MYO1E_MOUSE
ID MYO1E_MOUSE Reviewed; 1107 AA.
AC E9Q634; Q80X36; Q91ZI4;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Unconventional myosin-Ie;
DE AltName: Full=Unconventional myosin 1E;
GN Name=Myo1e; Synonyms=Myr3;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 600-726, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12486594; DOI=10.1007/s101620020049;
RA Dumont R.A., Zhao Y.-D., Holt J.R., Baehler M., Gillespie P.G.;
RT "Myosin-I isozymes in neonatal rodent auditory and vestibular epithelia.";
RL J. Assoc. Res. Otolaryngol. 3:375-389(2002).
RN [4]
RP IDENTIFICATION BY 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 [5]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19005011; DOI=10.1681/asn.2007111172;
RA Krendel M., Kim S.V., Willinger T., Wang T., Kashgarian M., Flavell R.A.,
RA Mooseker M.S.;
RT "Disruption of Myosin 1e promotes podocyte injury.";
RL J. Am. Soc. Nephrol. 20:86-94(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC 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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1053-1107.
RA Allsop G., Harris S.A., Peckham M., Edwards T.;
RT "Myosin 1E SH3 domain.";
RL Submitted (AUG-2011) to the PDB data bank.
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails bind to membranous compartments, which are then moved
CC relative to actin filaments. Binds to membranes containing anionic
CC phospholipids via its tail domain (By similarity). Required for normal
CC morphology of the glomerular basement membrane, normal development of
CC foot processes by kidney podocytes and normal kidney function. In
CC dendritic cells, may control the movement of class II-containing
CC cytoplasmic vesicles along the actin cytoskeleton by connecting them
CC with the actin network via ARL14EP and ARL14 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:19005011}.
CC -!- SUBUNIT: Interacts with CALM and F-actin. Interacts (via SH3 domain)
CC with SYNJ1, DNM1 and DNM2. Interacts with ARL14EP. Interacts with
CC CARMIL1. {ECO:0000250|UniProtKB:Q12965}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19005011}. Cell
CC junction {ECO:0000269|PubMed:19005011}. Cytoplasmic vesicle
CC {ECO:0000305|PubMed:19005011}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:19005011}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19005011}. Note=In podocytes, it localizes close to
CC and is associated with the cytoplasmic membrane, with enrichment at the
CC lamellipodia tips. Colocalizes with F-actin (By similarity). Detected
CC in cytoplasmic punctae. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in kidney glomeruli (at protein level).
CC Detected in utricle. {ECO:0000269|PubMed:12486594,
CC ECO:0000269|PubMed:19005011}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype at birth. Mice exhibit
CC massive proteinuria, combined with the presence of leukocytes and
CC hemoglobin in the urine. They develop enlarged kidneys, present damage
CC to the glomeruli, renal inflammation and fibrosis. In the glomeruli,
CC the thickness of the basement membrane is increased, and podocytes fail
CC to develop normal foot processes. {ECO:0000269|PubMed:19005011}.
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-1 (MYH1). {ECO:0000305}.
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DR EMBL; AC157086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051391; AAH51391.1; -; mRNA.
DR EMBL; AF426465; AAL26545.1; -; mRNA.
DR CCDS; CCDS40680.1; -.
DR RefSeq; NP_851417.2; NM_181072.3.
DR PDB; 2XMF; X-ray; 1.50 A; A=1053-1107.
DR PDBsum; 2XMF; -.
DR AlphaFoldDB; E9Q634; -.
DR SMR; E9Q634; -.
DR BioGRID; 214807; 6.
DR IntAct; E9Q634; 3.
DR MINT; E9Q634; -.
DR STRING; 10090.ENSMUSP00000034745; -.
DR iPTMnet; E9Q634; -.
DR PhosphoSitePlus; E9Q634; -.
DR EPD; E9Q634; -.
DR jPOST; E9Q634; -.
DR MaxQB; E9Q634; -.
DR PaxDb; E9Q634; -.
DR PeptideAtlas; E9Q634; -.
DR PRIDE; E9Q634; -.
DR ProteomicsDB; 287583; -.
DR Antibodypedia; 12911; 165 antibodies from 26 providers.
DR DNASU; 71602; -.
DR Ensembl; ENSMUST00000034745; ENSMUSP00000034745; ENSMUSG00000032220.
DR GeneID; 71602; -.
DR KEGG; mmu:71602; -.
DR UCSC; uc009qnx.1; mouse.
DR CTD; 4643; -.
DR MGI; MGI:106621; Myo1e.
DR VEuPathDB; HostDB:ENSMUSG00000032220; -.
DR eggNOG; KOG0162; Eukaryota.
DR GeneTree; ENSGT00940000157461; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; E9Q634; -.
DR OMA; MESKWGT; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; E9Q634; -.
DR TreeFam; TF312960; -.
DR BioGRID-ORCS; 71602; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Myo1e; mouse.
DR PRO; PR:E9Q634; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; E9Q634; protein.
DR Bgee; ENSMUSG00000032220; Expressed in lumbar dorsal root ganglion and 181 other tissues.
DR ExpressionAtlas; E9Q634; baseline and differential.
DR Genevisible; E9Q634; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISO:MGI.
DR GO; GO:0032437; C:cuticular plate; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; 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:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0032836; P:glomerular basement membrane development; IMP:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; IMP:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0072015; P:podocyte development; IMP:UniProtKB.
DR GO; GO:0035166; P:post-embryonic hemopoiesis; IMP:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11827; SH3_MyoIe_If_like; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR035507; Ie/If_SH3.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ATP-binding; Calmodulin-binding;
KW Cell junction; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Lipid-binding;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..1107
FT /note="Unconventional myosin-Ie"
FT /id="PRO_0000415664"
FT DOMAIN 19..692
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 695..724
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 730..922
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1050..1107
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 581..591
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 919..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1051
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12965"
FT CONFLICT 73
FT /note="V -> I (in Ref. 2; AAH51391)"
FT /evidence="ECO:0000305"
FT STRAND 1054..1059
FT /evidence="ECO:0007829|PDB:2XMF"
FT STRAND 1076..1082
FT /evidence="ECO:0007829|PDB:2XMF"
FT STRAND 1086..1092
FT /evidence="ECO:0007829|PDB:2XMF"
FT STRAND 1095..1100
FT /evidence="ECO:0007829|PDB:2XMF"
FT HELIX 1101..1103
FT /evidence="ECO:0007829|PDB:2XMF"
FT STRAND 1104..1106
FT /evidence="ECO:0007829|PDB:2XMF"
SQ SEQUENCE 1107 AA; 126818 MW; D745BE859E2F079D CRC64;
MGSKGAYRYH WQSHNVKHSG VDDMVLLSKI TESSIVENLK KRYMDDYIFT YIGSVLISVN
PFKQMPYFGE KEVEMYQGAA QYENPPHIYA LADSMYRNMI IDRENQCVII SGESGAGKTV
AAKYIMSYVS RVSGGGPKVQ HVKDIILQSN PLLEAFGNAK TVRNNNSSRF GKYFEIQFSP
GGEPDGGKIS NFLLEKSRVV MRNPGERSFH IFYQLIEGAS PEQKQSLGIT SMDYYYYLSL
SGSYKVDDID DKRDFQETLH AMNVIGIFSE EQTLVLQIVA GILHLGNISF KEVGNYAAVE
SEEFLAFPAY LLGINQDRLK EKLTSRQMDS KWGGKSESIH VTLNVEQACY TRDALAKALH
ARVFDFLVDS INKAMEKDHE EYNIGVLDIY GFEIFQKNGF EQFCINFVNE KLQQIFIELT
LKAEQEEYVQ EGIRWTPIEY FNNKIVCDLI ESKVNPPGIM SILDDVCATM HAVGEGADQT
LLQKLQMQIG SHEHFNSWNQ GFIIHHYAGK VSYDMDGFCE RNRDVLFMDL IELMQSSELP
FIKSLFPENL QADKKGRPTT AGSKIKKQAN DLVSTLMKCT PHYIRCIKPN ETKKPKDWEE
SRVKHQVEYL GLKENIRVRR AGYAYRRVFQ KFLQRYAILT KATWPVWRGD EKQGVLHLLQ
SVNMDSDQFQ LGRSKVFIKA PESLFLLEEM RERKYDGYAR VIQKTWRKFV ARKKYVQMRE
EASDLLLNKK ERRRNSINRN FIGDYIGMEE RPELQQFVGK REKIDFADTV TKYDRRFKGV
KRDLLLTPKC LYLIGREKVK QGPDKGVVKE VLKRRIEVER ILSVSLSTMQ DDIFILHEQE
YDSLLESVFK TEFLSLLAKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFH
QGFGDLAILK PSNKVLQVSI GPGLPKNSRP TRRNTVTSRG YPGGTKNNYP MRAAPAPPGC
HQNGVIRNQF VPPPHAFGNQ RSNQKSLYTS MARPPLPRQQ STGSDRLSQT PESLDFLKVP
DQGVAGVRRQ TSSRPPPAGG RPKPQPKPKP QVPQCKALYA YDAQDTDELS FNANDIIDII
KEDPSGWWTG RLRGKQGLFP NNYVTKI
