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E9Q634

- MYO1E_MOUSE

UniProt

E9Q634 - MYO1E_MOUSE

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Protein

Unconventional myosin-Ie

Gene

Myo1e

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain (By similarity). Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi112 – 1198ATPSequence Analysis

GO - Molecular functioni

  1. actin filament binding Source: UniProtKB
  2. ATPase activity, coupled Source: UniProtKB
  3. ATP binding Source: UniProtKB-KW
  4. calmodulin binding Source: UniProtKB
  5. motor activity Source: InterPro
  6. phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

  1. endocytosis Source: UniProtKB
  2. glomerular basement membrane development Source: UniProtKB
  3. glomerular filtration Source: UniProtKB
  4. glomerular visceral epithelial cell development Source: UniProtKB
  5. hemopoiesis Source: MGI
  6. in utero embryonic development Source: MGI
  7. kidney development Source: MGI
  8. nitrogen compound metabolic process Source: MGI
  9. platelet-derived growth factor receptor signaling pathway Source: MGI
  10. post-embryonic hemopoiesis Source: MGI
  11. vasculogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Lipid-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-Ie
Alternative name(s):
Unconventional myosin 1E
Gene namesi
Name:Myo1e
Synonyms:Myr3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:106621. Myo1e.

Subcellular locationi

Cytoplasm 1 Publication. Cell junction 1 Publication. Cytoplasmic vesicle 1 Publication. Cytoplasmic vesicleclathrin-coated vesicle 1 Publication. Cytoplasmcytoskeleton 1 Publication
Note: In podocytes, it localizes close to and is associated with the cytoplasmic membrane, with enrichment at the lamellipodia tips. Colocalizes with F-actin (By similarity). Detected in cytoplasmic punctae.By similarity

GO - Cellular componenti

  1. adherens junction Source: UniProtKB
  2. cell-cell junction Source: UniProtKB
  3. clathrin-coated endocytic vesicle Source: Ensembl
  4. cytoplasm Source: UniProtKB
  5. cytoskeleton Source: UniProtKB
  6. extracellular vesicular exosome Source: Ensembl
  7. myosin complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

No visible phenotype at birth. Mice exhibit massive proteinuria, combined with the presence of leukocytes and hemoglobin in the urine. They develop enlarged kidneys, present damage to the glomeruli, renal inflammation and fibrosis. In the glomeruli, the thickness of the basement membrane is increased, and podocytes fail to develop normal foot processes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11071107Unconventional myosin-IePRO_0000415664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1001 – 10011PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiE9Q634.
PRIDEiE9Q634.

PTM databases

PhosphoSiteiE9Q634.

Expressioni

Tissue specificityi

Detected in kidney glomeruli (at protein level). Detected in utricle.2 Publications

Gene expression databases

BgeeiE9Q634.
ExpressionAtlasiE9Q634. baseline and differential.

Interactioni

Subunit structurei

Interacts with CALM and F-actin. Interacts (via SH3 domain) with SYNJ1, DNM1 and DNM2 (By similarity). Interacts with ARL14EP (By similarity).By similarity

Structurei

Secondary structure

1
1107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1054 – 10596Combined sources
Beta strandi1076 – 10827Combined sources
Beta strandi1086 – 10927Combined sources
Beta strandi1095 – 11006Combined sources
Helixi1101 – 11033Combined sources
Beta strandi1104 – 11063Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XMFX-ray1.50A1053-1107[»]
ProteinModelPortaliE9Q634.
SMRiE9Q634. Positions 20-692, 1053-1107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 692674Myosin motorAdd
BLAST
Domaini695 – 72430IQPROSITE-ProRule annotationAdd
BLAST
Domaini718 – 923206Myosin tailSequence AnalysisAdd
BLAST
Domaini1050 – 110758SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni581 – 59111Actin-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 IQ domain.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated
Contains 1 myosin tail domain.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

GeneTreeiENSGT00760000118956.
HOGENOMiHOG000260265.
HOVERGENiHBG100702.
InParanoidiE9Q634.
KOiK10356.
OMAiKLKKENW.
OrthoDBiEOG7V49XQ.
TreeFamiTF312960.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
PR00452. SH3DOMAIN.
SMARTiSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E9Q634-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSKGAYRYH WQSHNVKHSG VDDMVLLSKI TESSIVENLK KRYMDDYIFT
60 70 80 90 100
YIGSVLISVN PFKQMPYFGE KEVEMYQGAA QYENPPHIYA LADSMYRNMI
110 120 130 140 150
IDRENQCVII SGESGAGKTV AAKYIMSYVS RVSGGGPKVQ HVKDIILQSN
160 170 180 190 200
PLLEAFGNAK TVRNNNSSRF GKYFEIQFSP GGEPDGGKIS NFLLEKSRVV
210 220 230 240 250
MRNPGERSFH IFYQLIEGAS PEQKQSLGIT SMDYYYYLSL SGSYKVDDID
260 270 280 290 300
DKRDFQETLH AMNVIGIFSE EQTLVLQIVA GILHLGNISF KEVGNYAAVE
310 320 330 340 350
SEEFLAFPAY LLGINQDRLK EKLTSRQMDS KWGGKSESIH VTLNVEQACY
360 370 380 390 400
TRDALAKALH ARVFDFLVDS INKAMEKDHE EYNIGVLDIY GFEIFQKNGF
410 420 430 440 450
EQFCINFVNE KLQQIFIELT LKAEQEEYVQ EGIRWTPIEY FNNKIVCDLI
460 470 480 490 500
ESKVNPPGIM SILDDVCATM HAVGEGADQT LLQKLQMQIG SHEHFNSWNQ
510 520 530 540 550
GFIIHHYAGK VSYDMDGFCE RNRDVLFMDL IELMQSSELP FIKSLFPENL
560 570 580 590 600
QADKKGRPTT AGSKIKKQAN DLVSTLMKCT PHYIRCIKPN ETKKPKDWEE
610 620 630 640 650
SRVKHQVEYL GLKENIRVRR AGYAYRRVFQ KFLQRYAILT KATWPVWRGD
660 670 680 690 700
EKQGVLHLLQ SVNMDSDQFQ LGRSKVFIKA PESLFLLEEM RERKYDGYAR
710 720 730 740 750
VIQKTWRKFV ARKKYVQMRE EASDLLLNKK ERRRNSINRN FIGDYIGMEE
760 770 780 790 800
RPELQQFVGK REKIDFADTV TKYDRRFKGV KRDLLLTPKC LYLIGREKVK
810 820 830 840 850
QGPDKGVVKE VLKRRIEVER ILSVSLSTMQ DDIFILHEQE YDSLLESVFK
860 870 880 890 900
TEFLSLLAKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFH
910 920 930 940 950
QGFGDLAILK PSNKVLQVSI GPGLPKNSRP TRRNTVTSRG YPGGTKNNYP
960 970 980 990 1000
MRAAPAPPGC HQNGVIRNQF VPPPHAFGNQ RSNQKSLYTS MARPPLPRQQ
1010 1020 1030 1040 1050
STGSDRLSQT PESLDFLKVP DQGVAGVRRQ TSSRPPPAGG RPKPQPKPKP
1060 1070 1080 1090 1100
QVPQCKALYA YDAQDTDELS FNANDIIDII KEDPSGWWTG RLRGKQGLFP

NNYVTKI
Length:1,107
Mass (Da):126,818
Last modified:April 5, 2011 - v1
Checksum:iD745BE859E2F079D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731V → I in AAH51391. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC157086 Genomic DNA. No translation available.
AC157950 Genomic DNA. No translation available.
AC157996 Genomic DNA. No translation available.
BC051391 mRNA. Translation: AAH51391.1.
AF426465 mRNA. Translation: AAL26545.1.
CCDSiCCDS40680.1.
RefSeqiNP_851417.2. NM_181072.3.
UniGeneiMm.249311.

Genome annotation databases

EnsembliENSMUST00000034745; ENSMUSP00000034745; ENSMUSG00000032220.
GeneIDi71602.
KEGGimmu:71602.
UCSCiuc009qnx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC157086 Genomic DNA. No translation available.
AC157950 Genomic DNA. No translation available.
AC157996 Genomic DNA. No translation available.
BC051391 mRNA. Translation: AAH51391.1 .
AF426465 mRNA. Translation: AAL26545.1 .
CCDSi CCDS40680.1.
RefSeqi NP_851417.2. NM_181072.3.
UniGenei Mm.249311.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XMF X-ray 1.50 A 1053-1107 [» ]
ProteinModelPortali E9Q634.
SMRi E9Q634. Positions 20-692, 1053-1107.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei E9Q634.

Proteomic databases

MaxQBi E9Q634.
PRIDEi E9Q634.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034745 ; ENSMUSP00000034745 ; ENSMUSG00000032220 .
GeneIDi 71602.
KEGGi mmu:71602.
UCSCi uc009qnx.1. mouse.

Organism-specific databases

CTDi 4643.
MGIi MGI:106621. Myo1e.

Phylogenomic databases

GeneTreei ENSGT00760000118956.
HOGENOMi HOG000260265.
HOVERGENi HBG100702.
InParanoidi E9Q634.
KOi K10356.
OMAi KLKKENW.
OrthoDBi EOG7V49XQ.
TreeFami TF312960.

Miscellaneous databases

ChiTaRSi Myo1e. mouse.
NextBioi 334081.
PROi E9Q634.
SOURCEi Search...

Gene expression databases

Bgeei E9Q634.
ExpressionAtlasi E9Q634. baseline and differential.

Family and domain databases

InterProi IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00193. MYOSINHEAVY.
PR00452. SH3DOMAIN.
SMARTi SM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  3. "Myosin-I isozymes in neonatal rodent auditory and vestibular epithelia."
    Dumont R.A., Zhao Y.-D., Holt J.R., Baehler M., Gillespie P.G.
    J. Assoc. Res. Otolaryngol. 3:375-389(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 600-726, TISSUE SPECIFICITY.
    Strain: C57BL/6.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Myosin 1E SH3 domain."
    Allsop G., Harris S.A., Peckham M., Edwards T.
    Submitted (AUG-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1053-1107.

Entry informationi

Entry nameiMYO1E_MOUSE
AccessioniPrimary (citable) accession number: E9Q634
Secondary accession number(s): Q80X36, Q91ZI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 5, 2011
Last modified: November 26, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-1 (MYH1).Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3