MYO10_MOUSE
ID MYO10_MOUSE Reviewed; 2062 AA.
AC F8VQB6; Q8R3S0; Q9JJY5;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Unconventional myosin-X;
DE AltName: Full=Unconventional myosin-10;
GN Name=Myo10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=10799329; DOI=10.1006/bbrc.2000.2669;
RA Yonezawa S., Kimura A., Koshiba S., Masaki S., Ono T., Hanai A., Sonta S.,
RA Kageyama T., Takahashi T., Moriyama A.;
RT "Mouse myosin X: molecular architecture and tissue expression as revealed
RT by northern blot and in situ hybridization analyses.";
RL Biochem. Biophys. Res. Commun. 271:526-533(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PROTEIN SEQUENCE OF 2-15 (ISOFORM HEADLESS), FUNCTION (ISOFORM HEADLESS),
RP REMOVAL OF INITIAL METHIONINE (ISOFORM HEADLESS), ALTERNATIVE PROMOTER
RP USAGE, AND TISSUE SPECIFICITY.
RX PubMed=22661706; DOI=10.1074/jbc.m112.369173;
RA Raines A.N., Nagdas S., Kerber M.L., Cheney R.E.;
RT "Headless Myo10 is a negative regulator of full-length Myo10 and inhibits
RT axon outgrowth in cortical neurons.";
RL J. Biol. Chem. 287:24873-24883(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1139-2062.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 SAH DOMAIN.
RX PubMed=16030012; DOI=10.1074/jbc.m504887200;
RA Knight P.J., Thirumurugan K., Xu Y., Wang F., Kalverda A.P.,
RA Stafford W.F. III, Sellers J.R., Peckham M.;
RT "The predicted coiled-coil domain of myosin 10 forms a novel elongated
RT domain that lengthens the head.";
RL J. Biol. Chem. 280:34702-34708(2005).
RN [6]
RP FUNCTION, INTERACTION WITH DCC AND NEO1, AND SUBCELLULAR LOCATION.
RX PubMed=17237772; DOI=10.1038/ncb1535;
RA Zhu X.J., Wang C.Z., Dai P.G., Xie Y., Song N.N., Liu Y., Du Q.S., Mei L.,
RA Ding Y.Q., Xiong W.C.;
RT "Myosin X regulates netrin receptors and functions in axonal path-
RT finding.";
RL Nat. Cell Biol. 9:184-192(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, INTERACTION WITH TUBULIN, AND SUBCELLULAR LOCATION.
RX PubMed=20081229; DOI=10.1074/jbc.m109.017269;
RA McMichael B.K., Cheney R.E., Lee B.S.;
RT "Myosin X regulates sealing zone patterning in osteoclasts through linkage
RT of podosomes and microtubules.";
RL J. Biol. Chem. 285:9506-9515(2010).
RN [9]
RP FUNCTION (ISOFORMS 1 AND HEADLESS), AND SUBCELLULAR LOCATION.
RX PubMed=23943878; DOI=10.1242/jcs.132969;
RA Lin W.H., Hurley J.T., Raines A.N., Cheney R.E., Webb D.J.;
RT "Myosin X and its motorless isoform differentially modulate dendritic spine
RT development by regulating trafficking and retention of vasodilator-
RT stimulated phosphoprotein.";
RL J. Cell Sci. 126:4756-4768(2013).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. MYO10 binds to
CC actin filaments and actin bundles and functions as a plus end-directed
CC motor. Moves with higher velocity and takes larger steps on actin
CC bundles than on single actin filaments (By similarity). The tail domain
CC binds to membranous compartments containing phosphatidylinositol 3,4,5-
CC trisphosphate or integrins, and mediates cargo transport along actin
CC filaments (By similarity). Regulates cell shape, cell spreading and
CC cell adhesion. Stimulates the formation and elongation of filopodia. In
CC hippocampal neurons it induces the formation of dendritic filopodia by
CC trafficking the actin-remodeling protein VASP to the tips of filopodia,
CC where it promotes actin elongation. Plays a role in formation of the
CC podosome belt in osteoclasts. {ECO:0000250|UniProtKB:Q9HD67,
CC ECO:0000269|PubMed:17237772, ECO:0000269|PubMed:20081229}.
CC -!- FUNCTION: [Isoform Headless]: Functions as a dominant-negative
CC regulator of isoform 1, suppressing its filopodia-inducing and axon
CC outgrowth-promoting activities. In hippocampal neurons, it increases
CC VASP retention in spine heads to induce spine formation and spine head
CC expansion. {ECO:0000269|PubMed:23943878}.
CC -!- SUBUNIT: Monomer, when in an inactive conformation in the cytosol.
CC Homodimer in its active, membrane-bound conformation; antiparallel
CC coiled coil-mediated dimer formation. Interacts with ECPAS. Interacts
CC with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding.
CC Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding.
CC Interacts strongly with CALM3 and weakly with CALM, the CALM3
CC interaction is essential for function in filopodial extension and
CC motility. Interacts with ITGB1, ITGB3 and ITGB5 (By similarity).
CC Interacts with NEO1. Interacts with VASP. {ECO:0000250,
CC ECO:0000269|PubMed:17237772, ECO:0000269|PubMed:20081229}.
CC -!- INTERACTION:
CC F8VQB6; P97798: Neo1; NbExp=3; IntAct=EBI-6445959, EBI-774991;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection,
CC lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}.
CC Cytoplasm, cytoskeleton. Cell projection, filopodium tip. Cytoplasm,
CC cell cortex. Cell projection, filopodium membrane; Peripheral membrane
CC protein. Note=May be in an inactive, monomeric conformation in the
CC cytosol. Detected in cytoplasmic punctae and in cell projections.
CC Colocalizes with actin fibers. Interacts with microtubules. Undergoes
CC forward and rearward movements within filopodia. Interaction with
CC membranes containing phosphatidylinositol 3,4,5-trisphosphate mediates
CC localization at filopodium membranes (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1; Synonyms=240kDa, FL-myo10;
CC IsoId=F8VQB6-1; Sequence=Displayed;
CC Name=Headless; Synonyms=165kDa, Hdl-myo10;
CC IsoId=F8VQB6-2; Sequence=VSP_054978;
CC -!- TISSUE SPECIFICITY: Detected in brain, heart, kidney, liver, stomach,
CC skeletal muscle, lung, testis and skin. Isoform Headless is expressed
CC in embryonic and neuronal stem cells, and enriched in proliferating and
CC migrating cells. {ECO:0000269|PubMed:10799329,
CC ECO:0000269|PubMed:22661706}.
CC -!- DOMAIN: Interaction between the motor domain and the tail leads to an
CC inactive, monomeric conformation. Phospholipid binding via the PH
CC domains leads to the formation of the active, dimeric form of the
CC protein and strongly increases actin-dependent ATPase activity and
CC motor activity (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Interacts with membranes containing phosphatidylinositol-3,4,5-
CC trisphosphate via the PH domains. {ECO:0000250}.
CC -!- DOMAIN: IQ 3 domain mediates high-affinity calcium-dependent binding to
CC CALM3/CLP. {ECO:0000250}.
CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high
CC content of charged residues which are predicted to stabilize the alpha-
CC helical structure by ionic bonds (PubMed:16030012). It can refold after
CC extension suggesting an in vivo force-dependent function (By
CC similarity). An anti-parallel coiled coil is located C-terminal to the
CC SAH domain and mediates dimerization (By similarity).
CC {ECO:0000250|UniProtKB:P79114, ECO:0000250|UniProtKB:Q9HD67,
CC ECO:0000269|PubMed:16030012}.
CC -!- PTM: The initiator methionine for isoform Headless is removed.
CC -!- MISCELLANEOUS: [Isoform Headless]: Produced by alternative promoter
CC usage. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-10 (MYH10). {ECO:0000305}.
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DR EMBL; AJ249706; CAB56466.2; -; mRNA.
DR EMBL; AC115746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024692; AAH24692.1; -; mRNA.
DR CCDS; CCDS37049.1; -. [F8VQB6-1]
DR PIR; A59297; A59297.
DR RefSeq; NP_062345.2; NM_019472.2. [F8VQB6-1]
DR RefSeq; XP_006520088.1; XM_006520025.3. [F8VQB6-2]
DR AlphaFoldDB; F8VQB6; -.
DR SMR; F8VQB6; -.
DR BioGRID; 201661; 5.
DR IntAct; F8VQB6; 4.
DR STRING; 10090.ENSMUSP00000106087; -.
DR iPTMnet; F8VQB6; -.
DR PhosphoSitePlus; F8VQB6; -.
DR EPD; F8VQB6; -.
DR jPOST; F8VQB6; -.
DR MaxQB; F8VQB6; -.
DR PaxDb; F8VQB6; -.
DR PeptideAtlas; F8VQB6; -.
DR PRIDE; F8VQB6; -.
DR ProteomicsDB; 293602; -. [F8VQB6-1]
DR ProteomicsDB; 293603; -. [F8VQB6-2]
DR Antibodypedia; 4455; 130 antibodies from 24 providers.
DR DNASU; 17909; -.
DR Ensembl; ENSMUST00000110457; ENSMUSP00000106087; ENSMUSG00000022272. [F8VQB6-1]
DR GeneID; 17909; -.
DR KEGG; mmu:17909; -.
DR UCSC; uc007vjc.1; mouse. [F8VQB6-1]
DR CTD; 4651; -.
DR MGI; MGI:107716; Myo10.
DR VEuPathDB; HostDB:ENSMUSG00000022272; -.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155469; -.
DR HOGENOM; CLU_001626_1_0_1; -.
DR InParanoid; F8VQB6; -.
DR OMA; CEKGNIQ; -.
DR PhylomeDB; F8VQB6; -.
DR TreeFam; TF316834; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR BioGRID-ORCS; 17909; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Myo10; mouse.
DR PRO; PR:F8VQB6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; F8VQB6; protein.
DR Bgee; ENSMUSG00000022272; Expressed in floor plate of midbrain and 268 other tissues.
DR ExpressionAtlas; F8VQB6; baseline and differential.
DR Genevisible; F8VQB6; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IDA:MGI.
DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032433; C:filopodium tip; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0060002; F:plus-end directed microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0048870; P:cell motility; IC:MGI.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; ISS:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IGI:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13202; FERM_C_MyoX; 1.
DR CDD; cd14873; MYSc_Myo10; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.530; -; 1.
DR Gene3D; 2.30.29.30; -; 4.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR031971; MYO10_CC.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041797; MyoX_FERM_C.
DR InterPro; IPR040640; MyoX_N_SH3.
DR InterPro; IPR036124; MYSc_Myo10.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF16735; MYO10_CC; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF18597; SH3_19; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 1.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 1.
DR SMART; SM00233; PH; 2.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative promoter usage; ATP-binding;
KW Calmodulin-binding; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Membrane; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Transport.
FT CHAIN 1..2062
FT /note="Unconventional myosin-X"
FT /id="PRO_0000416244"
FT DOMAIN 63..739
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 742..771
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 765..794
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 788..817
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1216..1314
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1396..1501
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1551..1699
FT /note="MyTH4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1704..2048
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 619..641
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 814..882
FT /note="SAH"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT REGION 822..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 883..933
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT COMPBIAS 1006..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT BINDING 160..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZJP6"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZJP6"
FT MOD_RES 1162
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZJP6"
FT VAR_SEQ 1..643
FT /note="Missing (in isoform Headless)"
FT /evidence="ECO:0000305"
FT /id="VSP_054978"
FT CONFLICT 77..78
FT /note="GS -> VA (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 253..254
FT /note="QN -> RI (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="G -> E (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="G -> R (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 870
FT /note="E -> A (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="N -> S (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 993
FT /note="A -> E (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1032
FT /note="D -> E (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1042
FT /note="Y -> D (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1083
FT /note="N -> P (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1371
FT /note="D -> Y (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1602
FT /note="D -> H (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1647
FT /note="R -> L (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1805
FT /note="S -> G (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1939
FT /note="N -> T (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1982
FT /note="D -> E (in Ref. 1; CAB56466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2062 AA; 237323 MW; FD685BEE8B88DE30 CRC64;
MDSFFPEGAR VWLRENGQHF PSTVNSCAEG VVVFQTDYGQ VFTYKQSTIT NQKVTAMHPL
HEEGVDDMAS LAELHGGSIM YNLFQRYKRN QIYTYIGSII ASVNPYQPIA GLYERATMEE
YSRCHLGELP PHIFAIANEC YRCLWKRHDN QCVLISGESG AGKTESTKLI LKFLSVISQQ
TLDLGLQEKT SSVEQAILQS SPIMEAFGNA KTVYNNNSSR FGKFVQLNIC QQGNIQGGRI
VDYLLEKNRV VRQNPGERNY HIFYALLAGL DQGEREEFYL SLPENYHYLN QSGCTEDKTI
SDQESFRQVI TAMEVMQFSK EEVREVLRLL AGILHLGNIE FITAGGAQIP FKTALGRSAD
LLGLDPTQLT DALTQRSMIL RGEEILTPLS VQQAVDSRDS LAMALYARCF EWVIKKINSR
IKGKDDFKSI GILDIFGFEN FEVNHFEQFN INYANEKLQE YFNKHIFSLE QLEYSREGLV
WEDIDWIDNG ECLDLIEKKL GLLALINEES HFPQATDSTL LEKLHSQHAN NHFYVKPRVA
VNNFGVKHYA GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH VSSRNNQDTL
KCGSKHRRPT VSSQFKDSLH SLMATLSSSN PFFVRCIKPN TQKMPDQFDQ VVVLNQLRYS
GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RNLALPDDIR GKCTVLLQVY DASNSEWQLG
KTKVFLRESL EQKLEKRREE EIDRAAMVIR AHILGYLARK QYRKVLCGVV TIQKNYRAFL
ARKKFLHLKK AAIVFQKQLR GQLARRVYRQ LLAEKRELEE KKRREEEKKR EEEERERERA
QREADLLRAH QEAETRRQQE LEALQKSQRE ADLTRELEKQ RENKQVEEIL RLEKEIEDLQ
RMKERQELSL TEASLQKLQQ LRDEELRRLE DEACRAAQEF LESLNFDEID ECVRNIERSL
SVGSEISGEE LSELAESASG EKPNFNFSQP YPAEEEVDEG FEADDDAFKD SPNPSEHGHS
DQRTSGIRTS DDSSEEDPYM NYTVVPTSPS ADSTVLLAAS MQDSASLHNS SSGESTYCMP
QNNGDLPSPD GDYDYDQDDY EDGAITSGSS VTFSNSYGSQ WSPDYRYSVG TYNSSGAYRF
SSEGAQSSFE DSEEDFDSRF DTDDELSYRR DSVYSCVTLP YFHSFLYMKG GLMNSWKRRW
CVLKDETFLW FRSKQEALKQ GWLHKKGGGS STLSRRNWKK RWFVLRQSKL MYFENDSEEK
LKGTVEVRTA KEIIDNTSKE NGIDIILADR TFHLIAESPE DASQWFSVLS QVHSSTDQEI
REMHDEQANP QNAVGTLDVG LIDSVCASDS PDRPNSFVII TANRVLHCNA DTPEEMHHWI
TLLQRSKGDT RVEGQEFIVR GWLHKEVKNS PKMSSLKLKK RWFVLTHNSL DYYKSSEKNA
LKLGTLVLNS LCSVVPPDEK IFKETGYWNV TVYGRKHCYR LYTKLLNEAT RWSSAIQNVT
DTKAPIDTPT QQLIQDIKEN CLNSDVVEQI YKRNPILRYT HHPLHSPLLP LPYGDINLNL
LKDKGYTTLQ DEAIKIFNSL QQLESMSDPI PIIQGILQTG HDLRPLRDEL YCQLIKQTNK
VPHPGSVGNL YSWQILTCLS CTFLPSRGIL KYLKFHLKRI REQFPGTEME KYALFIYESL
KKTKCREFVP SRDEIEALIH RQEMTSTVYC HGGGSCKITI NSHTTAGEVV EKLIRGLAME
DSRNMFALFE YNGQVDKAIE SRTIVADVLA KFEKLAATSE AGDAPWKFYF KLYCFLDTDS
MPKDSVEFAF MFEQAHEAVI HGHHPAPEES LQVLAALRLQ YLQGDYTPHT SIPPLEEVYS
VQRLRARISQ STKTFTPYER LEKRRTSFLE GTLRRSFRTG SVVRQKAEEE QMLDMWIKEE
VCSARTSIID KWKKLQGMNQ EQAMAKYMAL IKEWPGYGST LFDVECKEGG FPQELWLGVS
ADAVSVYKRG EGKPLEVFQY EHILSFGAPL ANTYKIVVDE RELLFETSEV VDVAKLMKAY
ISMIVKKRYS TTRSVSSQGS SR
