Unconventional myosin-Ie - Mus musculus (Mouse)

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E9Q634 (MYO1E_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 22. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Unconventional myosin-Ie

Alternative name(s):
Unconventional myosin 1E

Gene names

Name:	Myo1e
Synonyms:	Myr3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1107 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4
Subunit structure	Interacts with CALM and F-actin. Interacts (via SH3 domain) with SYNJ1, DNM1 and DNM2 By similarity. Interacts with ARL14EP By similarity.
Subcellular location	Cytoplasm. Cell junction. Cytoplasmic vesicle Probable. Cytoplasmic vesicle › clathrin-coated vesicle. Cytoplasm › cytoskeleton. 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. Ref.4
Tissue specificity	Detected in kidney glomeruli (at protein level). Detected in utricle. Ref.3 Ref.4
Disruption phenotype	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. Ref.4
Sequence similarities	Contains 1 IQ domain. Contains 1 myosin head-like domain. Contains 1 SH3 domain.
Caution	Represents a unconventional myosin. This protein should not be confused with the conventional myosin-1 (MYH1).

Ontologies

Keywords
Cellular component	Cell junction Cytoplasm Cytoplasmic vesicle Cytoskeleton
Domain	SH3 domain
Ligand	ATP-binding Actin-binding Calmodulin-binding Lipid-binding Nucleotide-binding
Molecular function	Motor protein Myosin
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from sequence or structural similarity. Source: UniProtKB glomerular basement membrane development Inferred from mutant phenotype Ref.4. Source: UniProtKB glomerular filtration Inferred from mutant phenotype Ref.4. Source: UniProtKB glomerular visceral epithelial cell development Inferred from mutant phenotype Ref.4. Source: UniProtKB in utero embryonic development Inferred from mutant phenotype PubMed 17143286. Source: MGI platelet-derived growth factor receptor signaling pathway Inferred from mutant phenotype PubMed 17143286. Source: MGI post-embryonic hemopoiesis Inferred from mutant phenotype PubMed 17143286. Source: MGI vasculogenesis Inferred from mutant phenotype PubMed 17143286. Source: MGI
Cellular_component	adherens junction Inferred from direct assay Ref.4. Source: UniProtKB cell-cell junction Inferred from direct assay Ref.4. Source: UniProtKB clathrin-coated endocytic vesicle Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay Ref.4. Source: UniProtKB cytoskeleton Inferred from sequence or structural similarity. Source: UniProtKB myosin complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled Inferred from sequence or structural similarity. Source: UniProtKB actin filament binding Inferred from sequence or structural similarity. Source: UniProtKB calmodulin binding Inferred from sequence or structural similarity. Source: UniProtKB motor activity Inferred from electronic annotation. Source: InterPro phosphatidylinositol binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1107

1107

Unconventional myosin-Ie

PRO_0000415664

Regions

Domain

21 – 679

659

Myosin head-like

Domain

695 – 724

Domain

1050 – 1107

SH3

Nucleotide binding

112 – 119

ATP Potential

Region

581 – 591

Actin-binding Potential

Amino acid modifications

Modified residue

1001

Phosphoserine By similarity

Experimental info

Sequence conflict

V → I in AAH51391. Ref.2

Secondary structure

1107

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

E9Q634 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: D745BE859E2F079D
Show »

FASTA

1,107

126,818

        10         20         30         40         50         60 
MGSKGAYRYH WQSHNVKHSG VDDMVLLSKI TESSIVENLK KRYMDDYIFT YIGSVLISVN 

        70         80         90        100        110        120 
PFKQMPYFGE KEVEMYQGAA QYENPPHIYA LADSMYRNMI IDRENQCVII SGESGAGKTV 

       130        140        150        160        170        180 
AAKYIMSYVS RVSGGGPKVQ HVKDIILQSN PLLEAFGNAK TVRNNNSSRF GKYFEIQFSP 

       190        200        210        220        230        240 
GGEPDGGKIS NFLLEKSRVV MRNPGERSFH IFYQLIEGAS PEQKQSLGIT SMDYYYYLSL 

       250        260        270        280        290        300 
SGSYKVDDID DKRDFQETLH AMNVIGIFSE EQTLVLQIVA GILHLGNISF KEVGNYAAVE 

       310        320        330        340        350        360 
SEEFLAFPAY LLGINQDRLK EKLTSRQMDS KWGGKSESIH VTLNVEQACY TRDALAKALH 

       370        380        390        400        410        420 
ARVFDFLVDS INKAMEKDHE EYNIGVLDIY GFEIFQKNGF EQFCINFVNE KLQQIFIELT 

       430        440        450        460        470        480 
LKAEQEEYVQ EGIRWTPIEY FNNKIVCDLI ESKVNPPGIM SILDDVCATM HAVGEGADQT 

       490        500        510        520        530        540 
LLQKLQMQIG SHEHFNSWNQ GFIIHHYAGK VSYDMDGFCE RNRDVLFMDL IELMQSSELP 

       550        560        570        580        590        600 
FIKSLFPENL QADKKGRPTT AGSKIKKQAN DLVSTLMKCT PHYIRCIKPN ETKKPKDWEE 

       610        620        630        640        650        660 
SRVKHQVEYL GLKENIRVRR AGYAYRRVFQ KFLQRYAILT KATWPVWRGD EKQGVLHLLQ 

       670        680        690        700        710        720 
SVNMDSDQFQ LGRSKVFIKA PESLFLLEEM RERKYDGYAR VIQKTWRKFV ARKKYVQMRE 

       730        740        750        760        770        780 
EASDLLLNKK ERRRNSINRN FIGDYIGMEE RPELQQFVGK REKIDFADTV TKYDRRFKGV 

       790        800        810        820        830        840 
KRDLLLTPKC LYLIGREKVK QGPDKGVVKE VLKRRIEVER ILSVSLSTMQ DDIFILHEQE 

       850        860        870        880        890        900 
YDSLLESVFK TEFLSLLAKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFH 

       910        920        930        940        950        960 
QGFGDLAILK PSNKVLQVSI GPGLPKNSRP TRRNTVTSRG YPGGTKNNYP MRAAPAPPGC 

       970        980        990       1000       1010       1020 
HQNGVIRNQF VPPPHAFGNQ RSNQKSLYTS MARPPLPRQQ STGSDRLSQT PESLDFLKVP 

      1030       1040       1050       1060       1070       1080 
DQGVAGVRRQ TSSRPPPAGG RPKPQPKPKP QVPQCKALYA YDAQDTDELS FNANDIIDII 

      1090       1100 
KEDPSGWWTG RLRGKQGLFP NNYVTKI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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]	"Disruption of Myosin 1e promotes podocyte injury." Krendel M., Kim S.V., Willinger T., Wang T., Kashgarian M., Flavell R.A., Mooseker M.S. J. Am. Soc. Nephrol. 20:86-94(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00330649.

RefSeq

NP_851417.2. NM_181072.3.

UniGene

Mm.249311.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XMF	X-ray	1.50	A	1053-1107	[»]

ProteinModelPortal

E9Q634.

SMR

E9Q634. Positions 20-692, 1053-1107.

ModBase

Search...

PTM databases

PhosphoSite

E9Q634.

Proteomic databases

PRIDE

E9Q634.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034745; ENSMUSP00000034745; ENSMUSG00000032220.

GeneID

71602.

KEGG

mmu:71602.

UCSC

uc009qnx.1. mouse.

Organism-specific databases

CTD

4643.

MGI

MGI:106621. Myo1e.

Phylogenomic databases

GeneTree

ENSGT00690000101741.

HOGENOM

HOG000260265.

HOVERGEN

HBG100702.

K10356.

OMA

KLKKENW.

Gene expression databases

ArrayExpress

E9Q634.

Bgee

E9Q634.

Family and domain databases

InterPro

IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00193. MYOSINHEAVY.
PR00452. SH3DOMAIN.

SMART

SM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.
SSF52540. SSF52540. 1 hit.

PROSITE

PS50096. IQ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MYO1E. mouse.

NextBio

334081.

SOURCE

Search...

Entry information

Entry name

MYO1E_MOUSE

Accession

Primary (citable) accession number: E9Q634
Secondary accession number(s): Q80X36, Q91ZI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2012
Last sequence update:	April 5, 2011
Last modified:	May 29, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents