SYEM_HUMAN
ID SYEM_HUMAN Reviewed; 523 AA.
AC Q5JPH6; B3KTT2; D3DWF1; Q86YH3; Q8TF31;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable glutamate--tRNA ligase, mitochondrial;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase;
DE Short=GluRS;
DE Flags: Precursor;
GN Name=EARS2; Synonyms=KIAA1970;
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), AND VARIANT GLY-457.
RC TISSUE=Kidney;
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 MRNA] (ISOFORM 1), AND VARIANT GLY-457.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-457.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-523 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [6]
RP IDENTIFICATION.
RX PubMed=15779907; DOI=10.1021/bi047527z;
RA Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C.,
RA Sissler M.;
RT "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases:
RT characterization of AspRS and TyrRS.";
RL Biochemistry 44:4805-4816(2005).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP VARIANTS COXPD12 HIS-55; LYS-96; HIS-107; TRP-108; SER-110; TYR-167;
RP GLY-168; SER-204; SER-224; CYS-317; 426-THR-ARG-427 DELINS LEU AND GLN-516.
RX PubMed=22492562; DOI=10.1093/brain/aws070;
RA Steenweg M.E., Ghezzi D., Haack T., Abbink T.E., Martinelli D.,
RA van Berkel C.G., Bley A., Diogo L., Grillo E., Te Water Naude J.,
RA Strom T.M., Bertini E., Prokisch H., van der Knaap M.S., Zeviani M.;
RT "Leukoencephalopathy with thalamus and brainstem involvement and high
RT lactate 'LTBL' caused by EARS2 mutations.";
RL Brain 135:1387-1394(2012).
RN [12]
RP VARIANT COXPD12 GLU-65.
RX PubMed=23008233; DOI=10.1093/brain/aws197;
RA Talim B., Pyle A., Griffin H., Topaloglu H., Tokatli A., Keogh M.J.,
RA Santibanez-Koref M., Chinnery P.F., Horvath R.;
RT "Multisystem fatal infantile disease caused by a novel homozygous EARS2
RT mutation.";
RL Brain 136:E228-E228(2013).
RN [13]
RP VARIANTS COXPD12 CYS-107 AND GLN-489.
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).
CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC then transferred to the acceptor end of tRNA(Glu). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; EC=6.1.1.17;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5JPH6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JPH6-2; Sequence=VSP_057203;
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 12 (COXPD12)
CC [MIM:614924]: An autosomal recessive, mitochondrial, neurologic
CC disorder characterized by onset in infancy of hypotonia and delayed
CC psychomotor development, or early developmental regression, associated
CC with T2-weighted hyperintensities in the deep cerebral white matter,
CC brainstem, and cerebellar white matter. Serum lactate is increased due
CC to a defect in mitochondrial respiration. There are 2 main phenotypic
CC groups: those with a milder disease course and some recovery of skills
CC after age 2 years, and those with a severe disease course resulting in
CC marked disability. {ECO:0000269|PubMed:22492562,
CC ECO:0000269|PubMed:23008233, ECO:0000269|PubMed:26741492}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily. {ECO:0000305}.
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DR EMBL; AK095998; BAG53194.1; -; mRNA.
DR EMBL; AL832489; CAI46121.1; -; mRNA.
DR EMBL; CH471145; EAW55822.1; -; Genomic_DNA.
DR EMBL; CH471145; EAW55824.1; -; Genomic_DNA.
DR EMBL; BC040013; AAH40013.1; -; mRNA.
DR EMBL; AB075850; BAB85556.1; -; mRNA.
DR CCDS; CCDS42132.1; -. [Q5JPH6-1]
DR CCDS; CCDS76844.1; -. [Q5JPH6-2]
DR RefSeq; NP_001077083.1; NM_001083614.1. [Q5JPH6-1]
DR RefSeq; NP_001295140.1; NM_001308211.1. [Q5JPH6-2]
DR AlphaFoldDB; Q5JPH6; -.
DR SMR; Q5JPH6; -.
DR BioGRID; 125866; 136.
DR IntAct; Q5JPH6; 8.
DR MINT; Q5JPH6; -.
DR STRING; 9606.ENSP00000395196; -.
DR DrugBank; DB00142; Glutamic acid.
DR iPTMnet; Q5JPH6; -.
DR PhosphoSitePlus; Q5JPH6; -.
DR BioMuta; EARS2; -.
DR DMDM; 117949790; -.
DR EPD; Q5JPH6; -.
DR jPOST; Q5JPH6; -.
DR MassIVE; Q5JPH6; -.
DR MaxQB; Q5JPH6; -.
DR PaxDb; Q5JPH6; -.
DR PeptideAtlas; Q5JPH6; -.
DR PRIDE; Q5JPH6; -.
DR ProteomicsDB; 63015; -. [Q5JPH6-1]
DR Antibodypedia; 25969; 129 antibodies from 22 providers.
DR DNASU; 124454; -.
DR Ensembl; ENST00000449606.7; ENSP00000395196.2; ENSG00000103356.18. [Q5JPH6-1]
DR Ensembl; ENST00000563232.1; ENSP00000456218.1; ENSG00000103356.18. [Q5JPH6-2]
DR Ensembl; ENST00000674054.1; ENSP00000501251.1; ENSG00000103356.18. [Q5JPH6-1]
DR GeneID; 124454; -.
DR KEGG; hsa:124454; -.
DR MANE-Select; ENST00000449606.7; ENSP00000395196.2; NM_001083614.2; NP_001077083.1.
DR UCSC; uc002dlt.5; human. [Q5JPH6-1]
DR CTD; 124454; -.
DR DisGeNET; 124454; -.
DR GeneCards; EARS2; -.
DR HGNC; HGNC:29419; EARS2.
DR HPA; ENSG00000103356; Low tissue specificity.
DR MalaCards; EARS2; -.
DR MIM; 612799; gene.
DR MIM; 614924; phenotype.
DR neXtProt; NX_Q5JPH6; -.
DR OpenTargets; ENSG00000103356; -.
DR Orphanet; 314051; Leukoencephalopathy-thalamus and brainstem anomalies-high lactate syndrome.
DR PharmGKB; PA144596439; -.
DR VEuPathDB; HostDB:ENSG00000103356; -.
DR eggNOG; KOG1149; Eukaryota.
DR GeneTree; ENSGT00390000009759; -.
DR HOGENOM; CLU_015768_6_3_1; -.
DR InParanoid; Q5JPH6; -.
DR OMA; WDEGPFF; -.
DR OrthoDB; 879920at2759; -.
DR PhylomeDB; Q5JPH6; -.
DR TreeFam; TF313268; -.
DR PathwayCommons; Q5JPH6; -.
DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
DR SignaLink; Q5JPH6; -.
DR BioGRID-ORCS; 124454; 357 hits in 1083 CRISPR screens.
DR ChiTaRS; EARS2; human.
DR GenomeRNAi; 124454; -.
DR Pharos; Q5JPH6; Tbio.
DR PRO; PR:Q5JPH6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q5JPH6; protein.
DR Bgee; ENSG00000103356; Expressed in adrenal tissue and 162 other tissues.
DR ExpressionAtlas; Q5JPH6; baseline and differential.
DR Genevisible; Q5JPH6; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0050561; F:glutamate-tRNA(Gln) ligase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IDA:UniProtKB.
DR GO; GO:0070127; P:tRNA aminoacylation for mitochondrial protein translation; IDA:UniProtKB.
DR CDD; cd00808; GluRS_core; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR033910; GluRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00464; gltX_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding;
KW Disease variant; Ligase; Mitochondrion; Nucleotide-binding;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..523
FT /note="Probable glutamate--tRNA ligase, mitochondrial"
FT /id="PRO_0000254560"
FT MOTIF 45..53
FT /note="'HIGH' region"
FT MOTIF 284..288
FT /note="'KMSKS' region"
FT BINDING 40..42
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 228..232
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 284..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 256
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CXJ1"
FT MOD_RES 486
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 497..523
FT /note="QGPPVAEMMLALGPKEVRERIQKVVSS -> VRQGHGLDCSLEPLIDPLNLH
FT FLAGTELNIEYTKVNET (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057203"
FT VARIANT 55
FT /note="R -> H (in COXPD12; dbSNP:rs770862902)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069235"
FT VARIANT 65
FT /note="K -> E (in COXPD12; dbSNP:rs397514595)"
FT /evidence="ECO:0000269|PubMed:23008233"
FT /id="VAR_069236"
FT VARIANT 96
FT /note="E -> K (in COXPD12; dbSNP:rs397514593)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069237"
FT VARIANT 107
FT /note="R -> C (in COXPD12; dbSNP:rs1355685453)"
FT /evidence="ECO:0000269|PubMed:26741492"
FT /id="VAR_076183"
FT VARIANT 107
FT /note="R -> H (in COXPD12; dbSNP:rs1021330566)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069238"
FT VARIANT 108
FT /note="R -> W (in COXPD12; dbSNP:rs376103091)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069239"
FT VARIANT 110
FT /note="G -> S (in COXPD12; dbSNP:rs201842633)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069240"
FT VARIANT 167
FT /note="C -> Y (in COXPD12; dbSNP:rs397514594)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069241"
FT VARIANT 168
FT /note="R -> G (in COXPD12; dbSNP:rs397514591)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069242"
FT VARIANT 204
FT /note="G -> S (in COXPD12; dbSNP:rs397514592)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069243"
FT VARIANT 224
FT /note="G -> S (in COXPD12; dbSNP:rs141129877)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069244"
FT VARIANT 317
FT /note="G -> C (in COXPD12; dbSNP:rs746838793)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069245"
FT VARIANT 426..427
FT /note="TR -> L (in COXPD12)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069246"
FT VARIANT 457
FT /note="S -> G (in dbSNP:rs6497671)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_028840"
FT VARIANT 489
FT /note="R -> Q (in COXPD12; dbSNP:rs757965573)"
FT /evidence="ECO:0000269|PubMed:26741492"
FT /id="VAR_076184"
FT VARIANT 516
FT /note="R -> Q (in COXPD12; dbSNP:rs201727231)"
FT /evidence="ECO:0000269|PubMed:22492562"
FT /id="VAR_069247"
SQ SEQUENCE 523 AA; 58689 MW; FA9B19569AD9F5DB CRC64;
MAALLRRLLQ RERPSAASGR PVGRREANLG TDAGVAVRVR FAPSPTGFLH LGGLRTALYN
YIFAKKYQGS FILRLEDTDQ TRVVPGAAEN IEDMLEWAGI PPDESPRRGG PAGPYQQSQR
LELYAQATEA LLKTGAAYPC FCSPQRLELL KKEALRNHQT PRYDNRCRNM SQEQVAQKLA
KDPKPAIRFR LEQVVPAFQD LVYGWNRHEV ASVEGDPVIM KSDGFPTYHL ACVVDDHHMG
ISHVLRGSEW LVSTAKHLLL YQALGWQPPH FAHLPLLLNR DGSKLSKRQG DVFLEHFAAD
GFLPDSLLDI ITNCGSGFAE NQMGRTLPEL ITQFNLTQVT CHSALLDLEK LPEFNRLHLQ
RLVSNESQRR QLVGKLQVLV EEAFGCQLQN RDVLNPVYVE RILLLRQGHI CRLQDLVSPV
YSYLWTRPAV GRAQLDAISE KVDVIAKRVL GLLERSSMSL TQDMLNGELK KLSEGLEGTK
YSNVMKLLRM ALSGQQQGPP VAEMMLALGP KEVRERIQKV VSS
