ID   SUCA_HUMAN              Reviewed;         346 AA.
AC   P53597; Q9BWB0; Q9UNP6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 4.
DT   27-MAR-2024, entry version 219.
DE   RecName: Full=Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03222};
DE            EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03222};
DE            EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03222};
DE   AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE            Short=SCS-alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE   Flags: Precursor;
GN   Name=SUCLG1 {ECO:0000255|HAMAP-Rule:MF_03222};
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 GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-346.
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-346.
RA   Tews K.N., Mehus J.G., Johnson J.D., Milavetz B.I., Lambeth D.O.;
RT   "Sequence of the alpha subunit of succinyl-CoA synthetase in human.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 12-145.
RC   TISSUE=Brain, and Skeletal muscle;
RX   PubMed=9128182; DOI=10.1016/s0925-4439(96)00076-2;
RA   James M., Man N.T., Edwards Y.H., Morris G.E.;
RT   "The molecular basis for cross-reaction anti-dystrophin antibody with
RT   alpha-actinin.";
RL   Biochim. Biophys. Acta 1360:169-176(1997).
RN   [5]
RP   INVOLVEMENT IN MTDPS9.
RX   PubMed=17668387; DOI=10.1086/519222;
RA   Ostergaard E., Christensen E., Kristensen E., Mogensen B., Duno M.,
RA   Shoubridge E.A., Wibrand F.;
RT   "Deficiency of the alpha subunit of succinate-coenzyme A ligase causes
RT   fatal infantile lactic acidosis with mitochondrial DNA depletion.";
RL   Am. J. Hum. Genet. 81:383-387(2007).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54, 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   [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   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   [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).
RN   [10]
RP   VARIANT MTDPS9 ALA-85.
RX   PubMed=19526370; DOI=10.1007/s00431-009-1007-z;
RA   Ostergaard E., Schwartz M., Batbayli M., Christensen E., Hjalmarson O.,
RA   Kollberg G., Holme E.;
RT   "A novel missense mutation in SUCLG1 associated with mitochondrial DNA
RT   depletion, encephalomyopathic form, with methylmalonic aciduria.";
RL   Eur. J. Pediatr. 169:201-205(2010).
RN   [11]
RP   VARIANT MTDPS9 ARG-170.
RX   PubMed=20693550; DOI=10.1136/jmg.2009.073445;
RA   Rouzier C., Le Guedard-Mereuze S., Fragaki K., Serre V., Miro J.,
RA   Tuffery-Giraud S., Chaussenot A., Bannwarth S., Caruba C., Ostergaard E.,
RA   Pellissier J.F., Richelme C., Espil C., Chabrol B., Paquis-Flucklinger V.;
RT   "The severity of phenotype linked to SUCLG1 mutations could be correlated
RT   with residual amount of SUCLG1 protein.";
RL   J. Med. Genet. 47:670-676(2010).
RN   [12]
RP   VARIANT MTDPS9 LEU-14.
RX   PubMed=20453710; DOI=10.1203/pdr.0b013e3181e5c3a4;
RA   Van Hove J.L., Saenz M.S., Thomas J.A., Gallagher R.C., Lovell M.A.,
RA   Fenton L.Z., Shanske S., Myers S.M., Wanders R.J., Ruiter J.,
RA   Turkenburg M., Waterham H.R.;
RT   "Succinyl-CoA ligase deficiency: a mitochondrial hepatoencephalomyopathy.";
RL   Pediatr. Res. 68:159-164(2010).
RN   [13]
RP   VARIANT ALA-37.
RX   PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
RA   Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
RA   Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
RT   "Homozygous missense mutation in the LMAN2L gene segregates with
RT   intellectual disability in a large consanguineous Pakistani family.";
RL   J. Med. Genet. 53:138-144(2016).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC       (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC       either ATP or GTP and thus represents the only step of substrate-level
CC       phosphorylation in the TCA. The alpha subunit of the enzyme binds the
CC       substrates coenzyme A and phosphate, while succinate binding and
CC       specificity for either ATP or GTP is provided by different beta
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03222};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03222};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_03222}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Different beta
CC       subunits determine nucleotide specificity. Together with the ATP-
CC       specific beta subunit SUCLA2, forms an ADP-forming succinyl-CoA
CC       synthetase (A-SCS). Together with the GTP-specific beta subunit SUCLG2
CC       forms a GDP-forming succinyl-CoA synthetase (G-SCS).
CC       {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- INTERACTION:
CC       P53597; Q96I99: SUCLG2; NbExp=2; IntAct=EBI-1237145, EBI-2511878;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- DISEASE: Mitochondrial DNA depletion syndrome 9 (MTDPS9) [MIM:245400]:
CC       A severe disorder due to mitochondrial dysfunction. It is characterized
CC       by infantile onset of hypotonia, lactic acidosis, severe psychomotor
CC       retardation, progressive neurologic deterioration, and excretion of
CC       methylmalonic acid. {ECO:0000269|PubMed:17668387,
CC       ECO:0000269|PubMed:19526370, ECO:0000269|PubMed:20453710,
CC       ECO:0000269|PubMed:20693550}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD17940.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH00504.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA92426.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC096770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000504; AAH00504.1; ALT_INIT; mRNA.
DR   EMBL; AF104921; AAD17940.2; ALT_INIT; mRNA.
DR   EMBL; Z68204; CAA92426.1; ALT_INIT; mRNA.
DR   CCDS; CCDS1967.2; -.
DR   RefSeq; NP_003840.2; NM_003849.3.
DR   PDB; 6G4Q; X-ray; 2.59 A; A=42-346.
DR   PDB; 6WCV; X-ray; 1.52 A; A=42-346.
DR   PDB; 7MSR; X-ray; 1.58 A; A=42-346.
DR   PDB; 7MSS; X-ray; 1.75 A; A=42-346.
DR   PDB; 7MST; X-ray; 1.61 A; A=42-346.
DR   PDBsum; 6G4Q; -.
DR   PDBsum; 6WCV; -.
DR   PDBsum; 7MSR; -.
DR   PDBsum; 7MSS; -.
DR   PDBsum; 7MST; -.
DR   AlphaFoldDB; P53597; -.
DR   SMR; P53597; -.
DR   BioGRID; 114330; 124.
DR   ComplexPortal; CPX-6175; Mitochondrial succinyl-CoA synthetase complex, GTP-specific variant.
DR   ComplexPortal; CPX-6176; Mitochondrial succinyl-CoA synthetase complex, ATP-specific variant.
DR   CORUM; P53597; -.
DR   IntAct; P53597; 27.
DR   MINT; P53597; -.
DR   STRING; 9606.ENSP00000377446; -.
DR   DrugBank; DB00787; Acyclovir.
DR   GlyCosmos; P53597; 1 site, 1 glycan.
DR   GlyGen; P53597; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P53597; -.
DR   PhosphoSitePlus; P53597; -.
DR   SwissPalm; P53597; -.
DR   BioMuta; SUCLG1; -.
DR   DMDM; 223634731; -.
DR   EPD; P53597; -.
DR   jPOST; P53597; -.
DR   MassIVE; P53597; -.
DR   MaxQB; P53597; -.
DR   PaxDb; 9606-ENSP00000377446; -.
DR   PeptideAtlas; P53597; -.
DR   ProteomicsDB; 56587; -.
DR   Pumba; P53597; -.
DR   TopDownProteomics; P53597; -.
DR   Antibodypedia; 47488; 138 antibodies from 29 providers.
DR   DNASU; 8802; -.
DR   Ensembl; ENST00000393868.7; ENSP00000377446.2; ENSG00000163541.12.
DR   GeneID; 8802; -.
DR   KEGG; hsa:8802; -.
DR   MANE-Select; ENST00000393868.7; ENSP00000377446.2; NM_003849.4; NP_003840.2.
DR   UCSC; uc002son.4; human.
DR   AGR; HGNC:11449; -.
DR   CTD; 8802; -.
DR   DisGeNET; 8802; -.
DR   GeneCards; SUCLG1; -.
DR   GeneReviews; SUCLG1; -.
DR   HGNC; HGNC:11449; SUCLG1.
DR   HPA; ENSG00000163541; Tissue enhanced (kidney).
DR   MalaCards; SUCLG1; -.
DR   MIM; 245400; phenotype.
DR   MIM; 611224; gene.
DR   neXtProt; NX_P53597; -.
DR   OpenTargets; ENSG00000163541; -.
DR   Orphanet; 17; Fatal infantile lactic acidosis with methylmalonic aciduria.
DR   PharmGKB; PA36246; -.
DR   VEuPathDB; HostDB:ENSG00000163541; -.
DR   eggNOG; KOG1255; Eukaryota.
DR   GeneTree; ENSGT00940000156351; -.
DR   HOGENOM; CLU_052104_1_0_1; -.
DR   InParanoid; P53597; -.
DR   OMA; VIICITE; -.
DR   OrthoDB; 474at2759; -.
DR   PhylomeDB; P53597; -.
DR   TreeFam; TF300666; -.
DR   BioCyc; MetaCyc:HS08877-MONOMER; -.
DR   BRENDA; 6.2.1.4; 2681.
DR   BRENDA; 6.2.1.5; 2681.
DR   PathwayCommons; P53597; -.
DR   Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR   SignaLink; P53597; -.
DR   SIGNOR; P53597; -.
DR   UniPathway; UPA00223; UER00999.
DR   BioGRID-ORCS; 8802; 72 hits in 1159 CRISPR screens.
DR   ChiTaRS; SUCLG1; human.
DR   GeneWiki; SUCLG1; -.
DR   GenomeRNAi; 8802; -.
DR   Pharos; P53597; Tbio.
DR   PRO; PR:P53597; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P53597; Protein.
DR   Bgee; ENSG00000163541; Expressed in nephron tubule and 207 other cell types or tissues.
DR   ExpressionAtlas; P53597; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR   GO; GO:0045244; C:succinate-CoA ligase complex (GDP-forming); IPI:ComplexPortal.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR   GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR   GO; GO:1901289; P:succinyl-CoA catabolic process; NAS:ComplexPortal.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR   HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005811; SUCC_ACL_C.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   NCBIfam; TIGR01019; sucCoAalpha; 1.
DR   PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
DR   UCD-2DPAGE; P53597; -.
DR   Genevisible; P53597; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Disease variant; Ligase; Mitochondrion;
KW   Nucleotide-binding; Primary mitochondrial disease; Reference proteome;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..40
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           41..346
FT                   /note="Succinate--CoA ligase [ADP/GDP-forming] subunit
FT                   alpha, mitochondrial"
FT                   /id="PRO_0000033340"
FT   ACT_SITE        299
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         64..67
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         90
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         143..145
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit beta"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   MOD_RES         54
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         57
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         57
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         66
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         66
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         81
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         105
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         338
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   VARIANT         14
FT                   /note="M -> L (in MTDPS9; with progressive liver disease
FT                   and recurrent hepatic failure; dbSNP:rs796052053)"
FT                   /evidence="ECO:0000269|PubMed:20453710"
FT                   /id="VAR_065120"
FT   VARIANT         37
FT                   /note="G -> A (in dbSNP:rs369610897)"
FT                   /evidence="ECO:0000269|PubMed:26566883"
FT                   /id="VAR_076432"
FT   VARIANT         85
FT                   /note="G -> A (in MTDPS9; dbSNP:rs267607097)"
FT                   /evidence="ECO:0000269|PubMed:19526370"
FT                   /id="VAR_065157"
FT   VARIANT         170
FT                   /note="P -> R (in MTDPS9; dbSNP:rs267607099)"
FT                   /evidence="ECO:0000269|PubMed:20693550"
FT                   /id="VAR_065121"
FT   CONFLICT        19
FT                   /note="S -> N (in Ref. 4; CAA92426)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="P -> Q (in Ref. 4; CAA92426)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="R -> Q (in Ref. 4; CAA92426)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="T -> L (in Ref. 3; AAD17940)"
FT                   /evidence="ECO:0000305"
FT   HELIX           43..50
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   TURN            62..64
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           66..78
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          82..86
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          98..102
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           104..111
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           122..134
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          138..142
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           149..160
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          170..172
FT                   /evidence="ECO:0007829|PDB:7MSR"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   TURN            178..180
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          181..186
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          193..201
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           203..215
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          220..225
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           236..245
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          251..261
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           262..273
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          274..276
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          282..287
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   STRAND          298..301
FT                   /evidence="ECO:0007829|PDB:7MSS"
FT   HELIX           311..320
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           329..331
FT                   /evidence="ECO:0007829|PDB:6WCV"
FT   HELIX           332..342
FT                   /evidence="ECO:0007829|PDB:6WCV"
SQ   SEQUENCE   346 AA;  36250 MW;  76EF06F323CD5188 CRC64;
     MTATLAAAAD IATMVSGSSG LAAARLLSRS FLLPQNGIRH CSYTASRQHL YVDKNTKIIC
     QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGQTHLGLPV FNTVKEAKEQ TGATASVIYV
     PPPFAAAAIN EAIEAEIPLV VCITEGIPQQ DMVRVKHKLL RQEKTRLIGP NCPGVINPGE
     CKIGIMPGHI HKKGRIGIVS RSGTLTYEAV HQTTQVGLGQ SLCVGIGGDP FNGTDFIDCL
     EIFLNDSATE GIILIGEIGG NAEENAAEFL KQHNSGPNSK PVVSFIAGLT APPGRRMGHA
     GAIIAGGKGG AKEKISALQS AGVVVSMSPA QLGTTIYKEF EKRKML
//