Q63356 (MYO1E_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Unconventional myosin-Ie

Alternative name(s):
Myosin heavy chain myr 3
Unconventional myosin 1E

Gene names

Name:	Myo1e
Synonyms:	Myr3

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function By similarity. 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.
Subunit structure	Interacts (via SH3 domain) with SYNJ1, DNM1 and DNM2 By similarity. Interacts with CALM and F-actin. Interacts with ARL14EP By similarity.
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cytoplasmic vesicle Probable. Cytoplasmic vesicle › clathrin-coated vesicle By similarity. Cell junction. Note: In cultured podocytes, it localizes close to and is associated with the cytoplasmic membrane, with enrichment at the lamellipodia tips. Colocalizes with cytoplasmic vesicles, including endocytic clathrin-coated vesicles. Colocalizes with dynamin at cytoplasmic vesicles By similarity. Detected in cytoplasmic punctae. Colocalizes with F-actin. Ref.1
Tissue specificity	Detected in brain stem, brain cortex, cerebellum, stomach, colon, heart, lung, liver, spleen and kidney. Detected in utricle, cochlea, outer hair cell bundle cuticular plate and vestibular epithelia (at protein level). Detected in cochlea and vestibular tissues. Detected in kidney, lung, spleen and intestine. Ref.1 Ref.2
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	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from sequence or structural similarity. Source: UniProtKB glomerular basement membrane development Inferred from sequence or structural similarity. Source: UniProtKB glomerular filtration Inferred from sequence or structural similarity. Source: UniProtKB glomerular visceral epithelial cell development Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	adherens junction Inferred from sequence or structural similarity. Source: UniProtKB cell-cell junction Inferred from sequence or structural similarity. Source: UniProtKB clathrin-coated vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB cytoskeleton Inferred from sequence or structural similarity. Source: UniProtKB myosin complex Inferred from electronic annotation. Source: UniProtKB-KW protein complex Inferred from direct assay PubMed 17257598. Source: RGD
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 protein complex binding Inferred from direct assay PubMed 17257598. Source: RGD
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_0000123451
Regions
	Domain	1 – 679	679	Myosin head-like
	Domain	695 – 724	30	IQ
	Domain	1050 – 1107	58	SH3
	Nucleotide binding	112 – 119	8	ATP Potential
	Region	581 – 591	11	Actin-binding Potential
Amino acid modifications
	Modified residue	1001	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63356 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B9D8FBB0CE047148	FASTA	1,107	126,827
	10 20 30 40 50 60 MGSKGAYRYH WQSHNVKHSG VDDMVLLSKI TESSIVENLK KRYMDDYIFT YIGSVLISVN 70 80 90 100 110 120 PFKQMPYFGE KEIEMYQGAA 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 GILHLGNINF 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 DASDLLLNKK ERRRNSINRN FIGDYIGMEE HPELQQFVGK REKIDFADIV TKYDRRFKGV 790 800 810 820 830 840 KRDLLLTPKC LYLIGREKVK QGPDKGLVKE VLKRKIEVER ILSVSLSTMQ DDIFILHEQE 850 860 870 880 890 900 YDSLLESVFK TEFLSLLTKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFY 910 920 930 940 950 960 QGFGDLAILK PSNKVLQVSI GPGLPKNARP TRRNTVSSRG YSGGTNNNYP MRAAPAPPGC 970 980 990 1000 1010 1020 HRNGLTRNQF VHPPRASGNQ RSNQKSLYTS MARPPLPRQQ STGSDRLSQT PESLDFLKVP 1030 1040 1050 1060 1070 1080 DQGAAGVRRQ TTSRPPPAGG RPKPQPKPKP QVPQCKALYA YDAQDTDELS FNANDVIDII 1090 1100 KEDPSGWWTG RLRGKQGLFP NNYVTKI

References

[1]	"A novel mammalian myosin I from rat with an SH3 domain localizes to Con A-inducible, F-actin-rich structures at cell-cell contacts." Stoeffler H.E., Ruppert C., Reinhard J., Bahler M. J. Cell Biol. 129:819-830(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACTIN-BINDING, CALMODULIN-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: Sprague-Dawley.
[2]	"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: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X74815 mRNA. Translation: CAA52815.1.
IPI	IPI00207988.
PIR	S52517.
RefSeq	NP_775124.1. NM_173101.1.
UniGene	Rn.8737.
3D structure databases
ProteinModelPortal	Q63356.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000016482.
PTM databases
PhosphoSite	Q63356.
Proteomic databases
PaxDb	Q63356.
PRIDE	Q63356.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	25484.
KEGG	rno:25484.
UCSC	RGD:3144. rat.
Organism-specific databases
CTD	4643.
RGD	3144. Myo1e.
Phylogenomic databases
eggNOG	COG5022.
HOGENOM	HOG000260265.
HOVERGEN	HBG100702.
KO	K10356.
OrthoDB	EOG49W2DM.
Gene expression databases
ArrayExpress	Q63356.
Genevestigator	Q63356.
GermOnline	ENSRNOG00000011886. Rattus norvegicus.
Family and domain databases
InterPro	IPR000048. IQ_motif_EF-hand-BS. IPR001609. Myosin_head_motor_dom. IPR010926. Myosin_tail_2. 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.
PROSITE	PS50096. IQ. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	606831.

Entry information

Entry name

MYO1E_RAT

Accession

Primary (citable) accession number: Q63356

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program