ID MYO7A_MOUSE Reviewed; 2215 AA. AC P97479; E9QLP7; Q5MJ57; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 14-OCT-2015, entry version 154. DE RecName: Full=Unconventional myosin-VIIa; GN Name=Myo7a; Synonyms=Myo7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISEASE. RX PubMed=7870172; DOI=10.1038/374062a0; RA Gibson F., Walsh J., Mburu P., Varela A., Brown K.A., Antonio M., RA Beisel K.W., Steel K.P., Brown S.D.M.; RT "A type VII myosin encoded by the mouse deafness gene shaker-1."; RL Nature 374:62-64(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9680294; RA Mburu P., Liu X.-Z., Walsh J., Saw D. Jr., Cope M.J., Gibson F., RA Kendrick-Jones J., Steel K.P., Brown S.D.M.; RT "Mutation analysis of the mouse myosin VIIA deafness gene."; RL Genes Funct. 1:191-203(1997). 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-2215 (ISOFORM 2), AND TISSUE RP SPECIFICITY. RC STRAIN=C57BL/6; TISSUE=Inner ear; 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 RT differential elongation of hair-cell stereocilia."; RL Nat. Cell Biol. 7:148-156(2005). RN [5] RP INTERACTION WITH MYRIP. RX PubMed=12221080; DOI=10.1074/jbc.M203862200; RA Fukuda M., Kuroda T.S.; RT "Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), RT a novel linker protein that interacts with Rab27, myosin Va/VIIa, and RT actin."; RL J. Biol. Chem. 277:43096-43103(2002). RN [6] RP INTERACTION WITH WHRN. RX PubMed=15590698; DOI=10.1093/hmg/ddi036; RA Delprat B., Michel V., Goodyear R., Yamasaki Y., Michalski N., RA El-Amraoui A., Perfettini I., Legrain P., Richardson G., RA Hardelin J.-P., Petit C.; RT "Myosin XVa and whirlin, two deafness gene products required for hair RT bundle growth, are located at the stereocilia tips and interact RT directly."; RL Hum. Mol. Genet. 14:401-410(2005). RN [7] RP INTERACTION WITH PLEKHB1. RX PubMed=15976448; DOI=10.1242/jcs.02424; RA Etournay R., El-Amraoui A., Bahloul A., Blanchard S., Roux I., RA Pezeron G., Michalski N., Daviet L., Hardelin J.-P., Legrain P., RA Petit C.; RT "PHR1, an integral membrane protein of the inner ear sensory cells, RT directly interacts with myosin 1c and myosin VIIa."; RL J. Cell Sci. 118:2891-2899(2005). RN [8] RP INTERACTION WITH PCDH15. RX PubMed=16481439; DOI=10.1523/JNEUROSCI.4251-05.2006; RA Senften M., Schwander M., Kazmierczak P., Lillo C., Shin J.B., RA Hasson T., Geleoc G.S., Gillespie P.G., Williams D., Holt J.R., RA Muller U.; RT "Physical and functional interaction between protocadherin 15 and RT myosin VIIa in mechanosensory hair cells."; RL J. Neurosci. 26:2060-2071(2006). RN [9] RP INTERACTION WITH TWF2. RC STRAIN=C3Heb/FeJ; TISSUE=Inner ear; RX PubMed=19774077; DOI=10.1371/journal.pone.0007097; RA Rzadzinska A.K., Nevalainen E.M., Prosser H.M., Lappalainen P., RA Steel K.P.; RT "MyosinVIIa interacts with Twinfilin-2 at the tips of mechanosensory RT stereocilia in the inner ear."; RL PLoS ONE 4:E7097-E7097(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1563; SER-1569 AND RP THR-1571, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Kidney, and Testis; 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 RT expression."; RL Cell 143:1174-1189(2010). RN [11] RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH RPE65. RX PubMed=21493626; DOI=10.1093/hmg/ddr155; RA Lopes V.S., Gibbs D., Libby R.T., Aleman T.S., Welch D.L., Lillo C., RA Jacobson S.G., Radu R.A., Steel K.P., Williams D.S.; RT "The Usher 1B protein, MYO7A, is required for normal localization and RT function of the visual retinoid cycle enzyme, RPE65."; RL Hum. Mol. Genet. 20:2560-2570(2011). RN [12] RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=21709241; DOI=10.1073/pnas.1104161108; RA Grati M., Kachar B.; RT "Myosin VIIa and sans localization at stereocilia upper tip-link RT density implicates these Usher syndrome proteins in RT mechanotransduction."; RL Proc. Natl. Acad. Sci. U.S.A. 108:11476-11481(2011). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 965-1687 IN COMPLEX WITH RP USH1G, INTERACTION WITH USH1G, AND MUTAGENESIS OF ALA-1189 AND RP PHE-1473. RX PubMed=21311020; DOI=10.1126/science.1198848; RA Wu L., Pan L., Wei Z., Zhang M.; RT "Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo."; RL Science 331:757-760(2011). CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase CC activity. Unconventional myosins serve in intracellular movements. CC Their highly divergent tails bind to membranous compartments, CC which are then moved relative to actin filaments. In the retina, CC plays an important role in the renewal of the outer photoreceptor CC disks. Plays an important role in the distribution and migration CC of retinal pigment epithelial (RPE) melanosomes and phagosomes, CC and in the regulation of opsin transport in retinal CC photoreceptors. Mediates intracellular transport of RPE65 in the CC retina pigment epithelium. In the inner ear, plays an important CC role in differentiation, morphogenesis and organization of CC cochlear hair cell bundles. Motor protein that is a part of the CC functional network formed by USH1C, USH1G, CDH23 and MYO7A that CC mediates mechanotransduction in cochlear hair cells. Required for CC normal hearing. Involved in hair-cell vesicle trafficking of CC aminoglycosides, which are known to induce ototoxicity. CC {ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:21709241}. CC -!- SUBUNIT: Might homodimerize in a two headed molecule through the CC formation of a coiled-coil rod. May interact with CALM (By CC similarity). Binds MYRIP and WHRN. Interacts with PLEKHB1 (via PH CC domain). Identified in a complex with USH1C and USH1G. Interacts CC with RPE65. Interacts with PCDH15. Interacts with TWF2. CC {ECO:0000250, ECO:0000269|PubMed:12221080, CC ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15976448, CC ECO:0000269|PubMed:16481439, ECO:0000269|PubMed:19774077, CC ECO:0000269|PubMed:21311020, ECO:0000269|PubMed:21493626}. CC -!- INTERACTION: CC P18084:ITGB5 (xeno); NbExp=8; IntAct=EBI-1149557, EBI-1223434; CC O70309:Itgb5; NbExp=3; IntAct=EBI-1149557, EBI-8401821; CC Q80T11:Ush1g; NbExp=4; IntAct=EBI-1149557, EBI-7418889; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21709241}. CC Cytoplasm, cell cortex {ECO:0000269|PubMed:21709241}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:21709241}. Note=In the CC photoreceptor cells, mainly localized in the inner and base of CC outer segments as well as in the synaptic ending region. CC Colocalizes with a subset of melanosomes in retinal pigment CC epithelium cells (By similarity). Detected at the tip of cochlear CC hair cell stereocilia. The complex formed by MYO7A, USH1C and CC USH1G colocalizes with F-actin. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P97479-1; Sequence=Displayed; CC Name=2; CC IsoId=P97479-2; Sequence=VSP_042238; CC -!- TISSUE SPECIFICITY: Detected in mechanosensory stereocilia of CC cochlea hair cells (at protein level). Expressed in the retina, CC cochlea, kidney and liver. {ECO:0000269|PubMed:15654330, CC ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:21709241}. CC -!- DEVELOPMENTAL STAGE: In the inner ear of the 16.5 day old embryo, CC expressed only in the cochlear and vestibular sensory hair cells. CC In addition, expression also occurs in the epithelial cells of the CC small intestine, hepatocytes, and choroidal plexus. CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a CC high content of charged residues which are predicted to stabilize CC the alpha-helical structure by ionic bonds. CC {ECO:0000250|UniProtKB:Q13402}. CC -!- DISEASE: Note=Defects in Myo7a are the cause of the shaker-1 (sh- CC 1) phenotype which affects only the inner ear. Sh-1 homozygote CC mutants show hyperactivity, head tossing and circling due to CC vestibular dysfunction, together with typical neuroepithelial-type CC cochlear defects involving dysfunction and progressive CC degeneration of the organ of Corti. {ECO:0000269|PubMed:7870172}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 FERM domains. {ECO:0000255|PROSITE- CC ProRule:PRU00084}. CC -!- SIMILARITY: Contains 5 IQ domains. {ECO:0000255|PROSITE- CC ProRule:PRU00116}. CC -!- SIMILARITY: Contains 1 myosin motor domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 MyTH4 domains. {ECO:0000255|PROSITE- CC ProRule:PRU00359}. CC -!- SIMILARITY: Contains 1 SH3 domain. {ECO:0000255|PROSITE- CC ProRule:PRU00192}. CC -!- CAUTION: Represents an unconventional myosin. This protein should CC not be confused with the conventional myosin-7 (MYH7). CC {ECO:0000305}. CC -!- CAUTION: Originally predicted to contain a coiled coil domain but CC proposed to contain a stable SAH domain instead. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U81453; AAB40708.1; -; mRNA. DR EMBL; AC115022; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC119880; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC157792; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY821853; AAV87212.1; -; mRNA. DR CCDS; CCDS40026.1; -. [P97479-2] DR CCDS; CCDS57565.1; -. [P97479-1] DR PIR; T30870; T30870. DR RefSeq; NP_001243010.1; NM_001256081.1. [P97479-1] DR RefSeq; NP_001243012.1; NM_001256083.1. DR RefSeq; NP_032689.2; NM_008663.2. [P97479-2] DR RefSeq; XP_011239993.1; XM_011241691.1. DR UniGene; Mm.1403; -. DR PDB; 3PVL; X-ray; 2.80 A; A=965-1687. DR PDBsum; 3PVL; -. DR ProteinModelPortal; P97479; -. DR SMR; P97479; 993-1686. DR BioGrid; 201669; 5. DR IntAct; P97479; 4. DR MINT; MINT-1896820; -. DR STRING; 10090.ENSMUSP00000102745; -. DR PhosphoSite; P97479; -. DR MaxQB; P97479; -. DR PaxDb; P97479; -. DR PRIDE; P97479; -. DR Ensembl; ENSMUST00000107127; ENSMUSP00000102744; ENSMUSG00000030761. [P97479-2] DR Ensembl; ENSMUST00000107128; ENSMUSP00000102745; ENSMUSG00000030761. [P97479-1] DR GeneID; 17921; -. DR KEGG; mmu:17921; -. DR UCSC; uc009ijy.2; mouse. [P97479-2] DR UCSC; uc009ijz.2; mouse. [P97479-1] DR CTD; 4647; -. DR MGI; MGI:104510; Myo7a. DR eggNOG; COG5022; -. DR GeneTree; ENSGT00810000125360; -. DR HOGENOM; HOG000007836; -. DR HOVERGEN; HBG052557; -. DR InParanoid; P97479; -. DR KO; K10359; -. DR OMA; TPWHNPS; -. DR OrthoDB; EOG7QG433; -. DR TreeFam; TF335306; -. DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision). DR ChiTaRS; Myo7a; mouse. DR NextBio; 292781; -. DR PRO; PR:P97479; -. DR Proteomes; UP000000589; Chromosome 7. DR Bgee; P97479; -. DR CleanEx; MM_MYO7A; -. DR ExpressionAtlas; P97479; baseline and differential. DR Genevisible; P97479; MM. DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB. DR GO; GO:0042470; C:melanosome; IDA:MGI. DR GO; GO:0005902; C:microvillus; ISA:MGI. DR GO; GO:0031477; C:myosin VII complex; IEA:Ensembl. DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI. DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB. DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB. DR GO; GO:0032420; C:stereocilium; IDA:MGI. DR GO; GO:0045202; C:synapse; IDA:UniProtKB. DR GO; GO:1990435; C:upper tip-link density; IEA:Ensembl. DR GO; GO:0051015; F:actin filament binding; ISO:MGI. DR GO; GO:0030898; F:actin-dependent ATPase activity; IEA:Ensembl. DR GO; GO:0043531; F:ADP binding; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB. DR GO; GO:0000146; F:microfilament motor activity; ISO:MGI. DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI. DR GO; GO:0030507; F:spectrin binding; ISO:MGI. DR GO; GO:0030048; P:actin filament-based movement; ISO:MGI. DR GO; GO:0042491; P:auditory receptor cell differentiation; IMP:MGI. DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI. DR GO; GO:0030030; P:cell projection organization; IMP:MGI. DR GO; GO:0050957; P:equilibrioception; ISO:MGI. DR GO; GO:0048839; P:inner ear development; IMP:MGI. DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI. DR GO; GO:0060113; P:inner ear receptor cell differentiation; IMP:MGI. DR GO; GO:0060122; P:inner ear receptor stereocilium organization; IMP:MGI. DR GO; GO:0006886; P:intracellular protein transport; IMP:MGI. DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB. DR GO; GO:0042490; P:mechanoreceptor differentiation; IMP:MGI. DR GO; GO:0006909; P:phagocytosis; IMP:MGI. DR GO; GO:0001845; P:phagolysosome assembly; IMP:MGI. DR GO; GO:0051875; P:pigment granule localization; IMP:MGI. DR GO; GO:0051904; P:pigment granule transport; IMP:MGI. DR GO; GO:0048563; P:post-embryonic organ morphogenesis; IMP:MGI. DR GO; GO:0007600; P:sensory perception; IMP:MGI. DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:MGI. DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB. DR GO; GO:0007601; P:visual perception; ISS:UniProtKB. DR Gene3D; 1.20.80.10; -; 2. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR000857; MyTH4_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011993; PH/PTB_dom. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR029071; Ubiquitin-rel_dom. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF00612; IQ; 3. DR Pfam; PF00063; Myosin_head; 1. DR Pfam; PF00784; MyTH4; 2. DR PRINTS; PR00193; MYOSINHEAVY. DR SMART; SM00295; B41; 2. DR SMART; SM00015; IQ; 4. DR SMART; SM00242; MYSc; 1. DR SMART; SM00139; MyTH4; 2. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF47031; SSF47031; 2. DR SUPFAM; SSF50044; SSF50044; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF54236; SSF54236; 2. DR PROSITE; PS50057; FERM_3; 2. DR PROSITE; PS50096; IQ; 3. 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 Calmodulin-binding; Complete proteome; Cytoplasm; Cytoskeleton; KW Deafness; Disease mutation; Hearing; Motor protein; Myosin; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; KW SH3 domain; Transport. FT CHAIN 1 2215 Unconventional myosin-VIIa. FT /FTId=PRO_0000123467. FT DOMAIN 65 741 Myosin motor. FT DOMAIN 745 765 IQ 1. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 768 788 IQ 2. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 791 811 IQ 3. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 814 834 IQ 4. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 837 857 IQ 5. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 1017 1253 MyTH4 1. {ECO:0000255|PROSITE- FT ProRule:PRU00359}. FT DOMAIN 1258 1602 FERM 1. {ECO:0000255|PROSITE- FT ProRule:PRU00084}. FT DOMAIN 1603 1672 SH3. {ECO:0000255|PROSITE- FT ProRule:PRU00192}. FT DOMAIN 1747 1896 MyTH4 2. {ECO:0000255|PROSITE- FT ProRule:PRU00359}. FT DOMAIN 1902 2205 FERM 2. {ECO:0000255|PROSITE- FT ProRule:PRU00084}. FT NP_BIND 158 165 ATP. {ECO:0000305}. FT REGION 632 639 Actin-binding. {ECO:0000305}. FT REGION 858 935 SAH. {ECO:0000250|UniProtKB:Q13402}. FT MOD_RES 1563 1563 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 1569 1569 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 1571 1571 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT VAR_SEQ 1523 1560 Missing (in isoform 2). FT {ECO:0000303|PubMed:15654330}. FT /FTId=VSP_042238. FT VARIANT 241 241 R -> P (in sh-1). FT VARIANT 502 502 R -> P (in sh-1). FT MUTAGEN 1189 1189 A->E: Strongly reduced affinity for FT USH1G. {ECO:0000269|PubMed:21311020}. FT MUTAGEN 1473 1473 F->Q: Reduced affinity for USH1G. FT {ECO:0000269|PubMed:21311020}. FT CONFLICT 85 85 L -> R (in Ref. 1; AAB40708). FT {ECO:0000305}. FT CONFLICT 238 238 E -> S (in Ref. 1; AAB40708). FT {ECO:0000305}. FT CONFLICT 589 589 I -> V (in Ref. 1; AAB40708). FT {ECO:0000305}. FT CONFLICT 682 682 V -> G (in Ref. 1; AAB40708). FT {ECO:0000305}. FT CONFLICT 1156 1156 F -> L (in Ref. 1; AAB40708). FT {ECO:0000305}. FT HELIX 1001 1008 {ECO:0000244|PDB:3PVL}. FT HELIX 1032 1048 {ECO:0000244|PDB:3PVL}. FT HELIX 1070 1075 {ECO:0000244|PDB:3PVL}. FT TURN 1076 1079 {ECO:0000244|PDB:3PVL}. FT HELIX 1084 1088 {ECO:0000244|PDB:3PVL}. FT HELIX 1150 1163 {ECO:0000244|PDB:3PVL}. FT HELIX 1165 1167 {ECO:0000244|PDB:3PVL}. FT HELIX 1168 1178 {ECO:0000244|PDB:3PVL}. FT HELIX 1185 1201 {ECO:0000244|PDB:3PVL}. FT TURN 1206 1208 {ECO:0000244|PDB:3PVL}. FT HELIX 1209 1217 {ECO:0000244|PDB:3PVL}. FT TURN 1221 1223 {ECO:0000244|PDB:3PVL}. FT HELIX 1224 1237 {ECO:0000244|PDB:3PVL}. FT HELIX 1246 1254 {ECO:0000244|PDB:3PVL}. FT STRAND 1258 1264 {ECO:0000244|PDB:3PVL}. FT STRAND 1269 1274 {ECO:0000244|PDB:3PVL}. FT HELIX 1280 1290 {ECO:0000244|PDB:3PVL}. FT STRAND 1299 1305 {ECO:0000244|PDB:3PVL}. FT STRAND 1308 1313 {ECO:0000244|PDB:3PVL}. FT HELIX 1319 1331 {ECO:0000244|PDB:3PVL}. FT TURN 1332 1334 {ECO:0000244|PDB:3PVL}. FT HELIX 1337 1339 {ECO:0000244|PDB:3PVL}. FT STRAND 1343 1348 {ECO:0000244|PDB:3PVL}. FT HELIX 1357 1359 {ECO:0000244|PDB:3PVL}. FT HELIX 1361 1376 {ECO:0000244|PDB:3PVL}. FT HELIX 1385 1400 {ECO:0000244|PDB:3PVL}. FT HELIX 1406 1416 {ECO:0000244|PDB:3PVL}. FT HELIX 1419 1421 {ECO:0000244|PDB:3PVL}. FT STRAND 1424 1426 {ECO:0000244|PDB:3PVL}. FT HELIX 1428 1444 {ECO:0000244|PDB:3PVL}. FT HELIX 1451 1465 {ECO:0000244|PDB:3PVL}. FT TURN 1467 1469 {ECO:0000244|PDB:3PVL}. FT STRAND 1472 1482 {ECO:0000244|PDB:3PVL}. FT STRAND 1487 1494 {ECO:0000244|PDB:3PVL}. FT STRAND 1497 1501 {ECO:0000244|PDB:3PVL}. FT STRAND 1507 1512 {ECO:0000244|PDB:3PVL}. FT HELIX 1513 1515 {ECO:0000244|PDB:3PVL}. FT STRAND 1516 1522 {ECO:0000244|PDB:3PVL}. FT STRAND 1564 1566 {ECO:0000244|PDB:3PVL}. FT STRAND 1569 1574 {ECO:0000244|PDB:3PVL}. FT STRAND 1579 1583 {ECO:0000244|PDB:3PVL}. FT HELIX 1587 1604 {ECO:0000244|PDB:3PVL}. FT STRAND 1607 1612 {ECO:0000244|PDB:3PVL}. FT STRAND 1632 1634 {ECO:0000244|PDB:3PVL}. FT HELIX 1640 1645 {ECO:0000244|PDB:3PVL}. FT STRAND 1646 1653 {ECO:0000244|PDB:3PVL}. FT TURN 1654 1656 {ECO:0000244|PDB:3PVL}. FT STRAND 1659 1663 {ECO:0000244|PDB:3PVL}. FT HELIX 1664 1666 {ECO:0000244|PDB:3PVL}. FT STRAND 1667 1669 {ECO:0000244|PDB:3PVL}. FT HELIX 1678 1684 {ECO:0000244|PDB:3PVL}. SQ SEQUENCE 2215 AA; 254939 MW; D942FC7674B75EC7 CRC64; MVILQKGDYV WMDLKSGQEF DVPIGAVVKL CDSGQIQVVD DEDNEHWISP QNATHIKPMH PTSVHGVEDM IRLGDLNEAG ILRNLLIRYR DHLIYTYTGS ILVAVNPYQL LSIYSPEHIR QYTNKKIGEM PPHIFAIADN CYFNMKRNNR DQCCIISGES GAGKTESTKL ILQFLAAISG QHSWIEQQVL EATPILEAFG NAKTIRNDNS SRFGKYIDIH FNKRGAIEGA KIEQYLLEKS RVCRQAPDER NYHVFYCMLE GMNEEEKKKL GLGQAADYNY LAMGNCITCE GRVDSQEYAN IRSAMKVLMF TDTENWEISK LLAAILHMGN LQYEARTFEN LDACEVLFSP SLATAASLLE VNPPDLMSCL TSRTLITRGE TVSTPLSREQ ALDVRDAFVK GIYGRLFVWI VEKINAAIYK PPPLEVKNSR RSIGLLDIFG FENFTVNSFE QLCINFANEH LQQFFVRHVF KLEQEEYDLE SIDWLHIEFT DNQEALDMIA NRPMNVISLI DEESKFPKGT DATMLHKLNS QHKLNANYVP PKNSHETQFG INHFAGVVYY ESQGFLEKNR DTLHGDIIQL VHSSRNKFIK QIFQADVAMG AETRKRSPTL SSQFKRSLEL LMRTLGACQP FFVRCIKPNE FKKPMLFDRH LCVRQLRYSG MMETIRIRHA GYPIRYSFVE FVERYRVLLP GVKPAYKQGD LRGTCQRMAE AVLGTHDDWQ IGKTKIFLKD HHDMLLEVER DKAITDRVIL LQKVIRGFKD RSNFLRLKSA ATLIQRHWRG HHCRKNYELI RLGFLRLQAL HRSRKLHKQY RLARQRIIEF QARCRAYLVR KAFRHRLWAV ITVQAYARGM IARRLHRRLR VEYQRRLEAE RMRLAEEEKL RKEMSAKKAK EEAERKHQER LAQLAREDAE RELKEKEEAR RKKELLEQME KARHEPINHS DMVDKMFGFL GTSGSLPGQE GQAPSGFEDL ERGRREMVEE DVDAALPLPD EDEEDLSEYK FAKFAATYFQ GTTTHSYTRR PLKQPLLYHD DEGDQLAALA VWITILRFMG DLPEPKYHTA MSDGSEKIPV MTKIYETLGK KTYKRELQAL QGEGETQLPE GQKKTSVRHK LVHLTLKKKS KLTEEVTKRL NDGESTVQGN SMLEDRPTSN LEKLHFIIGN GILRPALRDE IYCQISKQLT HNPSKSSYAR GWILVSLCVG CFAPSEKFVK YLRNFIHGGP PGYAPYCEER LRRTFVNGTR TQPPSWLELQ ATKSKKPIML PVTFMDGTTK TLLTDSATTA RELCNALADK ISLKDRFGFS LYIALFDKVS SLGSGSDHVM DAISQCEQYA KEQGAQERNA PWRLFFRKEV FTPWHNPSED NVATNLIYQQ VVRGVKFGEY RCEKEDDLAE LASQQYFVDY GSEMILERLL SLVPTYIPDR EITPLKNLEK WAQLAIAAHK KGIYAQRRTD SQKVKEDVVN YARFKWPLLF SRFYEAYKFS GPPLPKSDVI VAVNWTGVYF VDEQEQVLLE LSFPEIMAVS SSRECRVLLS LGCSDLGCAT CQSGRAGLTP AGPCSPCWSC RGTKMMAPSF TLATIKGDEY TFTSSNAEDI RDLVVTFLEG LRKRSKYVVA LQDNPNPAGE ESGFLSFAKG DLIILDHDTG EQVMNSGWAN GINERTKQRG DFPTDCVYVM PTVTLPPREI VALVTMTPDQ RQDVVRLLQL RTAEPEVRAK PYTLEEFSYD YFRPPPKHTL SRVMVSKARG KDRLWSHTRE PLKQALLKKI LGSEELSQEA CMAFVAVLKY MGDYPSKRMR SVNELTDQIF EWALKAEPLK DEAYVQILKQ LTDNHIRYSE ERGWELLWLC TGLFPPSNIL LPHVQRFLQS RKHCPLAIDC LQRLQKALRN GSRKYPPHLV EVEAIQHKTT QIFHKVYFPD DTDEAFEVES STKAKDFCQN IASRLLLKSS EGFSLFVKIA DKVISVPEND FFFDFVRHLT DWIKKARPIK DGIVPSLTYQ VFFMKKLWTT TVPGKDPMAD SIFHYYQELP KYLRGYHKCT REEVLQLGAL IYRVKFEEDK SYFPSIPKLL RELVPQDLIR QVSPDDWKRS IVAYFNKHAG KSKEEAKLAF LKLIFKWPTF GSAFFEVKQT TEPNFPEILL IAINKYGVSL IDPRTKDILT THPFTKISNW SSGNTYFHIT IGNLVRGSKL LCETSLGYKM DDLLTSYISQ MLTAMSKQRN SRSGR //