo-Guiomar P.F., Saada A., Sainz B. Jr., Salvemini H.,
RA Schoots M.H., Smeitink J.A., Szukszto M.J., Ter Horst H.J.,
RA van den Brandt F., van Spronsen F.J., Veltman J.A., Wartchow E.,
RA Wintjes L.T., Zohar Y., Fernandez-Moreno M.A., Baris H.N., Donnini C.,
RA Minczuk M., Rodenburg R.J., Van Hove J.L.K.;
RT "Pathogenic variants in glutamyl-tRNAGln amidotransferase subunits cause a
RT lethal mitochondrial cardiomyopathy disorder.";
RL Nat. Commun. 9:4065-4065(2018).
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in the
CC mitochondria. The reaction takes place in the presence of glutamine and
CC ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC {ECO:0000255|HAMAP-Rule:MF_03149, ECO:0000269|PubMed:19805282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03149};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits.
CC -!- INTERACTION:
CC O43716; P09917: ALOX5; NbExp=6; IntAct=EBI-6929453, EBI-79934;
CC O43716; P78358: CTAG1B; NbExp=3; IntAct=EBI-6929453, EBI-1188472;
CC O43716; O14964: HGS; NbExp=3; IntAct=EBI-6929453, EBI-740220;
CC O43716; Q9H0R6: QRSL1; NbExp=3; IntAct=EBI-6929453, EBI-2856796;
CC O43716; Q05519: SRSF11; NbExp=3; IntAct=EBI-6929453, EBI-1051785;
CC O43716; Q05519-2: SRSF11; NbExp=6; IntAct=EBI-6929453, EBI-11975029;
CC O43716; Q6UXN7: TOMM20L; NbExp=3; IntAct=EBI-6929453, EBI-11954062;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03149,
CC ECO:0000269|PubMed:19805282}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 42 (COXPD42)
CC [MIM:618839]: An autosomal recessive mitochondrial disorder
CC characterized by onset in the first months of life, cardiomyopathy,
CC respiratory insufficiency, lactic acidosis, anemia, and variable
CC impairment of mitochondrial respiratory complexes I, III, and IV. Death
CC occurs in infancy. {ECO:0000269|PubMed:30283131}. Note=The disease is
CC caused by variants 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_03149}.
CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC Rule:MF_03149}.
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DR EMBL; AK094319; BAG52859.1; -; mRNA.
DR EMBL; AL021546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC107145; AAI07146.1; -; mRNA.
DR EMBL; BC107146; AAI07147.1; -; mRNA.
DR CCDS; CCDS31911.1; -.
DR PIR; T09477; T09477.
DR RefSeq; NP_789788.1; NM_176818.2.
DR AlphaFoldDB; O43716; -.
DR BioGRID; 129569; 59.
DR ComplexPortal; CPX-6174; Mitochondrial glutamyl-tRNA(Gln) amidotransferase complex.
DR CORUM; O43716; -.
DR DIP; DIP-48969N; -.
DR IntAct; O43716; 31.
DR MINT; O43716; -.
DR STRING; 9606.ENSP00000446872; -.
DR GlyGen; O43716; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43716; -.
DR MetOSite; O43716; -.
DR PhosphoSitePlus; O43716; -.
DR BioMuta; GATC; -.
DR EPD; O43716; -.
DR jPOST; O43716; -.
DR MassIVE; O43716; -.
DR MaxQB; O43716; -.
DR PaxDb; O43716; -.
DR PeptideAtlas; O43716; -.
DR PRIDE; O43716; -.
DR ProteomicsDB; 49132; -.
DR Antibodypedia; 56388; 57 antibodies from 18 providers.
DR DNASU; 283459; -.
DR Ensembl; ENST00000551765.6; ENSP00000446872.1; ENSG00000257218.6.
DR GeneID; 283459; -.
DR KEGG; hsa:283459; -.
DR MANE-Select; ENST00000551765.6; ENSP00000446872.1; NM_176818.3; NP_789788.1.
DR UCSC; uc010szi.3; human.
DR CTD; 283459; -.
DR DisGeNET; 283459; -.
DR GeneCards; GATC; -.
DR HGNC; HGNC:25068; GATC.
DR HPA; ENSG00000257218; Low tissue specificity.
DR MalaCards; GATC; -.
DR MIM; 618839; phenotype.
DR neXtProt; NX_O43716; -.
DR OpenTargets; ENSG00000257218; -.
DR PharmGKB; PA162389278; -.
DR VEuPathDB; HostDB:ENSG00000257218; -.
DR eggNOG; KOG4247; Eukaryota.
DR GeneTree; ENSGT00390000018351; -.
DR HOGENOM; CLU_105899_0_2_1; -.
DR InParanoid; O43716; -.
DR OMA; HINTDHV; -.
DR OrthoDB; 1496962at2759; -.
DR PhylomeDB; O43716; -.
DR BRENDA; 6.3.5.7; 2681.
DR PathwayCommons; O43716; -.
DR SignaLink; O43716; -.
DR BioGRID-ORCS; 283459; 144 hits in 1073 CRISPR screens.
DR ChiTaRS; GATC; human.
DR GenomeRNAi; 283459; -.
DR Pharos; O43716; Tbio.
DR PRO; PR:O43716; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O43716; protein.
DR Bgee; ENSG00000257218; Expressed in tendon of biceps brachii and 186 other tissues.
DR ExpressionAtlas; O43716; baseline and differential.
DR Genevisible; O43716; HS.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IDA:UniProtKB.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IMP:UniProtKB.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR HAMAP; MF_00122; GatC; 1.
DR InterPro; IPR003837; Asp/Glu-ADT_csu.
DR InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR PANTHER; PTHR15004; PTHR15004; 1.
DR Pfam; PF02686; Glu-tRNAGln; 1.
DR SUPFAM; SSF141000; SSF141000; 1.
DR TIGRFAMs; TIGR00135; gatC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disease variant; Ligase; Mitochondrion; Nucleotide-binding;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome.
FT CHAIN 1..136
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C,
FT mitochondrial"
FT /id="PRO_0000105365"
FT VARIANT 3
FT /note="S -> L (in dbSNP:rs17431446)"
FT /id="VAR_049129"
FT VARIANT 78
FT /note="M -> R (in COXPD42; decreased protein abundance;
FT dbSNP:rs1370579526)"
FT /evidence="ECO:0000269|PubMed:30283131"
FT /id="VAR_083987"
SQ SEQUENCE 136 AA; 15086 MW; 113118E9507234E4 CRC64;
MWSRLVWLGL RAPLGGRQGF TSKADPQGSG RITAAVIEHL ERLALVDFGS REAVARLEKA
IAFADRLRAV DTDGVEPMES VLEDRCLYLR SDNVVEGNCA DELLQNSHRV VEEYFVAPPG
NISLPKLDEQ EPFPHS
