GATA_HUMAN
ID GATA_HUMAN Reviewed; 528 AA.
AC Q9H0R6; Q5VWJ4; Q9HA60; Q9NV19;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03150};
DE Short=Glu-AdT subunit A {ECO:0000255|HAMAP-Rule:MF_03150};
DE EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_03150};
DE AltName: Full=Glutaminyl-tRNA synthase-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03150};
GN Name=QRSL1 {ECO:0000255|HAMAP-Rule:MF_03150};
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] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland, and Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Uterus;
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 [6]
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 [7]
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 [8]
RP INVOLVEMENT IN COXPD40, VARIANTS COXPD40 GLU-117 AND VAL-133, AND
RP CHARACTERIZATION OF VARIANTS COXPD40 GLU-117 AND VAL-133.
RX PubMed=26741492; DOI=10.1371/journal.pgen.1005679;
RA Kohda M., Tokuzawa Y., Kishita Y., Nyuzuki H., Moriyama Y., Mizuno Y.,
RA Hirata T., Yatsuka Y., Yamashita-Sugahara Y., Nakachi Y., Kato H.,
RA Okuda A., Tamaru S., Borna N.N., Banshoya K., Aigaki T., Sato-Miyata Y.,
RA Ohnuma K., Suzuki T., Nagao A., Maehata H., Matsuda F., Higasa K.,
RA Nagasaki M., Yasuda J., Yamamoto M., Fushimi T., Shimura M.,
RA Kaiho-Ichimoto K., Harashima H., Yamazaki T., Mori M., Murayama K.,
RA Ohtake A., Okazaki Y.;
RT "A comprehensive genomic analysis reveals the genetic landscape of
RT mitochondrial respiratory chain complex deficiencies.";
RL PLoS Genet. 12:E1005679-E1005679(2016).
RN [9]
RP VARIANTS COXPD40 VAL-133; 185-TYR--GLN-528 DEL; 196-THR--PRO-199 DELINS
RP ASN-LYS-ASN-HIS AND LEU-427.
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_03150, 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; EC=6.3.5.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03150};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits.
CC -!- INTERACTION:
CC Q9H0R6; O75879: GATB; NbExp=2; IntAct=EBI-2856796, EBI-6137441;
CC Q9H0R6; O43716: GATC; NbExp=3; IntAct=EBI-2856796, EBI-6929453;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150,
CC ECO:0000269|PubMed:19805282}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0R6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0R6-2; Sequence=VSP_030773, VSP_030774;
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 40 (COXPD40)
CC [MIM:618835]: An autosomal recessive mitochondrial disorder
CC characterized by prenatal or infantile onset, fetal hydrops, severe
CC hypertrophic cardiomyopathy, poor growth, sensorineural hearing loss,
CC hepatic dysfunction, lactic acidosis, and decreased activities of
CC mitochondrial respiratory complexes I, III, IV, and V. The disorder is
CC lethal, with death occurring in infancy. {ECO:0000269|PubMed:26741492,
CC ECO:0000269|PubMed:30283131}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03150}.
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DR EMBL; AL136679; CAB66614.1; -; mRNA.
DR EMBL; AK001851; BAA91941.1; -; mRNA.
DR EMBL; AK022251; BAB13996.1; -; mRNA.
DR EMBL; AK023509; BAB14592.1; -; mRNA.
DR EMBL; AL390074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48407.1; -; Genomic_DNA.
DR EMBL; BC006084; AAH06084.1; -; mRNA.
DR EMBL; BC014389; AAH14389.1; -; mRNA.
DR CCDS; CCDS5057.1; -. [Q9H0R6-1]
DR RefSeq; NP_060762.3; NM_018292.4. [Q9H0R6-1]
DR AlphaFoldDB; Q9H0R6; -.
DR SMR; Q9H0R6; -.
DR BioGRID; 120566; 115.
DR ComplexPortal; CPX-6174; Mitochondrial glutamyl-tRNA(Gln) amidotransferase complex.
DR CORUM; Q9H0R6; -.
DR DIP; DIP-48970N; -.
DR IntAct; Q9H0R6; 16.
DR MINT; Q9H0R6; -.
DR STRING; 9606.ENSP00000358042; -.
DR iPTMnet; Q9H0R6; -.
DR MetOSite; Q9H0R6; -.
DR PhosphoSitePlus; Q9H0R6; -.
DR BioMuta; QRSL1; -.
DR DMDM; 167016573; -.
DR EPD; Q9H0R6; -.
DR jPOST; Q9H0R6; -.
DR MassIVE; Q9H0R6; -.
DR MaxQB; Q9H0R6; -.
DR PaxDb; Q9H0R6; -.
DR PeptideAtlas; Q9H0R6; -.
DR PRIDE; Q9H0R6; -.
DR ProteomicsDB; 80319; -. [Q9H0R6-1]
DR ProteomicsDB; 80320; -. [Q9H0R6-2]
DR Antibodypedia; 32156; 157 antibodies from 23 providers.
DR DNASU; 55278; -.
DR Ensembl; ENST00000369046.8; ENSP00000358042.4; ENSG00000130348.11. [Q9H0R6-1]
DR GeneID; 55278; -.
DR KEGG; hsa:55278; -.
DR MANE-Select; ENST00000369046.8; ENSP00000358042.4; NM_018292.5; NP_060762.3.
DR UCSC; uc003prm.4; human. [Q9H0R6-1]
DR CTD; 55278; -.
DR DisGeNET; 55278; -.
DR GeneCards; QRSL1; -.
DR HGNC; HGNC:21020; QRSL1.
DR HPA; ENSG00000130348; Low tissue specificity.
DR MalaCards; QRSL1; -.
DR MIM; 617209; gene.
DR MIM; 618835; phenotype.
DR neXtProt; NX_Q9H0R6; -.
DR OpenTargets; ENSG00000130348; -.
DR Orphanet; 570491; QRSL1-related combined oxidative phosphorylation defect.
DR PharmGKB; PA128394680; -.
DR VEuPathDB; HostDB:ENSG00000130348; -.
DR eggNOG; KOG1211; Eukaryota.
DR GeneTree; ENSGT00550000074866; -.
DR HOGENOM; CLU_009600_7_6_1; -.
DR InParanoid; Q9H0R6; -.
DR OMA; EVSCPHF; -.
DR OrthoDB; 1195292at2759; -.
DR PhylomeDB; Q9H0R6; -.
DR TreeFam; TF313766; -.
DR BRENDA; 6.3.5.7; 2681.
DR PathwayCommons; Q9H0R6; -.
DR SignaLink; Q9H0R6; -.
DR BioGRID-ORCS; 55278; 400 hits in 1079 CRISPR screens.
DR ChiTaRS; QRSL1; human.
DR GenomeRNAi; 55278; -.
DR Pharos; Q9H0R6; Tbio.
DR PRO; PR:Q9H0R6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9H0R6; protein.
DR Bgee; ENSG00000130348; Expressed in forelimb stylopod muscle and 195 other tissues.
DR ExpressionAtlas; Q9H0R6; baseline and differential.
DR Genevisible; Q9H0R6; 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:0031647; P:regulation of protein stability; IEA:Ensembl.
DR Gene3D; 3.90.1300.10; -; 1.
DR HAMAP; MF_00120; GatA; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR004412; GatA.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR TIGRFAMs; TIGR00132; gatA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Disease variant; Ligase; Mitochondrion;
KW Nucleotide-binding; Primary mitochondrial disease; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..528
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT mitochondrial"
FT /id="PRO_0000316767"
FT REGION 148..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 195
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT VAR_SEQ 284..304
FT /note="EYLVPELSSEVQSLWSKAADL -> VTFSFHYFTEILSSPIESTD (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030773"
FT VAR_SEQ 305..528
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030774"
FT VARIANT 11
FT /note="A -> V (in dbSNP:rs36016898)"
FT /id="VAR_038389"
FT VARIANT 117
FT /note="G -> E (in COXPD40; highly decreased glutaminyl-
FT tRNAGln biosynthesis via transamidation)"
FT /evidence="ECO:0000269|PubMed:26741492"
FT /id="VAR_076270"
FT VARIANT 133
FT /note="G -> V (in COXPD40; highly decreased glutaminyl-
FT tRNAGln biosynthesis via transamidation;
FT dbSNP:rs1562168768)"
FT /evidence="ECO:0000269|PubMed:26741492,
FT ECO:0000269|PubMed:30283131"
FT /id="VAR_076271"
FT VARIANT 185..528
FT /note="Missing (in COXPD40)"
FT /evidence="ECO:0000269|PubMed:30283131"
FT /id="VAR_083983"
FT VARIANT 196..199
FT /note="TRNP -> NKNH (in COXPD40; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30283131"
FT /id="VAR_083984"
FT VARIANT 263
FT /note="N -> S (in dbSNP:rs34221917)"
FT /id="VAR_038390"
FT VARIANT 427
FT /note="A -> L (in COXPD40; requires 2 nucleotide
FT substitutions; unknown pathological significance;
FT dbSNP:rs1562173313)"
FT /evidence="ECO:0000269|PubMed:30283131"
FT /id="VAR_083985"
FT CONFLICT 34
FT /note="T -> A (in Ref. 1; CAB66614)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="Q -> R (in Ref. 1; CAB66614)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="S -> P (in Ref. 1; CAB66614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 57460 MW; 06E21A7D17A6E963 CRC64;
MLGRSLREVS AALKQGQITP TELCQKCLSL IKKTKFLNAY ITVSEEVALK QAEESEKRYK
NGQSLGDLDG IPIAVKDNFS TSGIETTCAS NMLKGYIPPY NATVVQKLLD QGALLMGKTN
LDEFAMGSGS TDGVFGPVKN PWSYSKQYRE KRKQNPHSEN EDSDWLITGG SSGGSAAAVS
AFTCYAALGS DTGGSTRNPA AHCGLVGFKP SYGLVSRHGL IPLVNSMDVP GILTRCVDDA
AIVLGALAGP DPRDSTTVHE PINKPFMLPS LADVSKLCIG IPKEYLVPEL SSEVQSLWSK
AADLFESEGA KVIEVSLPHT SYSIVCYHVL CTSEVASNMA RFDGLQYGHR CDIDVSTEAM
YAATRREGFN DVVRGRILSG NFFLLKENYE NYFVKAQKVR RLIANDFVNA FNSGVDVLLT
PTTLSEAVPY LEFIKEDNRT RSAQDDIFTQ AVNMAGLPAV SIPVALSNQG LPIGLQFIGR
AFCDQQLLTV AKWFEKQVQF PVIQLQELMD DCSAVLENEK LASVSLKQ
