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   27-MAR-2024, entry version 99.
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). Involved in
CC       clathrin-mediated endocytosis and intracellular movement of clathrin-
CC       coated ve (By similarity)sicles. Required for normal morphology of the
CC       glomerular basement membrane, normal development of foot processes by
CC       kidney podocytes and normal kidney function. In dendritic cells, may
CC       control the movement of class II-containing cytoplasmic vesicles along
CC       the actin cytoskeleton by connecting them with the actin network via
CC       ARL14EP and ARL14 (By similarity). {ECO:0000250,
CC       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; 7.
DR   IntAct; E9Q634; 3.
DR   MINT; E9Q634; -.
DR   STRING; 10090.ENSMUSP00000034745; -.
DR   GlyGen; E9Q634; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; E9Q634; -.
DR   PhosphoSitePlus; E9Q634; -.
DR   EPD; E9Q634; -.
DR   jPOST; E9Q634; -.
DR   MaxQB; E9Q634; -.
DR   PaxDb; 10090-ENSMUSP00000034745; -.
DR   PeptideAtlas; E9Q634; -.
DR   ProteomicsDB; 287583; -.
DR   Pumba; E9Q634; -.
DR   Antibodypedia; 12911; 174 antibodies from 26 providers.
DR   DNASU; 71602; -.
DR   Ensembl; ENSMUST00000034745.9; ENSMUSP00000034745.8; ENSMUSG00000032220.11.
DR   GeneID; 71602; -.
DR   KEGG; mmu:71602; -.
DR   UCSC; uc009qnx.1; mouse.
DR   AGR; MGI:106621; -.
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; MAFHWQS; -.
DR   OrthoDB; 1094820at2759; -.
DR   PhylomeDB; E9Q634; -.
DR   TreeFam; TF312960; -.
DR   BioGRID-ORCS; 71602; 1 hit in 77 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 183 other cell types or tissues.
DR   ExpressionAtlas; E9Q634; baseline and differential.
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; IEA:Ensembl.
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:0031982; C:vesicle; IBA:GO_Central.
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; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF341; UNCONVENTIONAL MYOSIN-IE; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS51757; TH1; 1.
DR   Genevisible; E9Q634; MM.
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
//