ACTN3_HUMAN
ID ACTN3_HUMAN Reviewed; 901 AA.
AC Q08043; A6NP77; Q4KKV2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Alpha-actinin-3;
DE AltName: Full=Alpha-actinin skeletal muscle isoform 3;
DE AltName: Full=F-actin cross-linking protein;
GN Name=ACTN3;
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 [MRNA], AND VARIANTS GLN-523; ARG-628 AND ARG-776.
RC TISSUE=Skeletal muscle;
RX PubMed=1339456; DOI=10.1016/s0021-9258(19)50420-3;
RA Beggs A.H., Byers T.J., Knoll J.H.M., Boyce F.M., Bruns G.A.P.,
RA Kunkel L.M.;
RT "Cloning and characterization of two human skeletal muscle alpha-actinin
RT genes located on chromosomes 1 and 11.";
RL J. Biol. Chem. 267:9281-9288(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-523; ARG-628 AND
RP ARG-776.
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 TISSUE SPECIFICITY, AND POLYMORPHISM.
RX PubMed=11440986; DOI=10.1093/hmg/10.13.1335;
RA Mills M., Yang N., Weinberger R., Vander Woude D.L., Beggs A.H.,
RA Easteal S., North K.N.;
RT "Differential expression of the actin-binding proteins, alpha-actinin-2 and
RT -3, in different species: implications for the evolution of functional
RT redundancy.";
RL Hum. Mol. Genet. 10:1335-1346(2001).
RN [5]
RP INTERACTION WITH MYOZ1.
RX PubMed=11171996; DOI=10.1073/pnas.98.4.1595;
RA Takada F., Vander Woude D.L., Tong H.-Q., Thompson T.G., Watkins S.C.,
RA Kunkel L.M., Beggs A.H.;
RT "Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal
RT muscle Z lines.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1595-1600(2001).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 26-273.
RX PubMed=15808860; DOI=10.1016/j.jmb.2005.01.002;
RA Franzot G., Sjoblom B., Gautel M., Djinovic Carugo K.;
RT "The crystal structure of the actin binding domain from alpha-actinin in
RT its closed conformation: structural insight into phospholipid regulation of
RT alpha-actinin.";
RL J. Mol. Biol. 348:151-165(2005).
RN [8]
RP VARIANTS GLN-523 AND 577-ARG--LEU-901 DEL, AND POLYMORPHISM.
RX PubMed=10192379; DOI=10.1038/7675;
RA North K.N., Yang N., Wattanasirichaigoon D., Mills M., Easteal S.,
RA Beggs A.H.;
RT "A common nonsense mutation results in alpha-actinin-3 deficiency in the
RT general population.";
RL Nat. Genet. 21:353-354(1999).
CC -!- FUNCTION: F-actin cross-linking protein which is thought to anchor
CC actin to a variety of intracellular structures. This is a bundling
CC protein.
CC -!- SUBUNIT: Homodimer; antiparallel. Also forms heterodimers with ACTN2.
CC Interacts with MYOZ1. {ECO:0000269|PubMed:11171996}.
CC -!- INTERACTION:
CC Q08043; P12814: ACTN1; NbExp=3; IntAct=EBI-2880652, EBI-351710;
CC Q08043; Q08043: ACTN3; NbExp=3; IntAct=EBI-2880652, EBI-2880652;
CC Q08043; O43707: ACTN4; NbExp=3; IntAct=EBI-2880652, EBI-351526;
CC Q08043; Q96DX5: ASB9; NbExp=3; IntAct=EBI-2880652, EBI-745641;
CC Q08043; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-2880652, EBI-12811889;
CC Q08043; Q9H1P6: C20orf85; NbExp=3; IntAct=EBI-2880652, EBI-12155483;
CC Q08043; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-2880652, EBI-739879;
CC Q08043; A2RRN7: CADPS; NbExp=3; IntAct=EBI-2880652, EBI-10179719;
CC Q08043; P78358: CTAG1B; NbExp=5; IntAct=EBI-2880652, EBI-1188472;
CC Q08043; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-2880652, EBI-751587;
CC Q08043; P42830: CXCL5; NbExp=3; IntAct=EBI-2880652, EBI-12175919;
CC Q08043; O95865: DDAH2; NbExp=3; IntAct=EBI-2880652, EBI-749139;
CC Q08043; Q16610: ECM1; NbExp=3; IntAct=EBI-2880652, EBI-947964;
CC Q08043; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-2880652, EBI-6658203;
CC Q08043; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-2880652, EBI-7251368;
CC Q08043; O14964: HGS; NbExp=3; IntAct=EBI-2880652, EBI-740220;
CC Q08043; P35452-2: HOXD12; NbExp=3; IntAct=EBI-2880652, EBI-17244356;
CC Q08043; O75031: HSF2BP; NbExp=3; IntAct=EBI-2880652, EBI-7116203;
CC Q08043; P26440: IVD; NbExp=3; IntAct=EBI-2880652, EBI-2866408;
CC Q08043; P48668: KRT6C; NbExp=3; IntAct=EBI-2880652, EBI-2564105;
CC Q08043; Q9UBR4-2: LHX3; NbExp=5; IntAct=EBI-2880652, EBI-12039345;
CC Q08043; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2880652, EBI-739832;
CC Q08043; P43360: MAGEA6; NbExp=3; IntAct=EBI-2880652, EBI-1045155;
CC Q08043; Q8IY33: MICALL2; NbExp=3; IntAct=EBI-2880652, EBI-2555563;
CC Q08043; Q9UBF9: MYOT; NbExp=3; IntAct=EBI-2880652, EBI-296701;
CC Q08043; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-2880652, EBI-744402;
CC Q08043; O14561: NDUFAB1; NbExp=3; IntAct=EBI-2880652, EBI-1246261;
CC Q08043; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-2880652, EBI-3920396;
CC Q08043; A8MYP8: ODF3B; NbExp=3; IntAct=EBI-2880652, EBI-12010090;
CC Q08043; P05166: PCCB; NbExp=3; IntAct=EBI-2880652, EBI-1371908;
CC Q08043; Q99959-2: PKP2; NbExp=3; IntAct=EBI-2880652, EBI-10987518;
CC Q08043; P78424: POU6F2; NbExp=3; IntAct=EBI-2880652, EBI-12029004;
CC Q08043; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-2880652, EBI-2557469;
CC Q08043; Q13882: PTK6; NbExp=3; IntAct=EBI-2880652, EBI-1383632;
CC Q08043; Q14D33: RTP5; NbExp=3; IntAct=EBI-2880652, EBI-10217913;
CC Q08043; O95863: SNAI1; NbExp=3; IntAct=EBI-2880652, EBI-1045459;
CC Q08043; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-2880652, EBI-12288855;
CC Q08043; Q9H987-2: SYNPO2L; NbExp=3; IntAct=EBI-2880652, EBI-12082116;
CC Q08043; Q13077: TRAF1; NbExp=3; IntAct=EBI-2880652, EBI-359224;
CC Q08043; Q14134: TRIM29; NbExp=3; IntAct=EBI-2880652, EBI-702370;
CC Q08043; O75604: USP2; NbExp=3; IntAct=EBI-2880652, EBI-743272;
CC Q08043; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-2880652, EBI-10252492;
CC Q08043; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-2880652, EBI-743265;
CC -!- TISSUE SPECIFICITY: Expressed only in a subset of type 2 skeletal
CC muscle fibers. {ECO:0000269|PubMed:11440986}.
CC -!- POLYMORPHISM: About 18% of the world population lack a functional ACTN3
CC due to a stop codon polymorphism at position 577. The absence of a
CC functional ACTN3 expression is not correlated with a disease state
CC [MIM:617749]. {ECO:0000269|PubMed:10192379}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AP002748; Type=Miscellaneous discrepancy; Note=According to the human genome assembly there is a stop codon in position 577 which is only found in 18% of the world population.; Evidence={ECO:0000305};
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DR EMBL; M86407; AAA51585.1; -; mRNA.
DR EMBL; AP002748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099647; AAH99647.1; -; mRNA.
DR EMBL; BC099649; AAH99649.1; -; mRNA.
DR CCDS; CCDS53663.1; -.
DR PIR; B40199; FAHUA3.
DR RefSeq; NP_001095.2; NM_001104.3.
DR RefSeq; NP_001245300.2; NM_001258371.2.
DR PDB; 1TJT; X-ray; 2.19 A; A=26-273.
DR PDB; 1WKU; X-ray; 1.60 A; A/B=26-273.
DR PDB; 3LUE; EM; -; K/L/M/N/O/P/Q/R/S/T=42-150.
DR PDBsum; 1TJT; -.
DR PDBsum; 1WKU; -.
DR PDBsum; 3LUE; -.
DR AlphaFoldDB; Q08043; -.
DR SMR; Q08043; -.
DR BioGRID; 106604; 99.
DR IntAct; Q08043; 57.
DR MINT; Q08043; -.
DR STRING; 9606.ENSP00000422007; -.
DR iPTMnet; Q08043; -.
DR PhosphoSitePlus; Q08043; -.
DR SwissPalm; Q08043; -.
DR BioMuta; ACTN3; -.
DR DMDM; 215273967; -.
DR EPD; Q08043; -.
DR jPOST; Q08043; -.
DR MassIVE; Q08043; -.
DR MaxQB; Q08043; -.
DR PeptideAtlas; Q08043; -.
DR PRIDE; Q08043; -.
DR ProteomicsDB; 58566; -.
DR Antibodypedia; 73518; 262 antibodies from 30 providers.
DR DNASU; 89; -.
DR Ensembl; ENST00000513398.2; ENSP00000426797.1; ENSG00000248746.6.
DR GeneID; 89; -.
DR KEGG; hsa:89; -.
DR MANE-Select; ENST00000513398.2; ENSP00000426797.1; NM_001104.4; NP_001095.2.
DR UCSC; uc021qlz.4; human.
DR CTD; 89; -.
DR DisGeNET; 89; -.
DR GeneCards; ACTN3; -.
DR HGNC; HGNC:165; ACTN3.
DR HPA; ENSG00000248746; Tissue enriched (skeletal).
DR MalaCards; ACTN3; -.
DR MIM; 102574; phenotype.
DR MIM; 617749; phenotype.
DR neXtProt; NX_Q08043; -.
DR OpenTargets; ENSG00000248746; -.
DR PharmGKB; PA24485; -.
DR VEuPathDB; HostDB:ENSG00000248746; -.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000153968; -.
DR HOGENOM; CLU_005217_1_1_1; -.
DR InParanoid; Q08043; -.
DR OMA; MLNQRDY; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; Q08043; -.
DR PathwayCommons; Q08043; -.
DR Reactome; R-HSA-373753; Nephrin family interactions.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; Q08043; -.
DR BioGRID-ORCS; 89; 7 hits in 188 CRISPR screens.
DR ChiTaRS; ACTN3; human.
DR EvolutionaryTrace; Q08043; -.
DR GeneWiki; ACTN3; -.
DR GenomeRNAi; 89; -.
DR Pharos; Q08043; Tbio.
DR PRO; PR:Q08043; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q08043; protein.
DR Bgee; ENSG00000248746; Expressed in skeletal muscle tissue of rectus abdominis and 100 other tissues.
DR ExpressionAtlas; Q08043; baseline and differential.
DR Genevisible; Q08043; HS.
DR GO; GO:0005884; C:actin filament; TAS:ProtInc.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; TAS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005178; F:integrin binding; TAS:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR GO; GO:0048041; P:focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; ISS:UniProtKB.
DR GO; GO:1901078; P:negative regulation of relaxation of muscle; IEA:Ensembl.
DR GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; IEA:Ensembl.
DR GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; IEA:Ensembl.
DR GO; GO:1904025; P:positive regulation of glucose catabolic process to lactate via pyruvate; ISS:UniProtKB.
DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; ISS:UniProtKB.
DR GO; GO:1903715; P:regulation of aerobic respiration; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0014728; P:regulation of the force of skeletal muscle contraction; ISS:UniProtKB.
DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; ISS:UniProtKB.
DR GO; GO:0014732; P:skeletal muscle atrophy; ISS:UniProtKB.
DR GO; GO:0014883; P:transition between fast and slow fiber; ISS:UniProtKB.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 3.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00150; SPEC; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Calcium; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..901
FT /note="Alpha-actinin-3"
FT /id="PRO_0000073438"
FT DOMAIN 45..149
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 158..264
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 288..398
FT /note="Spectrin 1"
FT REPEAT 408..513
FT /note="Spectrin 2"
FT REPEAT 523..634
FT /note="Spectrin 3"
FT REPEAT 644..747
FT /note="Spectrin 4"
FT DOMAIN 760..795
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 796..831
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..261
FT /note="Actin-binding"
FT BINDING 773
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 777
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 779
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 784
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 809
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 811
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VARIANT 523
FT /note="R -> Q (in dbSNP:rs1671064)"
FT /evidence="ECO:0000269|PubMed:10192379,
FT ECO:0000269|PubMed:1339456, ECO:0000269|PubMed:15489334"
FT /id="VAR_012705"
FT VARIANT 577..901
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:10192379"
FT /id="VAR_080044"
FT VARIANT 628
FT /note="C -> R (in dbSNP:rs618838)"
FT /evidence="ECO:0000269|PubMed:1339456,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047528"
FT VARIANT 635
FT /note="E -> A (in dbSNP:rs2229456)"
FT /id="VAR_033488"
FT VARIANT 776
FT /note="Q -> R (in dbSNP:rs540874)"
FT /evidence="ECO:0000269|PubMed:1339456,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047529"
FT HELIX 43..59
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1WKU"
FT TURN 69..75
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:1WKU"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:1WKU"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:1WKU"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:1WKU"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1TJT"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 215..229
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:1WKU"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1WKU"
FT HELIX 249..265
FT /evidence="ECO:0007829|PDB:1WKU"
SQ SEQUENCE 901 AA; 103241 MW; C49B7885E7E1EDA7 CRC64;
MMMVMQPEGL GAGEGRFAGG GGGGEYMEQE EDWDRDLLLD PAWEKQQRKT FTAWCNSHLR
KAGTQIENIE EDFRNGLKLM LLLEVISGER LPRPDKGKMR FHKIANVNKA LDFIASKGVK
LVSIGAEEIV DGNLKMTLGM IWTIILRFAI QDISVEETSA KEGLLLWCQR KTAPYRNVNV
QNFHTSWKDG LALCALIHRH RPDLIDYAKL RKDDPIGNLN TAFEVAEKYL DIPKMLDAED
IVNTPKPDEK AIMTYVSCFY HAFAGAEQAE TAANRICKVL AVNQENEKLM EEYEKLASEL
LEWIRRTVPW LENRVGEPSM SAMQRKLEDF RDYRRLHKPP RIQEKCQLEI NFNTLQTKLR
LSHRPAFMPS EGKLVSDIAN AWRGLEQVEK GYEDWLLSEI RRLQRLQHLA EKFRQKASLH
EAWTRGKEEM LSQRDYDSAL LQEVRALLRR HEAFESDLAA HQDRVEHIAA LAQELNELDY
HEAASVNSRC QAICDQWDNL GTLTQKRRDA LERMEKLLET IDRLQLEFAR RAAPFNNWLD
GAVEDLQDVW LVHSVEETQS LLTAHDQFKA TLPEADRERG AIMGIQGEIQ KICQTYGLRP
CSTNPYITLS PQDINTKWDM VRKLVPSCDQ TLQEELARQQ VNERLRRQFA AQANAIGPWI
QAKVEEVGRL AAGLAGSLEE QMAGLRQQEQ NIINYKTNID RLEGDHQLLQ ESLVFDNKHT
VYSMEHIRVG WEQLLTSIAR TINEVENQVL TRDAKGLSQE QLNEFRASFN HFDRKQNGMM
EPDDFRACLI SMGYDLGEVE FARIMTMVDP NAAGVVTFQA FIDFMTRETA ETDTTEQVVA
SFKILAGDKN YITPEELRRE LPAKQAEYCI RRMVPYKGSG APAGALDYVA FSSALYGESD
L
