MYO3A_HUMAN
ID MYO3A_HUMAN Reviewed; 1616 AA.
AC Q8NEV4; Q4G0X2; Q5VZ28; Q8WX17; Q9NYS8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Myosin-IIIa;
DE EC=2.7.11.1;
GN Name=MYO3A;
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] (ISOFORM 1), AND VARIANT SER-1313.
RX PubMed=10936054; DOI=10.1006/geno.2000.6256;
RA Dose A.C., Burnside B.;
RT "Cloning and chromosomal localization of a human class III myosin.";
RL Genomics 67:333-342(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-1313, INVOLVEMENT IN
RP DFNB30, AND FUNCTION.
RX PubMed=12032315; DOI=10.1073/pnas.102091699;
RA Walsh T., Walsh V., Vreugde S., Hertzano R., Shahin H., Haika S., Lee M.K.,
RA Kanaan M., King M.-C., Avraham K.B.;
RT "From flies' eyes to our ears: mutations in a human class III myosin cause
RT progressive nonsyndromic hearing loss DFNB30.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7518-7523(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [5]
RP INTERACTION WITH MORN4, AND SUBCELLULAR LOCATION.
RX PubMed=25822849; DOI=10.1371/journal.pone.0122502;
RA Mecklenburg K.L., Freed S.A., Raval M., Quintero O.A., Yengo C.M.,
RA O'Tousa J.E.;
RT "Invertebrate and vertebrate class III myosins interact with MORN repeat-
RT containing adaptor proteins.";
RL PLoS ONE 10:E0122502-E0122502(2015).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-178; HIS-319; VAL-348; ILE-369;
RP LYS-525; SER-833; ASN-956; ARG-956; THR-1032; MET-1045; MET-1137; ALA-1195;
RP SER-1284; THR-1287; SER-1313; HIS-1347; ILE-1417 AND GLU-1488.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Probable actin-based motor with a protein kinase activity.
CC Probably plays a role in vision and hearing (PubMed:12032315). Required
CC for normal cochlear hair bundle development and hearing. Plays an
CC important role in the early steps of cochlear hair bundle
CC morphogenesis. Influences the number and lengths of stereocilia to be
CC produced and limits the growth of microvilli within the forming
CC auditory hair bundles thereby contributing to the architecture of the
CC hair bundle, including its staircase pattern. Involved in the
CC elongation of actin in stereocilia tips by transporting the actin
CC regulatory factor ESPN to the plus ends of actin filaments (By
CC similarity). {ECO:0000250|UniProtKB:Q8K3H5,
CC ECO:0000269|PubMed:12032315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with MORN4 (PubMed:25822849). Interacts (via C-
CC terminus) with ESPN and ESPNL (By similarity).
CC {ECO:0000250|UniProtKB:Q8K3H5, ECO:0000269|PubMed:25822849}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm
CC {ECO:0000269|PubMed:25822849}. Cell projection, filopodium tip
CC {ECO:0000269|PubMed:25822849}. Cell projection, stereocilium
CC {ECO:0000250|UniProtKB:Q8K3H5}. Note=Increased localization at the
CC filodium tip seen in the presence of MORN4.
CC {ECO:0000269|PubMed:25822849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NEV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NEV4-2; Sequence=VSP_056231, VSP_056232;
CC -!- TISSUE SPECIFICITY: Strongest expression in retina, retinal pigment
CC epithelial cells, cochlea and pancreas.
CC -!- DISEASE: Deafness, autosomal recessive, 30 (DFNB30) [MIM:607101]: A
CC form of non-syndromic deafness characterized by bilateral progressive
CC hearing loss, which first affects the high frequencies. Hearing loss
CC begins in the second decade, and by age 50 is severe in high and middle
CC frequencies and moderate at low frequencies.
CC {ECO:0000269|PubMed:12032315}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase
CC superfamily. STE Ser/Thr protein kinase family. {ECO:0000305}.
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DR EMBL; AF229172; AAF70861.1; -; mRNA.
DR EMBL; AY101367; AAM34500.1; -; mRNA.
DR EMBL; AL162503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036079; AAH36079.1; -; mRNA.
DR CCDS; CCDS7148.1; -. [Q8NEV4-1]
DR RefSeq; NP_059129.3; NM_017433.4. [Q8NEV4-1]
DR RefSeq; XP_011517800.1; XM_011519498.2. [Q8NEV4-1]
DR RefSeq; XP_011517801.1; XM_011519499.1. [Q8NEV4-1]
DR RefSeq; XP_011517802.1; XM_011519500.2. [Q8NEV4-1]
DR PDB; 6JLE; X-ray; 1.55 A; E=1410-1457.
DR PDBsum; 6JLE; -.
DR AlphaFoldDB; Q8NEV4; -.
DR SMR; Q8NEV4; -.
DR BioGRID; 119814; 9.
DR IntAct; Q8NEV4; 3.
DR STRING; 9606.ENSP00000265944; -.
DR BindingDB; Q8NEV4; -.
DR ChEMBL; CHEMBL5546; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q8NEV4; -.
DR iPTMnet; Q8NEV4; -.
DR PhosphoSitePlus; Q8NEV4; -.
DR BioMuta; MYO3A; -.
DR DMDM; 160112826; -.
DR EPD; Q8NEV4; -.
DR MassIVE; Q8NEV4; -.
DR PaxDb; Q8NEV4; -.
DR PeptideAtlas; Q8NEV4; -.
DR PRIDE; Q8NEV4; -.
DR ProteomicsDB; 62136; -.
DR ProteomicsDB; 73220; -. [Q8NEV4-1]
DR Antibodypedia; 25882; 146 antibodies from 18 providers.
DR DNASU; 53904; -.
DR Ensembl; ENST00000376302.5; ENSP00000365479.1; ENSG00000095777.17. [Q8NEV4-2]
DR Ensembl; ENST00000642920.2; ENSP00000495965.1; ENSG00000095777.17. [Q8NEV4-1]
DR GeneID; 53904; -.
DR KEGG; hsa:53904; -.
DR MANE-Select; ENST00000642920.2; ENSP00000495965.1; NM_017433.5; NP_059129.3.
DR UCSC; uc001ism.3; human. [Q8NEV4-1]
DR CTD; 53904; -.
DR DisGeNET; 53904; -.
DR GeneCards; MYO3A; -.
DR GeneReviews; MYO3A; -.
DR HGNC; HGNC:7601; MYO3A.
DR HPA; ENSG00000095777; Group enriched (retina, testis).
DR MalaCards; MYO3A; -.
DR MIM; 606808; gene.
DR MIM; 607101; phenotype.
DR neXtProt; NX_Q8NEV4; -.
DR OpenTargets; ENSG00000095777; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA31405; -.
DR VEuPathDB; HostDB:ENSG00000095777; -.
DR eggNOG; KOG0587; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155939; -.
DR HOGENOM; CLU_000192_10_1_1; -.
DR InParanoid; Q8NEV4; -.
DR OMA; RDICPRN; -.
DR OrthoDB; 36742at2759; -.
DR PhylomeDB; Q8NEV4; -.
DR TreeFam; TF326512; -.
DR PathwayCommons; Q8NEV4; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q8NEV4; -.
DR SIGNOR; Q8NEV4; -.
DR BioGRID-ORCS; 53904; 8 hits in 1104 CRISPR screens.
DR GeneWiki; MYO3A; -.
DR GenomeRNAi; 53904; -.
DR Pharos; Q8NEV4; Tbio.
DR PRO; PR:Q8NEV4; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8NEV4; protein.
DR Bgee; ENSG00000095777; Expressed in islet of Langerhans and 104 other tissues.
DR ExpressionAtlas; Q8NEV4; baseline and differential.
DR Genevisible; Q8NEV4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0032433; C:filopodium tip; IDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0001917; C:photoreceptor inner segment; IBA:GO_Central.
DR GO; GO:0032426; C:stereocilium tip; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0060002; F:plus-end directed microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0090103; P:cochlea morphogenesis; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0030832; P:regulation of actin filament length; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd01379; MYSc_Myo3; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036083; MYSc_Myo3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; ATP-binding;
KW Cell projection; Cytoplasm; Cytoskeleton; Deafness; Hearing; Kinase;
KW Motor protein; Myosin; Non-syndromic deafness; Nucleotide-binding;
KW Reference proteome; Repeat; Sensory transduction;
KW Serine/threonine-protein kinase; Transferase; Vision.
FT CHAIN 1..1616
FT /note="Myosin-IIIa"
FT /id="PRO_0000086413"
FT DOMAIN 21..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 338..1053
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1055..1084
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1082..1111
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1346..1375
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 934..956
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1401..1479
FT /note="Interaction with MORN4"
FT /evidence="ECO:0000269|PubMed:25822849"
FT REGION 1545..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1581..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 245..247
FT /note="NPP -> SDD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056231"
FT VAR_SEQ 248..1616
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056232"
FT VARIANT 178
FT /note="T -> I (in dbSNP:rs33968748)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040871"
FT VARIANT 204
FT /note="D -> N (in dbSNP:rs3737274)"
FT /id="VAR_021866"
FT VARIANT 319
FT /note="R -> H (in dbSNP:rs3824700)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040872"
FT VARIANT 348
FT /note="I -> V (in dbSNP:rs3824699)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040873"
FT VARIANT 369
FT /note="V -> I (in dbSNP:rs3817420)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040874"
FT VARIANT 525
FT /note="N -> K (in an ovarian mucinous carcinoma sample;
FT somatic mutation; dbSNP:rs1423134583)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040875"
FT VARIANT 833
FT /note="A -> S (in dbSNP:rs33947968)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040876"
FT VARIANT 956
FT /note="S -> N (in dbSNP:rs3758449)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_021867"
FT VARIANT 956
FT /note="S -> R (in an ovarian serous carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040877"
FT VARIANT 1032
FT /note="A -> T (in dbSNP:rs34918608)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040878"
FT VARIANT 1045
FT /note="V -> M (in dbSNP:rs35447806)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040879"
FT VARIANT 1137
FT /note="V -> M (in dbSNP:rs35449183)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040880"
FT VARIANT 1195
FT /note="V -> A (in dbSNP:rs35675577)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040881"
FT VARIANT 1284
FT /note="T -> S (in dbSNP:rs3740231)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_033905"
FT VARIANT 1287
FT /note="P -> T (in dbSNP:rs35575696)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040882"
FT VARIANT 1313
FT /note="R -> S (in dbSNP:rs1999240)"
FT /evidence="ECO:0000269|PubMed:10936054,
FT ECO:0000269|PubMed:12032315, ECO:0000269|PubMed:17344846"
FT /id="VAR_022779"
FT VARIANT 1347
FT /note="D -> H (in a renal clear cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040883"
FT VARIANT 1417
FT /note="T -> I (in dbSNP:rs34151474)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040884"
FT VARIANT 1488
FT /note="K -> E (in dbSNP:rs34204285)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040885"
FT CONFLICT 418
FT /note="M -> I (in Ref. 1; AAF70861 and 2; AAM34500)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="A -> V (in Ref. 1; AAF70861 and 2; AAM34500)"
FT /evidence="ECO:0000305"
FT CONFLICT 848..851
FT /note="RDTL -> KTLV (in Ref. 2; AAM34500)"
FT /evidence="ECO:0000305"
FT CONFLICT 886..890
FT /note="TKNVI -> LKML (in Ref. 2; AAM34500)"
FT /evidence="ECO:0000305"
FT CONFLICT 1099
FT /note="R -> G (in Ref. 1; AAF70861 and 2; AAM34500)"
FT /evidence="ECO:0000305"
FT CONFLICT 1217
FT /note="S -> F (in Ref. 1; AAF70861 and 2; AAM34500)"
FT /evidence="ECO:0000305"
FT CONFLICT 1378
FT /note="R -> K (in Ref. 1; AAF70861 and 2; AAM34500)"
FT /evidence="ECO:0000305"
FT HELIX 1414..1445
FT /evidence="ECO:0007829|PDB:6JLE"
FT HELIX 1452..1454
FT /evidence="ECO:0007829|PDB:6JLE"
SQ SEQUENCE 1616 AA; 186208 MW; 7D126A7E22520574 CRC64;
MFPLIGKTII FDNFPDPSDT WEITETIGKG TYGKVFKVLN KKNGQKAAVK ILDPIHDIDE
EIEAEYNILK ALSDHPNVVR FYGIYFKKDK VNGDKLWLVL ELCSGGSVTD LVKGFLKRGE
RMSEPLIAYI LHEALMGLQH LHNNKTIHRD VKGNNILLTT EGGVKLVDFG VSAQLTSTRH
RRNTSVGTPF WMAPEVIACE QQLDTTYDAR CDTWSLGITA IELGDGDPPL ADLHPMRALF
KIPRNPPPKL RQPELWSAEF NDFISKCLTK DYEKRPTVSE LLQHKFITQI EGKDVMLQKQ
LTEFIGIHQC MGGTEKARRE RIHTKKGNFN RPLISNLKDV DDLATLEILD ENTVSEQLEK
CYSRDQIYVY VGDILIALNP FQSLGLYSTK HSKLYIGSKR TASPPHIFAM ADLGYQSMIT
YNSDQCIVIS GESGAGKTEN AHLLVQQLTV LGKANNRTLQ EKILQVNNLV EAFGNACTII
NDNSSRFGKY LEMKFTSSGA VVGAQISEYL LEKSRVIHQA IGEKNFHIFY YIYAGLAEKK
KLAHYKLPEN KPPRYLQNDH LRTVQDIMNN SFYKSQYELI EQCFKVIGFT MEQLGSIYSI
LAAILNVGNI EFSSVATEHQ IDKSHISNHT ALENCASLLC IRADELQEAL TSHCVVTRGE
TIIRPNTVEK ATDVRDAMAK TLYGRLFSWI VNCINSLLKH DSSPSGNGDE LSIGILDIFG
FENFKKNSFE QLCINIANEQ IQYYYNQHVF AWEQNEYLNE DVDARVIEYE DNWPLLDMFL
QKPMGLLSLL DEESRFPKAT DQTLVEKFEG NLKSQYFWRP KRMELSFGIH HYAGKVLYNA
SGFLAKNRDT LPTDIVLLLR SSDNSVIRQL VNHPLTKTGN LPHSKTKNVI NYQMRTSEKL
INLAKGDTGE ATRHARETTN MKTQTVASYF RYSLMDLLSK MVVGQPHFVR CIKPNSERQA
RKYDKEKVLL QLRYTGILET ARIRRLGFSH RILFANFIKR YYLLCYKSSE EPRMSPDTCA
TILEKAGLDN WALGKTKVFL KYYHVEQLNL MRKEAIDKLI LIQACVRAFL CSRRYQKIQE
KRKESAIIIQ SAARGHLVRK QRKEIVDMKN TAVTTIQTSD QEFDYKKNFE NTRESFVKKQ
AENAISANER FISAPNNKGS VSVVKTSTFK PEEETTNAVE SNNRVYQTPK KMNNVYEEEV
KQEFYLVGPE VSPKQKSVKD LEENSNLRKV EKEEAMIQSY YQRYTEERNC EESKAAYLER
KAISERPSYP VPWLAENETS FKKTLEPTLS QRSIYQNANS MEKEKKTSVV TQRAPICSQE
EGRGRLRHET VKERQVEPVT QAQEEEDKAA VFIQSKYRGY KRRQQLRKDK MSSFKHQRIV
TTPTEVARNT HNLYSYPTKH EEINNIKKKD NKDSKATSER EACGLAIFSK QISKLSEEYF
ILQKKLNEMI LSQQLKSLYL GVSHHKPINR RVSSQQCLSG VCKGEEPKIL RPPRRPRKPK
TLNNPEDSTY YYLLHKSIQE EKRRPRKDSQ GKLLDLEDFY YKEFLPSRSG PKEHSPSLRE
RRPQQELQNQ CIKANERCWA AESPEKEEER EPAANPYDFR RLLRKTSQRR RLVQQS
