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   24-JAN-2024, entry version 186.
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   CCDS; CCDS91223.1; -. [Q8NEV4-2]
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; 4.
DR   STRING; 9606.ENSP00000495965; -.
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; 9606-ENSP00000265944; -.
DR   PeptideAtlas; Q8NEV4; -.
DR   ProteomicsDB; 73220; -. [Q8NEV4-1]
DR   Antibodypedia; 25882; 158 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   AGR; HGNC:7601; -.
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; Rare 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; MVESCEM; -.
DR   OrthoDB; 1094820at2759; -.
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; 9 hits in 1182 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 106 other cell types or tissues.
DR   ExpressionAtlas; Q8NEV4; baseline and differential.
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: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; cd21956; MBD_Myo3a; 1.
DR   CDD; cd01379; MYSc_Myo3; 1.
DR   CDD; cd06638; STKc_myosinIIIA_N; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR46256; AGAP011099-PA; 1.
DR   PANTHER; PTHR46256:SF4; MYOSIN-IIIA; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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.
DR   Genevisible; Q8NEV4; HS.
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
//