SYAM_HUMAN
ID SYAM_HUMAN Reviewed; 985 AA.
AC Q5JTZ9; A2RRN5; Q8N198; Q96D02; Q9ULF0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Alanine--tRNA ligase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03133};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03133};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
DE Flags: Precursor;
GN Name=AARS2 {ECO:0000255|HAMAP-Rule:MF_03133}; Synonyms=AARSL, KIAA1270;
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], AND VARIANT VAL-339.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-339.
RC TISSUE=Lung;
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 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 [5]
RP SUBCELLULAR LOCATION, AND VARIANTS COXPD8 ARG-155 AND TRP-592.
RX PubMed=21549344; DOI=10.1016/j.ajhg.2011.04.006;
RA Gotz A., Tyynismaa H., Euro L., Ellonen P., Hyotylainen T., Ojala T.,
RA Hamalainen R.H., Tommiska J., Raivio T., Oresic M., Karikoski R.,
RA Tammela O., Simola K.O., Paetau A., Tyni T., Suomalainen A.;
RT "Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations
RT in infantile mitochondrial cardiomyopathy.";
RL Am. J. Hum. Genet. 88:635-642(2011).
RN [6]
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 [7]
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 [8]
RP INVOLVEMENT IN LKENP, VARIANTS LKENP CYS-50; LYS-405 AND ARG-965, VARIANTS
RP VAL-77; PHE-131 DEL; CYS-199 AND MET-730, AND CHARACTERIZATION OF VARIANT
RP LKENP CYS-50.
RX PubMed=24808023; DOI=10.1212/wnl.0000000000000497;
RA Dallabona C., Diodato D., Kevelam S.H., Haack T.B., Wong L.J.,
RA Salomons G.S., Baruffini E., Melchionda L., Mariotti C., Strom T.M.,
RA Meitinger T., Prokisch H., Chapman K., Colley A., Rocha H., Ounap K.,
RA Schiffmann R., Salsano E., Savoiardo M., Hamilton E.M., Abbink T.E.,
RA Wolf N.I., Ferrero I., Lamperti C., Zeviani M., Vanderver A., Ghezzi D.,
RA van der Knaap M.S.;
RT "Novel (ovario) leukodystrophy related to AARS2 mutations.";
RL Neurology 82:2063-2071(2014).
RN [9]
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).
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged tRNA(Ala) via its editing domain.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03133};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- INTERACTION:
CC Q5JTZ9; Q08426: EHHADH; NbExp=3; IntAct=EBI-308736, EBI-2339219;
CC Q5JTZ9; Q15257-2: PTPA; NbExp=3; IntAct=EBI-308736, EBI-12164121;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03133,
CC ECO:0000269|PubMed:21549344}.
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 8 (COXPD8)
CC [MIM:614096]: A mitochondrial disease characterized by a lethal
CC infantile hypertrophic cardiomyopathy, generalized muscle dysfunction
CC and some neurologic involvement. The liver is not affected.
CC {ECO:0000269|PubMed:21549344}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Leukoencephalopathy, progressive, with ovarian failure (LKENP)
CC [MIM:615889]: An autosomal recessive neurodegenerative disorder
CC characterized by childhood- to adulthood-onset of signs of neurologic
CC deterioration consisting of ataxia, spasticity, and cognitive decline
CC with features of frontal lobe dysfunction. Brain MRI shows
CC leukoencephalopathy with striking involvement of deep white matter, and
CC cerebellar atrophy. All female patients develop premature ovarian
CC failure. {ECO:0000269|PubMed:24808023}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86584.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB033096; BAA86584.1; ALT_INIT; mRNA.
DR EMBL; AL353588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013593; AAH13593.1; -; mRNA.
DR EMBL; BC033169; AAH33169.1; -; mRNA.
DR EMBL; BC131728; AAI31729.1; -; mRNA.
DR CCDS; CCDS34464.1; -.
DR RefSeq; NP_065796.1; NM_020745.3.
DR PDB; 6NLQ; X-ray; 1.15 A; A/B/C/D=873-985.
DR PDB; 6NLY; X-ray; 2.31 A; A/B/C/D=802-985.
DR PDB; 6NOW; X-ray; 4.10 A; A/B=783-985.
DR PDBsum; 6NLQ; -.
DR PDBsum; 6NLY; -.
DR PDBsum; 6NOW; -.
DR AlphaFoldDB; Q5JTZ9; -.
DR SMR; Q5JTZ9; -.
DR BioGRID; 121569; 317.
DR IntAct; Q5JTZ9; 37.
DR MINT; Q5JTZ9; -.
DR STRING; 9606.ENSP00000244571; -.
DR DrugBank; DB00160; Alanine.
DR GlyGen; Q5JTZ9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5JTZ9; -.
DR PhosphoSitePlus; Q5JTZ9; -.
DR BioMuta; AARS2; -.
DR DMDM; 74742244; -.
DR EPD; Q5JTZ9; -.
DR jPOST; Q5JTZ9; -.
DR MassIVE; Q5JTZ9; -.
DR MaxQB; Q5JTZ9; -.
DR PaxDb; Q5JTZ9; -.
DR PeptideAtlas; Q5JTZ9; -.
DR PRIDE; Q5JTZ9; -.
DR ProteomicsDB; 63245; -.
DR TopDownProteomics; Q5JTZ9; -.
DR Antibodypedia; 46060; 137 antibodies from 28 providers.
DR DNASU; 57505; -.
DR Ensembl; ENST00000244571.5; ENSP00000244571.4; ENSG00000124608.5.
DR GeneID; 57505; -.
DR KEGG; hsa:57505; -.
DR MANE-Select; ENST00000244571.5; ENSP00000244571.4; NM_020745.4; NP_065796.2.
DR UCSC; uc010jza.2; human.
DR CTD; 57505; -.
DR DisGeNET; 57505; -.
DR GeneCards; AARS2; -.
DR HGNC; HGNC:21022; AARS2.
DR HPA; ENSG00000124608; Low tissue specificity.
DR MalaCards; AARS2; -.
DR MIM; 612035; gene.
DR MIM; 614096; phenotype.
DR MIM; 615889; phenotype.
DR neXtProt; NX_Q5JTZ9; -.
DR OpenTargets; ENSG00000124608; -.
DR Orphanet; 319504; Combined oxidative phosphorylation defect type 8.
DR Orphanet; 313808; Hereditary diffuse leukoencephalopathy with axonal spheroids and pigmented glia.
DR Orphanet; 99853; Ovarioleukodystrophy.
DR PharmGKB; PA162375129; -.
DR VEuPathDB; HostDB:ENSG00000124608; -.
DR eggNOG; KOG0188; Eukaryota.
DR GeneTree; ENSGT00940000158246; -.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; Q5JTZ9; -.
DR OMA; DTEACCG; -.
DR OrthoDB; 129373at2759; -.
DR PhylomeDB; Q5JTZ9; -.
DR TreeFam; TF300737; -.
DR BRENDA; 6.1.1.7; 2681.
DR PathwayCommons; Q5JTZ9; -.
DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
DR SignaLink; Q5JTZ9; -.
DR BioGRID-ORCS; 57505; 417 hits in 1093 CRISPR screens.
DR ChiTaRS; AARS2; human.
DR GeneWiki; AARS2; -.
DR GenomeRNAi; 57505; -.
DR Pharos; Q5JTZ9; Tbio.
DR PRO; PR:Q5JTZ9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5JTZ9; protein.
DR Bgee; ENSG00000124608; Expressed in tendon of biceps brachii and 186 other tissues.
DR Genevisible; Q5JTZ9; HS.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IMP:BHF-UCL.
DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0070143; P:mitochondrial alanyl-tRNA aminoacylation; IMP:BHF-UCL.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF101353; SSF101353; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cardiomyopathy;
KW Disease variant; Ligase; Metal-binding; Mitochondrion; Neurodegeneration;
KW Nucleotide-binding; Premature ovarian failure;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome;
KW RNA-binding; Transit peptide; tRNA-binding; Zinc.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT CHAIN 24..985
FT /note="Alanine--tRNA ligase, mitochondrial"
FT /id="PRO_0000250725"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 240..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 242
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 265
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 632
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 636
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 749
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 753
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT VARIANT 50
FT /note="F -> C (in LKENP; deleterious only under stress
FT conditions; dbSNP:rs587777590)"
FT /evidence="ECO:0000269|PubMed:24808023"
FT /id="VAR_071837"
FT VARIANT 77
FT /note="A -> V (found in patient with leukoencephalopathy;
FT unknown pathological significance; dbSNP:rs375949891)"
FT /evidence="ECO:0000269|PubMed:24808023"
FT /id="VAR_071838"
FT VARIANT 131
FT /note="Missing (found in patient with leukoencephalopathy;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:24808023"
FT /id="VAR_071839"
FT VARIANT 155
FT /note="L -> R (in COXPD8; dbSNP:rs387907061)"
FT /evidence="ECO:0000269|PubMed:21549344"
FT /id="VAR_065956"
FT VARIANT 199
FT /note="R -> C (found in patient with leukoencephalopathy;
FT unknown pathological significance; dbSNP:rs200105202)"
FT /evidence="ECO:0000269|PubMed:24808023"
FT /id="VAR_071840"
FT VARIANT 339
FT /note="I -> V (in dbSNP:rs324136)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_027609"
FT VARIANT 405
FT /note="E -> K (in LKENP; dbSNP:rs587777592)"
FT /evidence="ECO:0000269|PubMed:24808023"
FT /id="VAR_071841"
FT VARIANT 484
FT /note="A -> D (in dbSNP:rs495294)"
FT /id="VAR_027610"
FT VARIANT 592
FT /note="R -> W (in COXPD8; dbSNP:rs138119149)"
FT /evidence="ECO:0000269|PubMed:21549344"
FT /id="VAR_065957"
FT VARIANT 730
FT /note="V -> M (in dbSNP:rs35623954)"
FT /evidence="ECO:0000269|PubMed:24808023"
FT /id="VAR_071842"
FT VARIANT 850
FT /note="M -> V (in dbSNP:rs35783144)"
FT /id="VAR_057357"
FT VARIANT 965
FT /note="G -> R (in LKENP; dbSNP:rs543267101)"
FT /evidence="ECO:0000269|PubMed:24808023"
FT /id="VAR_071843"
FT HELIX 812..832
FT /evidence="ECO:0007829|PDB:6NLY"
FT HELIX 838..877
FT /evidence="ECO:0007829|PDB:6NLY"
FT STRAND 883..887
FT /evidence="ECO:0007829|PDB:6NLQ"
FT HELIX 893..906
FT /evidence="ECO:0007829|PDB:6NLQ"
FT STRAND 911..917
FT /evidence="ECO:0007829|PDB:6NLQ"
FT HELIX 919..921
FT /evidence="ECO:0007829|PDB:6NLQ"
FT STRAND 922..928
FT /evidence="ECO:0007829|PDB:6NLQ"
FT HELIX 939..949
FT /evidence="ECO:0007829|PDB:6NLQ"
FT STRAND 953..956
FT /evidence="ECO:0007829|PDB:6NLQ"
FT STRAND 958..966
FT /evidence="ECO:0007829|PDB:6NLQ"
FT HELIX 970..984
FT /evidence="ECO:0007829|PDB:6NLQ"
SQ SEQUENCE 985 AA; 107340 MW; 721368BD05474F86 CRC64;
MAASVAAAAR RLRRAIRRSP AWRGLSHRPL SSEPPAAKAS AVRAAFLNFF RDRHGHRLVP
SASVRPRGDP SLLFVNAGMN QFKPIFLGTV DPRSEMAGFR RVANSQKCVR AGGHHNDLED
VGRDLSHHTF FEMLGNWAFG GEYFKEEACN MAWELLTQVY GIPEERLWIS YFDGDPKAGL
DPDLETRDIW LSLGVPASRV LSFGPQENFW EMGDTGPCGP CTEIHYDLAG GVGAPQLVEL
WNLVFMQHNR EADGSLQPLP QRHVDTGMGL ERLVAVLQGK HSTYDTDLFS PLLNAIQQGC
RAPPYLGRVG VADEGRTDTA YRVVADHIRT LSVCISDGIF PGMSGPPLVL RRILRRAVRF
SMEILKAPPG FLGSLVPVVV ETLGDAYPEL QRNSAQIANL VSEDEAAFLA SLERGRRIID
RTLRTLGPSD MFPAEVAWSL SLCGDLGLPL DMVELMLEEK GVQLDSAGLE RLAQEEAQHR
ARQAEPVQKQ GLWLDVHALG ELQRQGVPPT DDSPKYNYSL RPSGSYEFGT CEAQVLQLYT
EDGTAVASVG KGQRCGLLLD RTNFYAEQGG QASDRGYLVR AGQEDVLFPV ARAQVCGGFI
LHEAVAPECL RLGDQVQLHV DEAWRLGCMA KHTATHLLNW ALRQTLGPGT EQQGSHLNPE
QLRLDVTTQT PLTPEQLRAV ENTVQEAVGQ DEAVYMEEVP LALTAQVPGL RSLDEVYPDP
VRVVSVGVPV AHALDPASQA ALQTSVELCC GTHLLRTGAV GDLVIIGDRQ LSKGTTRLLA
VTGEQAQQAR ELGQSLAQEV KAATERLSLG SRDVAEALRL SKDIGRLIEA VETAVMPQWQ
RRELLATVKM LQRRANTAIR KLQMGQAAKK TQELLERHSK GPLIVDTVSA ESLSVLVKVV
RQLCEQAPST SVLLLSPQPM GKVLCACQVA QGAMPTFTAE AWALAVCSHM GGKAWGSRVV
AQGTGSTTDL EAALSIAQTY ALSQL
