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   16-SEP-2015, entry version 44.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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.,
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   [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
RT   project: 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/6;
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
RT   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.,
RA   Flavell R.A., 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
RT   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
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. Binds to
CC       membranes containing anionic phospholipids via its tail domain (By
CC       similarity). Required for normal morphology of the glomerular
CC       basement membrane, normal development of foot processes by kidney
CC       podocytes and normal kidney function. In dendritic cells, may
CC       control the movement of class II-containing cytoplasmic vesicles
CC       along the actin cytoskeleton by connecting them with the actin
CC       network via ARL14EP and ARL14 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CALM and F-actin. Interacts (via SH3
CC       domain) with SYNJ1, DNM1 and DNM2 (By similarity). Interacts with
CC       ARL14EP (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19005011}.
CC       Cell junction {ECO:0000269|PubMed:19005011}. Cytoplasmic vesicle
CC       {ECO:0000305|PubMed:19005011}. Cytoplasmic vesicle, clathrin-
CC       coated vesicle {ECO:0000269|PubMed:19005011}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:19005011}. Note=In podocytes, it
CC       localizes close to and is associated with the cytoplasmic
CC       membrane, with enrichment at the lamellipodia tips. Colocalizes
CC       with F-actin (By similarity). Detected in cytoplasmic punctae.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in kidney glomeruli (at protein
CC       level). 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
CC       damage to the glomeruli, renal inflammation and fibrosis. In the
CC       glomeruli, the thickness of the basement membrane is increased,
CC       and podocytes fail to develop normal foot processes.
CC       {ECO:0000269|PubMed:19005011}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 IQ domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00116}.
CC   -!- SIMILARITY: Contains 1 myosin motor domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 SH3 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00192}.
CC   -!- SIMILARITY: Contains 1 TH1 (class I myosin tail homology) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU01093}.
CC   -!- CAUTION: Represents an unconventional myosin. This protein should
CC       not be confused with the conventional myosin-1 (MYH1).
CC       {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   UniGene; Mm.249311; -.
DR   UniGene; Mm.444670; -.
DR   PDB; 2XMF; X-ray; 1.50 A; A=1053-1107.
DR   PDBsum; 2XMF; -.
DR   ProteinModelPortal; E9Q634; -.
DR   SMR; E9Q634; 20-692, 698-858, 1053-1107.
DR   BioGrid; 214807; 3.
DR   STRING; 10090.ENSMUSP00000034745; -.
DR   PhosphoSite; E9Q634; -.
DR   MaxQB; E9Q634; -.
DR   PRIDE; E9Q634; -.
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   GeneTree; ENSGT00760000118956; -.
DR   HOGENOM; HOG000260265; -.
DR   HOVERGEN; HBG100702; -.
DR   InParanoid; E9Q634; -.
DR   KO; K10356; -.
DR   OMA; ATWPSWQ; -.
DR   OrthoDB; EOG7V49XQ; -.
DR   TreeFam; TF312960; -.
DR   ChiTaRS; Myo1e; mouse.
DR   NextBio; 334081; -.
DR   PRO; PR:E9Q634; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; E9Q634; -.
DR   Genevisible; E9Q634; MM.
DR   GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR   GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR   GO; GO:0045334; C:clathrin-coated endocytic vesicle; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042623; F:ATPase activity, coupled; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
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:0072015; P:glomerular visceral epithelial cell development; 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:0035166; P:post-embryonic hemopoiesis; IMP:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR010926; Myosin_TH1.
DR   InterPro; IPR027417; P-loop_NTPase.
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; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW   Cytoskeleton; Lipid-binding; Motor protein; Myosin;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN         1   1107       Unconventional myosin-Ie.
FT                                /FTId=PRO_0000415664.
FT   DOMAIN       19    692       Myosin motor.
FT   DOMAIN      695    724       IQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00116}.
FT   DOMAIN      730    922       TH1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01093}.
FT   DOMAIN     1050   1107       SH3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00192}.
FT   NP_BIND     112    119       ATP. {ECO:0000255}.
FT   REGION      581    591       Actin-binding. {ECO:0000255}.
FT   MOD_RES    1001   1001       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12965}.
FT   CONFLICT     73     73       V -> I (in Ref. 2; AAH51391).
FT                                {ECO:0000305}.
FT   STRAND     1054   1059       {ECO:0000244|PDB:2XMF}.
FT   STRAND     1076   1082       {ECO:0000244|PDB:2XMF}.
FT   STRAND     1086   1092       {ECO:0000244|PDB:2XMF}.
FT   STRAND     1095   1100       {ECO:0000244|PDB:2XMF}.
FT   HELIX      1101   1103       {ECO:0000244|PDB:2XMF}.
FT   STRAND     1104   1106       {ECO:0000244|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
//