MYO5A_MOUSE
ID MYO5A_MOUSE Reviewed; 1853 AA.
AC Q99104; E9PUE5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Unconventional myosin-Va;
DE AltName: Full=Dilute myosin heavy chain, non-muscle;
GN Name=Myo5a; Synonyms=Dilute;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=1996138; DOI=10.1038/349709a0;
RA Mercer J.A., Seperack P.K., Strobel M.C., Copeland N.G., Jenkins N.A.;
RT "Novel myosin heavy chain encoded by murine dilute coat colour locus.";
RL Nature 349:709-712(1991).
RN [2]
RP ERRATUM OF PUBMED:1996138, AND SEQUENCE REVISION.
RA Mercer J.A., Seperack P.K., Strobel M.C., Copeland N.G., Jenkins N.A.;
RL Nature 352:547-547(1991).
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 INTERACTION WITH FMR1.
RX PubMed=12147688; DOI=10.1074/jbc.m203608200;
RA Ohashi S., Koike K., Omori A., Ichinose S., Ohara S., Kobayashi S.,
RA Sato T.A., Anzai K.;
RT "Identification of mRNA/protein (mRNP) complexes containing Puralpha,
RT mStaufen, fragile X protein, and myosin Va and their association with rough
RT endoplasmic reticulum equipped with a kinesin motor.";
RL J. Biol. Chem. 277:37804-37810(2002).
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), a
RT 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 MLPH.
RX PubMed=11887186; DOI=10.1038/ncb760;
RA Wu X.S., Rao K., Zhang H., Wang F., Sellers J.R., Matesic L.E.,
RA Copeland N.G., Jenkins N.A., Hammer J.A. III;
RT "Identification of an organelle receptor for myosin-Va.";
RL Nat. Cell Biol. 4:271-278(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-1450 AND SER-1650,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
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 [11]
RP FUNCTION IN VESICULAR TRANSPORT, AND INTERACTION WITH RAB10.
RX PubMed=22908308; DOI=10.1083/jcb.201111091;
RA Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S.,
RA Hammer J.A., Xu T., Lippincott-Schwartz J.;
RT "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle
RT translocation in adipocytes.";
RL J. Cell Biol. 198:545-560(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 763-820 IN COMPLEX WITH CALM, AND
RP SUBUNIT.
RX PubMed=17151196; DOI=10.1073/pnas.0609436103;
RA Houdusse A., Gaucher J.F., Krementsova E., Mui S., Trybus K.M., Cohen C.;
RT "Crystal structure of apo-calmodulin bound to the first two IQ motifs of
RT myosin V reveals essential recognition features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19326-19331(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1469-1853 OF APOPROTEIN AND IN
RP COMPLEX WITH RIPL2 AND MLPH, INTERACTION WITH SYTL4; RIPL2 AND MLPH, AND
RP MUTAGENESIS OF ARG-1528; ILE-1535 AND LYS-1539.
RX PubMed=23798443; DOI=10.1073/pnas.1306768110;
RA Wei Z., Liu X., Yu C., Zhang M.;
RT "Structural basis of cargo recognitions for class V myosins.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11314-11319(2013).
CC -!- FUNCTION: Processive actin-based motor that can move in large steps
CC approximating the 36-nm pseudo-repeat of the actin filament. Involved
CC in melanosome transport. Also mediates the transport of vesicles to the
CC plasma membrane. May also be required for some polarization process
CC involved in dendrite formation. {ECO:0000269|PubMed:22908308}.
CC -!- SUBUNIT: May be a homodimer, which associates with multiple calmodulin
CC or myosin light chains (PubMed:17151196). Interacts with RIPL2, the
CC interaction is required for its role in dendrite formation
CC (PubMed:23798443). Interacts with MLPH (PubMed:11887186). Interacts
CC with SYTL4 (PubMed:23798443). Interacts with MYRIP (PubMed:12221080).
CC Interacts with RAB10; mediates the transport to the plasma membrane of
CC SLC2A4/GLUT4 storage vesicles (PubMed:22908308). Interacts with FMR1;
CC this interaction occurs in association with polyribosome
CC (PubMed:12147688). {ECO:0000269|PubMed:11887186,
CC ECO:0000269|PubMed:12147688, ECO:0000269|PubMed:12221080,
CC ECO:0000269|PubMed:17151196, ECO:0000269|PubMed:22908308,
CC ECO:0000269|PubMed:23798443}.
CC -!- INTERACTION:
CC Q99104; Q99104: Myo5a; NbExp=2; IntAct=EBI-400199, EBI-400199;
CC -!- TISSUE SPECIFICITY: Detected in melanocytes.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; X57377; CAA40651.1; -; mRNA.
DR EMBL; AC133947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT033761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52860.1; -.
DR PIR; A46761; A46761.
DR RefSeq; NP_034994.2; NM_010864.2.
DR PDB; 2IX7; X-ray; 2.50 A; C=763-820.
DR PDB; 3WB8; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1469-1853.
DR PDB; 4KP3; X-ray; 2.40 A; A/B=1469-1853.
DR PDB; 4ZLK; X-ray; 2.50 A; A=1-791.
DR PDB; 6KU0; X-ray; 1.60 A; A/C=1469-1853.
DR PDBsum; 2IX7; -.
DR PDBsum; 3WB8; -.
DR PDBsum; 4KP3; -.
DR PDBsum; 4ZLK; -.
DR PDBsum; 6KU0; -.
DR AlphaFoldDB; Q99104; -.
DR SMR; Q99104; -.
DR BioGRID; 201666; 32.
DR CORUM; Q99104; -.
DR DIP; DIP-29542N; -.
DR IntAct; Q99104; 22.
DR MINT; Q99104; -.
DR STRING; 10090.ENSMUSP00000116028; -.
DR BindingDB; Q99104; -.
DR ChEMBL; CHEMBL4295928; -.
DR iPTMnet; Q99104; -.
DR PhosphoSitePlus; Q99104; -.
DR SwissPalm; Q99104; -.
DR EPD; Q99104; -.
DR jPOST; Q99104; -.
DR MaxQB; Q99104; -.
DR PaxDb; Q99104; -.
DR PeptideAtlas; Q99104; -.
DR PRIDE; Q99104; -.
DR ProteomicsDB; 293606; -.
DR Antibodypedia; 686; 172 antibodies from 32 providers.
DR DNASU; 17918; -.
DR Ensembl; ENSMUST00000123128; ENSMUSP00000116028; ENSMUSG00000034593.
DR GeneID; 17918; -.
DR KEGG; mmu:17918; -.
DR UCSC; uc009qrr.1; mouse.
DR CTD; 4644; -.
DR MGI; MGI:105976; Myo5a.
DR VEuPathDB; HostDB:ENSMUSG00000034593; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000155347; -.
DR HOGENOM; CLU_000192_9_4_1; -.
DR InParanoid; Q99104; -.
DR OrthoDB; 311886at2759; -.
DR TreeFam; TF328771; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR BioGRID-ORCS; 17918; 4 hits in 28 CRISPR screens.
DR ChiTaRS; Myo5a; mouse.
DR EvolutionaryTrace; Q99104; -.
DR PRO; PR:Q99104; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q99104; protein.
DR Bgee; ENSMUSG00000034593; Expressed in medial geniculate body and 244 other tissues.
DR ExpressionAtlas; Q99104; baseline and differential.
DR Genevisible; Q99104; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0042641; C:actomyosin; IDA:MGI.
DR GO; GO:0042642; C:actomyosin, myosin complex part; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0032433; C:filopodium tip; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0032593; C:insulin-responsive compartment; IDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0016459; C:myosin complex; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0016461; C:unconventional myosin complex; IMP:CAFA.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0043008; F:ATP-dependent protein binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR GO; GO:0003774; F:cytoskeletal motor activity; IDA:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000146; F:microfilament motor activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; IDA:MGI.
DR GO; GO:0099640; P:axo-dendritic protein transport; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
DR GO; GO:0042417; P:dopamine metabolic process; ISO:MGI.
DR GO; GO:0051643; P:endoplasmic reticulum localization; IMP:MGI.
DR GO; GO:0099089; P:establishment of endoplasmic reticulum localization to postsynapse; IDA:SynGO.
DR GO; GO:0006887; P:exocytosis; IMP:MGI.
DR GO; GO:0048820; P:hair follicle maturation; IMP:MGI.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; IMP:MGI.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:MGI.
DR GO; GO:0016236; P:macroautophagy; ISO:MGI.
DR GO; GO:0042438; P:melanin biosynthetic process; IMP:MGI.
DR GO; GO:0006582; P:melanin metabolic process; IMP:MGI.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:MGI.
DR GO; GO:0032400; P:melanosome localization; IMP:MGI.
DR GO; GO:0032402; P:melanosome transport; IDA:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; ISO:MGI.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0042476; P:odontogenesis; IDA:MGI.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:1904960; P:positive regulation of cytochrome-c oxidase activity; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0150103; P:reactive gliosis; ISO:MGI.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:MGI.
DR GO; GO:0031585; P:regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IMP:MGI.
DR GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:0032252; P:secretory granule localization; IMP:MGI.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR GO; GO:0030050; P:vesicle transport along actin filament; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd15478; Myo5a_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR037988; Myo5a_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 6.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
KW Coiled coil; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4I1"
FT CHAIN 2..1853
FT /note="Unconventional myosin-Va"
FT /id="PRO_0000123457"
FT DOMAIN 8..60
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 69..763
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 766..788
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 789..813
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 814..836
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 837..861
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 862..884
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 885..913
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1532..1808
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 598..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..665
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 1105..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 914..1237
FT /evidence="ECO:0000255"
FT COILED 1314..1443
FT /evidence="ECO:0000255"
FT COMPBIAS 598..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4I1"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1032
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYF3"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1758
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MUTAGEN 1528
FT /note="R->H: Slightly reduces affinity for MLPH."
FT /evidence="ECO:0000269|PubMed:23798443"
FT MUTAGEN 1535
FT /note="I->E: Strongly reduces affinity for MLPH and SYTL4."
FT /evidence="ECO:0000269|PubMed:23798443"
FT MUTAGEN 1539
FT /note="K->E: Strongly reduces affinity for MLPH and SYTL4."
FT /evidence="ECO:0000269|PubMed:23798443"
FT CONFLICT 695
FT /note="A -> R (in Ref. 1; CAA40651)"
FT /evidence="ECO:0000305"
FT CONFLICT 904..905
FT /note="EL -> DV (in Ref. 1; CAA40651)"
FT /evidence="ECO:0000305"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:4ZLK"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:4ZLK"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:4ZLK"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:4ZLK"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 319..335
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 368..376
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 393..421
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 449..479
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 493..500
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 505..513
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 520..531
FT /evidence="ECO:0007829|PDB:4ZLK"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 553..560
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 564..568
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 574..581
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 587..591
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 635..651
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 653..661
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 674..683
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 686..693
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 703..710
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 711..713
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 723..734
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 738..740
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 741..743
FT /evidence="ECO:0007829|PDB:4ZLK"
FT STRAND 745..750
FT /evidence="ECO:0007829|PDB:4ZLK"
FT HELIX 765..818
FT /evidence="ECO:0007829|PDB:2IX7"
FT STRAND 1473..1476
FT /evidence="ECO:0007829|PDB:4KP3"
FT HELIX 1479..1481
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1482..1489
FT /evidence="ECO:0007829|PDB:6KU0"
FT TURN 1490..1492
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1498..1502
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1506..1520
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1524..1545
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1549..1568
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1573..1575
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1581..1585
FT /evidence="ECO:0007829|PDB:6KU0"
FT STRAND 1589..1592
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1594..1627
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1659..1675
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1680..1704
FT /evidence="ECO:0007829|PDB:6KU0"
FT STRAND 1705..1708
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1711..1730
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1734..1736
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1739..1742
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1743..1751
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1759..1768
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1774..1783
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1796..1805
FT /evidence="ECO:0007829|PDB:6KU0"
FT TURN 1806..1808
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1836..1838
FT /evidence="ECO:0007829|PDB:6KU0"
FT HELIX 1843..1845
FT /evidence="ECO:0007829|PDB:6KU0"
FT STRAND 1850..1852
FT /evidence="ECO:0007829|PDB:6KU0"
SQ SEQUENCE 1853 AA; 215538 MW; D729DF9222EBCAA0 CRC64;
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY RLDPKTGELP
HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY TYCGIVLVAI NPYEQLPIYG
EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM ARDERNQSII VSGESGAGKT VSAKYAMRYF
ATVSGSASEA NVEEKVLASN PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR
TYLLEKSRVV FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADSFHYTKQ GGSPMIEGVD
DAKEMAHTRQ ACTLLGISES YQMGIFRILA GILHLGNVGF ASRDSDSCTI PPKHEPLTIF
CDLMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR DALAKHIYAK LFNWIVDHVN
QALHSAVKQH SFIGVLDIYG FETFEINSFE QFCINYANEK LQQQFNMHVF KLEQEEYMKE
QIPWTLIDFY DNQPCINLIE SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK
PRMSNKAFII KHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS
PTSATSSGRT PLTRVPVKPT KGRPGQTAKE HKKTVGHQFR NSLHLLMETL NATTPHYVRC
IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR WTYQEFFSRY RVLMKQKDVL
GDRKQTCKNV LEKLILDKDK YQFGKTKIFF RAGQVAYLEK LRADKLRAAC IRIQKTIRGW
LLRKRYLCMQ RAAITVQRYV RGYQARCYAK FLRRTKAATT IQKYWRMYVV RRRYKIRRAA
TIVIQSYLRG YLTRNRYRKI LREYKAVIIQ KRVRGWLART HYKRTMKAIV YLQCCFRRMM
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLMEKL TNLEGVYNSE
TEKLRNDVER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE QTRSEKKSIE ERADKYKQET
DQLVSNLKEE NTLLKQEKET LNHRIVEQAK EMTETMERKL VEETKQLELD LNDERLRYQN
LLNEFSRLEE RYDDLKEEMT LMLNVPKPGH KRTDSTHSSN ESEYTFSSEF AETEDIAPRT
EEPIEKKVPL DMSLFLKLQK RVTELEQEKQ LMQDELDRKE EQVFRSKAKE EERPQIRGAE
LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME QLTSVSEELD
VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ KMKDKGEIAQ AYIGLKETNR
LLESQLQSQK RSHENEAEAL RGEIQSLKEE NNRQQQLLAQ NLQLPPEARI EASLQHEITR
LTNENLYFEE LYADDPKKYQ SYRISLYKRM IDLMEQLEKQ DKTVRKLKKQ LKVFAKKIGE
LEVGQMENIS PGQIIDEPIR PVNIPRKEKD FQGMLEYKRE DEQKLVKNLI LELKPRGVAV
NLIPGLPAYI LFMCVRHADY LNDDQKVRSL LTSTINSIKK VLKKRGDDFE TVSFWLSNTC
RFLHCLKQYS GEEGFMKHNT SRQNEHCLTN FDLAEYRQVL SDLAIQIYQQ LVRVLENILQ
PMIVSGMLEH ETIQGVSGVK PTGLRKRTSS IADEGTYTLD SILRQLNSFH SVMCQHGMDP
ELIKQVVKQM FYIVGAITLN NLLLRKDMCS WSKGMQIRYN VSQLEEWLRD KNLMNSGAKE
TLEPLIQAAQ LLQVKKKTDD DAEAICSMCN ALTTAQIVKV LNLYTPVNEF EERVSVSFIR
TIQMRLRDRK DSPQLLMDAK HIFPVTFPFN PSSLALETIQ IPASLGLGFI ARV
