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   24-JAN-2024, entry version 201.
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; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-2880652, EBI-739879;
CC       Q08043; A2RRN7: CADPS; NbExp=3; IntAct=EBI-2880652, EBI-10179719;
CC       Q08043; A8MYP8: CIMAP1B; NbExp=3; IntAct=EBI-2880652, EBI-12010090;
CC       Q08043; Q9H1P6: CIMIP1; NbExp=3; IntAct=EBI-2880652, EBI-12155483;
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; 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: The sequence shown in this entry differs from the
CC       translation of the reference genome assembly (GRCh38/hg38) due to a
CC       nonsense variant creating stop codon at position 577 in the reference
CC       genome, leading to ACTN3 deficiency. However, the presence of this
CC       variant is not associated with any disease phenotype [MIM:617749]. The
CC       sequence shown in this entry is that of variant p.Ter577Arg, which has
CC       a frequency of about 62% in the human population according to the
CC       Genome Aggregation Database (gnomAD v3.1.2).
CC       {ECO:0000269|PubMed:10192379}.
CC   -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
CC   -!- CAUTION: The sequence shown in this entry differs from the translation
CC       of the reference genome assembly (GRCh38/hg38) due to a nonsense
CC       variant creating stop codon at position 577 in the reference genome.
CC       {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   EMDB; EMD-5170; -.
DR   SMR; Q08043; -.
DR   BioGRID; 106604; 101.
DR   IntAct; Q08043; 58.
DR   MINT; Q08043; -.
DR   STRING; 9606.ENSP00000422007; -.
DR   GlyGen; Q08043; 1 site, 1 O-linked glycan (1 site).
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   PaxDb; 9606-ENSP00000422007; -.
DR   PeptideAtlas; Q08043; -.
DR   PRIDE; Q08043; -.
DR   ProteomicsDB; 58566; -.
DR   Pumba; Q08043; -.
DR   Antibodypedia; 73518; 296 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   AGR; HGNC:165; -.
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; RMTKYTG; -.
DR   OrthoDB; 2872403at2759; -.
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 233 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 cell types or tissues.
DR   ExpressionAtlas; Q08043; baseline and differential.
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; cd21214; CH_ACTN_rpt1; 1.
DR   CDD; cd21216; CH_ACTN_rpt2; 1.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd00176; SPEC; 3.
DR   Gene3D; 1.20.58.60; -; 4.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
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   PANTHER; PTHR11915:SF432; ALPHA-ACTININ-3; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
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; SM01184; efhand_Ca_insen; 1.
DR   SMART; SM00150; SPEC; 2.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 4.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   Genevisible; Q08043; HS.
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 (in dbSNP:rs1815739)"
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
//