SUCA_HUMAN
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 03-AUG-2022, entry version 210.
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 PDBsum; 6G4Q; -.
DR PDBsum; 6WCV; -.
DR AlphaFoldDB; P53597; -.
DR SMR; P53597; -.
DR BioGRID; 114330; 110.
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; 24.
DR MINT; P53597; -.
DR STRING; 9606.ENSP00000377446; -.
DR DrugBank; DB00787; Acyclovir.
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 UCD-2DPAGE; P53597; -.
DR EPD; P53597; -.
DR jPOST; P53597; -.
DR MassIVE; P53597; -.
DR MaxQB; P53597; -.
DR PaxDb; P53597; -.
DR PeptideAtlas; P53597; -.
DR PRIDE; P53597; -.
DR ProteomicsDB; 56587; -.
DR TopDownProteomics; P53597; -.
DR Antibodypedia; 47488; 122 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 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; 1247548at2759; -.
DR PhylomeDB; P53597; -.
DR TreeFam; TF300666; -.
DR BioCyc; MetaCyc:HS08877-MON; -.
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; 69 hits in 1080 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 205 other tissues.
DR ExpressionAtlas; P53597; baseline and differential.
DR Genevisible; P53597; HS.
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; IC:ComplexPortal.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.40.50.261; -; 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; IPR005811; CoA_ligase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001553; SucCS_alpha; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
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 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 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
