MYO15_MOUSE
ID MYO15_MOUSE Reviewed; 3511 AA.
AC Q9QZZ4; A2A637; A2A638; O70395; Q5SX93; Q7TMR5; Q7TMR6; Q9QWL6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Unconventional myosin-XV;
DE AltName: Full=Unconventional myosin-15;
GN Name=Myo15a; Synonyms=Myo15;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10552926; DOI=10.1006/geno.1999.5976;
RA Liang Y., Wang A., Belyantseva I.A., Anderson D.W., Probst F.J.,
RA Barber T.D., Miller W., Touchman J.W., Jin L., Sullivan S.L., Sellers J.R.,
RA Camper S.A., Lloyd R.V., Kachar B., Friedman T.B., Fridell R.A.;
RT "Characterization of the human and mouse unconventional myosin XV genes
RT responsible for hereditary deafness DFNB3 and shaker 2.";
RL Genomics 61:243-258(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14610277; DOI=10.1073/pnas.2334417100;
RA Belyantseva I.A., Boger E.T., Friedman T.B.;
RT "Myosin XVa localizes to the tips of inner ear sensory cell stereocilia and
RT is essential for staircase formation of the hair bundle.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13958-13963(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1168-2970 (ISOFORM 1), AND VARIANT SH-2
RP TYR-1779.
RC TISSUE=Embryo;
RX PubMed=9603735; DOI=10.1126/science.280.5368.1444;
RA Probst F.J., Fridell R.A., Raphael Y., Saunders T.L., Wang A., Liang Y.,
RA Morell R.J., Touchman J.W., Lyons R.H., Noben-Trauth K., Friedman T.B.,
RA Camper S.A.;
RT "Correction of deafness in shaker-2 mice by an unconventional myosin in a
RT BAC transgene.";
RL Science 280:1444-1447(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1237-1823, AND VARIANT SH-2 TYR-1779.
RC STRAIN=C57BL/6J;
RX PubMed=9703981; DOI=10.1006/bbrc.1998.8976;
RA Wakabayashi Y., Takahashi Y., Kikkawa Y., Okano H., Mishima Y., Ushiki T.,
RA Yonekawa H., Kominami R.;
RT "A novel type of myosin encoded by the mouse deafness gene shaker-2.";
RL Biochem. Biophys. Res. Commun. 248:655-659(1998).
RN [6]
RP FUNCTION, AND INTERACTION WITH WHRN.
RX PubMed=15654330; DOI=10.1038/ncb1219;
RA Belyantseva I.A., Boger E.T., Naz S., Frolenkov G.I., Sellers J.R.,
RA Ahmed Z.M., Griffith A.J., Friedman T.B.;
RT "Myosin-XVa is required for tip localization of whirlin and differential
RT elongation of hair-cell stereocilia.";
RL Nat. Cell Biol. 7:148-156(2005).
RN [7]
RP INTERACTION WITH EPS8.
RX PubMed=21236676; DOI=10.1016/j.cub.2010.12.046;
RA Manor U., Disanza A., Grati M., Andrade L., Lin H., Di Fiore P.P.,
RA Scita G., Kachar B.;
RT "Regulation of stereocilia length by myosin XVa and whirlin depends on the
RT actin-regulatory protein Eps8.";
RL Curr. Biol. 21:167-172(2011).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails are presumed to bind to membranous compartments, which
CC would be moved relative to actin filaments (By similarity). Required
CC for the arrangement of stereocilia in mature hair bundles.
CC {ECO:0000250, ECO:0000269|PubMed:14610277,
CC ECO:0000269|PubMed:15654330}.
CC -!- SUBUNIT: Interacts with the third PDZ domain of WHRN which is necessary
CC for localization of WHRN to stereocilium tips. Interacts with FASLG (By
CC similarity). Interacts with EPS8. {ECO:0000250,
CC ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:21236676}.
CC -!- INTERACTION:
CC Q9QZZ4; Q80VW5: Whrn; NbExp=5; IntAct=EBI-4281382, EBI-7417603;
CC -!- SUBCELLULAR LOCATION: Cell projection, stereocilium
CC {ECO:0000269|PubMed:14610277}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14610277}. Note=Localizes to stereocilium tips in
CC cochlear and vestibular hair cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9QZZ4-1; Sequence=Displayed;
CC Name=2; Synonyms=1a;
CC IsoId=Q9QZZ4-2; Sequence=VSP_029945;
CC Name=3; Synonyms=2a;
CC IsoId=Q9QZZ4-3; Sequence=VSP_029944, VSP_029945;
CC -!- TISSUE SPECIFICITY: In the developing inner ear, expressed in cochlea
CC and vestibular apparatus. Expression appears to be restricted to
CC cochlear neurosensory cells and upper epithelial layer of macula
CC saccula. Also expressed in macula utriculi and cristae ampullaris of
CC the semicircular canals. In adult cochlear hair cells, highest
CC expression in stereocilia and apical body.
CC {ECO:0000269|PubMed:10552926}.
CC -!- DISEASE: Note=Defects in Myo15a are the cause of shaker-2 (sh-2), a
CC condition causing deafness, circling behavior, head tossing and
CC hyperactivity. Auditory hair cells of affected animals have very short
CC stereocilia and a long actin-containing protrusion at their basal end.
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-15 (MYH15). {ECO:0000305}.
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DR EMBL; AF144095; AAF05904.1; -; mRNA.
DR EMBL; AY331132; AAP88402.1; -; mRNA.
DR EMBL; AY331133; AAP88403.1; -; mRNA.
DR EMBL; AL596090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF053130; AAC40124.1; -; mRNA.
DR EMBL; AB014510; BAA36582.1; -; mRNA.
DR CCDS; CCDS24792.1; -. [Q9QZZ4-1]
DR CCDS; CCDS24793.1; -. [Q9QZZ4-3]
DR CCDS; CCDS48811.1; -. [Q9QZZ4-2]
DR PIR; A59295; A59295.
DR PIR; T42386; T42386.
DR RefSeq; NP_001096641.1; NM_001103171.1. [Q9QZZ4-2]
DR RefSeq; NP_034992.2; NM_010862.2. [Q9QZZ4-1]
DR RefSeq; NP_874357.2; NM_182698.2. [Q9QZZ4-3]
DR RefSeq; XP_017169821.1; XM_017314332.1.
DR RefSeq; XP_017169822.1; XM_017314333.1.
DR PDB; 6Y38; X-ray; 1.70 A; C/D=3499-3511.
DR PDB; 6Y9N; X-ray; 1.93 A; B=3499-3511.
DR PDB; 7R91; EM; 2.83 A; D=1205-1889.
DR PDB; 7RB8; EM; 3.63 A; D=1205-1889.
DR PDB; 7RB9; EM; 3.76 A; D=1205-1889.
DR PDBsum; 6Y38; -.
DR PDBsum; 6Y9N; -.
DR PDBsum; 7R91; -.
DR PDBsum; 7RB8; -.
DR PDBsum; 7RB9; -.
DR SMR; Q9QZZ4; -.
DR BioGRID; 201662; 4.
DR IntAct; Q9QZZ4; 4.
DR MINT; Q9QZZ4; -.
DR STRING; 10090.ENSMUSP00000071777; -.
DR iPTMnet; Q9QZZ4; -.
DR PhosphoSitePlus; Q9QZZ4; -.
DR jPOST; Q9QZZ4; -.
DR MaxQB; Q9QZZ4; -.
DR PaxDb; Q9QZZ4; -.
DR PRIDE; Q9QZZ4; -.
DR ProteomicsDB; 287576; -. [Q9QZZ4-1]
DR ProteomicsDB; 287577; -. [Q9QZZ4-2]
DR Antibodypedia; 58384; 34 antibodies from 13 providers.
DR DNASU; 17910; -.
DR Ensembl; ENSMUST00000071880; ENSMUSP00000071777; ENSMUSG00000042678. [Q9QZZ4-1]
DR Ensembl; ENSMUST00000081823; ENSMUSP00000080507; ENSMUSG00000042678. [Q9QZZ4-3]
DR Ensembl; ENSMUST00000094135; ENSMUSP00000091686; ENSMUSG00000042678. [Q9QZZ4-2]
DR GeneID; 17910; -.
DR KEGG; mmu:17910; -.
DR UCSC; uc007jfz.1; mouse. [Q9QZZ4-1]
DR UCSC; uc007jga.1; mouse. [Q9QZZ4-3]
DR UCSC; uc007jgb.2; mouse. [Q9QZZ4-2]
DR CTD; 17910; -.
DR MGI; MGI:1261811; Myo15.
DR VEuPathDB; HostDB:ENSMUSG00000042678; -.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155335; -.
DR InParanoid; Q9QZZ4; -.
DR OMA; AIQSMIT; -.
DR OrthoDB; 14609at2759; -.
DR PhylomeDB; Q9QZZ4; -.
DR TreeFam; TF316834; -.
DR BioGRID-ORCS; 17910; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Myo15; mouse.
DR PRO; PR:Q9QZZ4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QZZ4; protein.
DR Bgee; ENSMUSG00000042678; Expressed in epithelium of saccule and 23 other tissues.
DR ExpressionAtlas; Q9QZZ4; baseline and differential.
DR Genevisible; Q9QZZ4; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0098858; C:actin-based cell projection; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032420; C:stereocilium; IDA:MGI.
DR GO; GO:0032421; C:stereocilium bundle; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13201; FERM_C_MyoXV; 1.
DR CDD; cd01387; MYSc_Myo15; 1.
DR Gene3D; 1.25.40.530; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.850.10; -; 1.
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; IPR035487; MYO15A.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041795; MyoXV_FERM_C.
DR InterPro; IPR036057; MYSc_Myo15.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22692:SF21; PTHR22692:SF21; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; ATP-binding;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Deafness;
KW Disease variant; Hearing; Motor protein; Myosin; Nucleotide-binding;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..3511
FT /note="Unconventional myosin-XV"
FT /id="PRO_0000123475"
FT DOMAIN 1206..1883
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1886..1908
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1909..1938
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2049..2195
FT /note="MyTH4 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 2848..2934
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 3031..3185
FT /note="MyTH4 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 3190..3511
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..1783
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 1872..2013
FT /note="Neck or regulatory domain"
FT REGION 2014..3511
FT /note="Tail"
FT REGION 2330..2359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2392..2425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2460..2509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2565..2584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2629..2648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2964..2984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1307..1334
FT /evidence="ECO:0000255"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..809
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..936
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2340..2355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2629..2643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1299..1306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..1187
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14610277"
FT /id="VSP_029944"
FT VAR_SEQ 1955..1972
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14610277"
FT /id="VSP_029945"
FT VARIANT 1779
FT /note="C -> Y (in sh-2)"
FT /evidence="ECO:0000269|PubMed:9603735,
FT ECO:0000269|PubMed:9703981"
FT CONFLICT 1141
FT /note="R -> C (in Ref. 1; AAF05904 and 2; AAP88402)"
FT /evidence="ECO:0000305"
FT CONFLICT 1330..1331
FT /note="Missing (in Ref. 4; AAC40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 1579
FT /note="L -> R (in Ref. 5; BAA36582)"
FT /evidence="ECO:0000305"
FT CONFLICT 2077
FT /note="L -> M (in Ref. 4; AAC40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 2139
FT /note="L -> P (in Ref. 4; AAC40124)"
FT /evidence="ECO:0000305"
FT CONFLICT 2953
FT /note="A -> V (in Ref. 1; AAF05904 and 2; AAP88402/
FT AAP88403)"
FT /evidence="ECO:0000305"
FT CONFLICT 3195
FT /note="F -> S (in Ref. 1; AAF05904 and 2; AAP88402/
FT AAP88403)"
FT /evidence="ECO:0000305"
FT CONFLICT 3449
FT /note="Q -> K (in Ref. 1; AAF05904 and 2; AAP88402/
FT AAP88403)"
FT /evidence="ECO:0000305"
FT HELIX 1211..1213
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1219..1231
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1237..1239
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1242..1246
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1257..1262
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1275..1289
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1293..1299
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1305..1319
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1326..1332
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1335..1342
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1350..1353
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1355..1364
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1367..1377
FT /evidence="ECO:0007829|PDB:7R91"
FT TURN 1381..1384
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1394..1402
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1405..1411
FT /evidence="ECO:0007829|PDB:7R91"
FT TURN 1416..1418
FT /evidence="ECO:0007829|PDB:7R91"
FT TURN 1420..1424
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1435..1448
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1453..1469
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1474..1478
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1480..1488
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1491..1500
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1504..1512
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1513..1517
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1522..1526
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1529..1558
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1565..1572
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1584..1614
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1615..1617
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1628..1635
FT /evidence="ECO:0007829|PDB:7R91"
FT TURN 1637..1639
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1641..1648
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1656..1667
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1671..1674
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1681..1687
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1690..1695
FT /evidence="ECO:0007829|PDB:7R91"
FT TURN 1699..1703
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1709..1716
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1721..1733
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1754..1767
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1770..1772
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1775..1780
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1793..1802
FT /evidence="ECO:0007829|PDB:7R91"
FT TURN 1803..1805
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1806..1812
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1822..1828
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1829..1831
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1844..1852
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1858..1860
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 1865..1867
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 1874..1888
FT /evidence="ECO:0007829|PDB:7R91"
FT STRAND 3508..3511
FT /evidence="ECO:0007829|PDB:6Y38"
SQ SEQUENCE 3511 AA; 395622 MW; B66F3E06F4B5983E CRC64;
MADEEKKAKK GKKGKKAPEP EKPKRSLKGT SRLFMGFRDR TPKISKKGQF RSASAFFWGL
HTGPQKTKRK KKARTVLKST SKLMTQMRVG KKKRAMKGKK PSFMVIRFPG RRGYGRLRPR
AQSLSKASTA INWLTKKFLL KKAEESGSEQ ATVDAWLQRS SSRVGSRKLP FPSGAEILRH
GGRLRRFPRS HSIYSSGEPV GFLPFEDEAP FRHAGSRKSL YGLEGFQDLG EYYDYHREGD
DYYDQQSLYH YEEQEPYLAE FGGYSPAWPP YDDYGYPPGD PYNYYHPDYY GDTLYPGYAY
GYGYGYDDFE PPYAPPSGYS SPYSYHDSFE SEAYPYSYYL DPYATHHMPY PPYDFPYDTP
YDIPYFDPYG VPYAEGVYGG GAEAIYPPGM PYVYPEEPAF MYPWVPPPIM SPHNPYAHPM
DDIAELEEPE ETGEERQSTS FRLPSAAFFE QQGMDKPARS KLSLIRKFRL FPRPQVKLFG
KEKLEVPLPP SLDIPLPLGD AEGEEEEEEM PPVPTMPYTH PYWSFLTPRQ RNLQRALSAF
GARQGLGFGP EFGHPTPRPA TSLARFLKKT LSEKKPIPRL RGSQKARGGR PPVREAAYKR
FGYKLAGMDP DRPNTPIVLR RSQPQARNNN NSHGPPSPRP APRALTHWSA LISPPMPAPS
PSPASPLTPP FSPTFSRPPR LASPYGSLRQ HPPPWAAPAH VPFPPQANWW GFAEPPGTSP
EVAPDLLAFP VPRPSFRASR SRSRRAAYGF PSPSLIGSRR RPHLPSPQPS LRSLPGQGYH
SPLGPLSPQL SLRRGPFQPP FPPPPRRPQS LREAFSLRRA SGRLGPPRSP VLGSPRPPSP
PPLLKHGPRH RSLNLPSRLP RTWRRLSEPP TRAVKPWVHR AYPPPPSAGP WGASTGALEQ
QENQREAEDS ETPWTVPPLA PSWDVDMPPT QRPPSPWPEG IGSLRGFSRP PPVPENPLLE
HTSPSCEPQS EDRVSNLTGI FLGQHHDPGP GQLTKSADPS LEKPEEVVTL GDPQPPAEPE
ALNPTPPNKN VVSERKVLRL SASYPLVTCK QARATWPQWH RWKTVSRTPA PLAPTRAPGP
LLKAGEQPRA EPGRFAVVMP QVRGVSSFRP KGPAPVQPPE HPDQDPEQGP APQACSLRWP
RLWPPTDAHC LWSRIRTYSS QSHLRGHGGD CHKSLWKKTR PQSWQNKMHS IRNLPSMRSR
EQHREDGVED MTQLEDLQET TVLANLKTRF ERNLIYTYIG SILVSVNPYR MFAIYGPEQV
QQYSGRALGE NPPHLFAIAN LAFAKMLDAK QNQCVIISGE SGSGKTEATK LILRCLAAMN
QRRDVMQQIK ILEATPLLEA FGNAKTVRND NSSRFGKFVE IFLEGGVICG AITSQYLLEK
SRIVFQAKNE RNYHIFYELL AGLPAQLRQA FSLQEAETYY YLNQGGNCEI AGKSDADDFR
RLLAAMEVLG FTSEDQDSIF RILASILHLG NVYFEKHETD AQEVASVVSA REIQAVAELL
QVSPEGLQKA ITFKVTETIR EKIFTPLTVE SAVDARDAIA KVLYALLFGW LITRVNALVS
PKQDTLSIAI LDIYGFEDLS FNSFEQLCIN YANENLQYLF NKIVFQEEQE EYIREQMDWR
EIAFADNQPC INLISLKPYG ILRILDDQCC FPQATDHTFL QKCHYHHGAN PLYSKPKMPL
PEFTIKHYAG KVTYQVHKFL DKNHDQVRQD VLDLFVHSRT RVVAHLFSSH AAQTAPPRLG
KSSSITRLYK AHTVAAKFQQ SLLDLVEKME RCNPLFVRCL KPNHKKEPGL FEPDVMMAQL
RYSGVLETVR IRKEGFPVRL PFQVFIDRYR CLVALKLNVP ADGDMCVSLL SRLCTVTPDM
YRVGISKLFL KEHLHQLLES MRERVQNRAA LTLQRYLRGF FIQRHFRSLR RKIILLQSRA
RGFLARQRYQ QMRQSLLKFR SLVHTYVNRR RYLKLRAEQR RRAQEAWLRE QEELSKREVV
PVRHLEVPAE VAGLLQAAAG LKLSSGPRVA VVRAPRLQAE PCVTLPLDIN NYPMAKFIRC
HFKEPSFGML TVPLKMPLTR LPVEHHAEAI SVFKLILRFM GDPHLHGTQE MILGNYIVHQ
GLVEPALRDE ILAQLANQVW RNPNAYNSKR GWLLLAACLS GFAPSPHLDK FLLKFVSDYG
QNGFQAVCQH RLLQAMGSGA ARTFPPTQLE WTAIQEKASM ALDVSCFNGD QFSCPVHTWS
TGEAVAGDIL KHRGLADGWR GWTVAMKNGV QWAELAGHDY VLDLVSDLEL LRDFPRQKSY
FIVGAEGPLA GRGDTRGVFG NCWDSDEDTP TRPQPQDHVA KMPDLDGYCS HKEDGTNGET
EAQRWTSNRQ AVDSIGESTV PPRELDGYLD SLFDPVLACG DADLEKPTAI AYRMKGGGQP
GGGGGSTSED TSRRPPEPKL KPIPGLDAST LALQQAFIHR QAVLLAREMT LQALALQQQP
LSATSRPQLP ERPLAPEARP KTVVGTGPPA KPVLVRPTPQ SWAPGSVAKA PKIPSKPVAV
PILAQDWTAP ESISASPELV RYSTLNSEHF PQPTQQIRSI IKQYKQPPWA GHPEARRTDG
GKVFRRPPDP HEEALMILKG QKTQLAVVPG TQVSREAVAM VKPVTSAPRP CMGPTPVQPS
RSLEPPEDPV QTQLHRLVNP NFYGYQDIPW RIFLRKEVFY PKDNYSHPVQ LDLLFRQILH
DTFSEACLRI SEDERLQMKA LFAQNQLDTQ RPLVTESVKR AAISMARDSW EIYFSRLFPA
MGSVGTGVQI LAVSHTGIKL LQMVKGSKEA SRRLRVLCAY SFADILFVTM PSQNMLEFNL
SNEKLILFSA RAQQVKTLVD TFILELKKDS DYVVAVRNFL SEDPELLSFH KGDIIHLQSL
EPTRVGYSAG CVVRKKLVYL EELRRRGPDF GWRFGAVHGR VGRFPSELVQ PAAAPDFLQL
PAEPGRGRAA AVAAAVASAA AAQEVGRRRE GPPVRARSAD SGEDSIALPP STMLEFAQKY
FRDPRRRPRD GLKLKSKEDR ESKTLEDVLC FTKVPIQESL IELSDSNLNK MAVDMFVAVM
RFMGDAPLKG QSELDVLCTL LKLCGDHEVM RDECYCQIVK QITDNSSPKQ DSCQRGWRLL
YIMAAYYSCS EVFYPYLIRF LQHVSWTPGL PFQGIAKACE QNLQKTLRFG GRLEFPSNME
LRAMLAGRSS KRQLFLLPGG LERHLKIKTC TVALDVIEGL CTEMALTRPE AFDEYVIFVV
TNRGQHVCPL SCRAYILDVA SEMEQVDGGY TLWFRRVLWD QPLKFENELY VTMHYNQVLP
DYLKGLFSSV PARQPTEQQL QQVSKLASLQ HRAKDHFYLP SVREVQEYIP AQLYHTTAGD
TWLNLVSQHR QQTQALSPHQ ARAQFLGLLS AFPLFGSSFF FIQSCSNVLV PAPCILAVNH
NGLNFLSTKT HELIVKIPLK EIQSTWTQQP TANSSYPYVE ISLGDVAAQR TMQLQLEQGL
ELCRVVAVHV ESMLSAREER LTLPPSEITL L