Q12965 (MYO1E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Unconventional myosin-Ie

Alternative name(s):
Myosin-Ic
Unconventional myosin 1E

Gene names

Name:	MYO1E
Synonyms:	MYO1C

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1108 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. 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. Ref.5 Ref.6 Ref.8
Subunit structure	Interacts with CALM and F-actin By similarity. Interacts (via SH3 domain) with SYNJ1, DNM1 and DNM2. Interacts with ARL14EP. Ref.5 Ref.6 Ref.11
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cytoplasmic vesicle. Cytoplasmic vesicle › clathrin-coated vesicle. Cell junction By similarity. Note: Colocalizes with F-actin By similarity. 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. Ref.6 Ref.8 Ref.12
Tissue specificity	Expressed in the immune system. In the kidney, predominantly expressed in the glomerulus, including podocytes. Ref.11 Ref.12
Involvement in disease	Focal segmental glomerulosclerosis 6 (FSGS6) [MIM:614131]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. FSGS6 is a childhood-onset disorder resulting in nephrotic syndrome, which includes massive proteinuria, hypoalbuminemia, hyperlipidemia, and edema. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13
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
Coding sequence diversity	Polymorphism
Disease	Disease mutation
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	actin filament-based movement Traceable author statement Ref.1. Source: UniProtKB endocytosis Inferred from mutant phenotype Ref.6. 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 in utero embryonic development Inferred from electronic annotation. Source: Compara platelet-derived growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara post-embryonic hemopoiesis Inferred from electronic annotation. Source: Compara vasculogenesis Inferred from electronic annotation. Source: Compara
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 myosin complex Traceable author statement Ref.5. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled Inferred from direct assay Ref.5. Source: UniProtKB actin filament binding Inferred from direct assay Ref.5. Source: UniProtKB calmodulin binding Inferred from direct assay Ref.5. Source: UniProtKB microfilament motor activity Traceable author statement Ref.1. Source: UniProtKB phosphatidylinositol binding Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARL14EP	Q8N8R7	2	EBI-4279548,EBI-2807994

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1108	1108	Unconventional myosin-Ie		PRO_0000123450
Regions
	Domain	1 – 679	679	Myosin head-like
	Domain	695 – 724	30	IQ
	Domain	1051 – 1108	58	SH3
	Nucleotide binding	112 – 119	8	ATP Potential
	Region	581 – 591	11	Actin-binding Potential
Amino acid modifications
	Modified residue	980	1	Phosphoserine Ref.7 Ref.9
	Modified residue	1002	1	Phosphoserine Ref.7
Natural variations
	Natural variant	159	1	A → P in FSGS6; the mutant shows diffuse cytosolic localization with a punctate pattern. Ref.12 Ref.13		VAR_065958
	Natural variant	185	1	D → G. Ref.12 Corresponds to variant rs141565214 [ dbSNP | Ensembl ].		VAR_065959
	Natural variant	221	1	A → V. Ref.12		VAR_065960
	Natural variant	795	1	G → R. Ref.12		VAR_065961
	Natural variant	1049	1	P → H. Ref.12 Corresponds to variant rs147579391 [ dbSNP | Ensembl ].		VAR_065962
Experimental info
	Sequence conflict	889 – 892	4	WSAG → GVQGA in AAA62667. Ref.1
	Sequence conflict	984	1	N → I in AAA62667. Ref.1
	Sequence conflict	1097	1	Q → P in AAA62667. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q12965 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 3073050B9BB4DDC6	FASTA	1,108	127,062
	10 20 30 40 50 60 MGSKGVYQYH WQSHNVKHSG VDDMVLLSKI TENSIVENLK KRYMDDYIFT YIGSVLISVN 70 80 90 100 110 120 PFKQMPYFGE KEIEMYQGAA QYENPPHIYA LADNMYRNMI IDRENQCVII SGESGAGKTV 130 140 150 160 170 180 AAKYIMSYIS RVSGGGTKVQ HVKDIILQSN PLLEAFGNAK TVRNNNSSRF GKYFEIQFSP 190 200 210 220 230 240 GGEPDGGKIS NFLLEKSRVV MRNPGERSFH IFYQLIEGAS AEQKHSLGIT SMDYYYYLSL 250 260 270 280 290 300 SGSYKVDDID DRREFQETLH AMNVIGIFAE 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 ENKVNPPGIM 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 ETKKPRDWEE 610 620 630 640 650 660 SRVKHQVEYL GLKENIRVRR AGYAYRRIFQ KFLQRYAILT KATWPSWQGE EKQGVLHLLQ 670 680 690 700 710 720 SVNMDSDQFQ LGRSKVFIKA PESLFLLEEM RERKYDGYAR VIQKSWRKFV ARKKYVQMRE 730 740 750 760 770 780 EASDLLLNKK ERRRNSINRN FIGDYIGMEE HPELQQFVGK REKIDFADTV TKYDRRFKGV 790 800 810 820 830 840 KRDLLLTPKC LYLIGREKVK QGPDKGLVKE VLKRKIEIER ILSVSLSTMQ DDIFILHEQE 850 860 870 880 890 900 YDSLLESVFK TEFLSLLAKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFH 910 920 930 940 950 960 QGFGDLAVLK PSNKVLQVSI GPGLPKNSRP TRRNTTQNTG YSSGTQNANY PVRAAPPPPG 970 980 990 1000 1010 1020 YHQNGVIRNQ YVPYPHAPGS QRSNQKSLYT SMARPPLPRQ QSTSSDRVSQ TPESLDFLKV 1030 1040 1050 1060 1070 1080 PDQGAAGVRR QTTSRPPPAG GRPKPQPKPK PQVPQCKALY AYDAQDTDEL SFNANDIIDI 1090 1100 IKEDPSGWWT GRLRGKQGLF PNNYVTKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and mRNA expression of human unconventional myosin-IC. A homologue of amoeboid myosins-I with a single IQ motif and an SH3 domain." Bement W.M., Wirth J.A., Mooseker M.S. J. Mol. Biol. 243:356-363(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types." Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S. Proc. Natl. Acad. Sci. U.S.A. 91:6549-6553(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 107-196.
[4]	Erratum Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S. Proc. Natl. Acad. Sci. U.S.A. 91:11767-11767(1994) [PubMed] [Europe PMC] [Abstract]
[5]	"The kinetic mechanism of Myo1e (human myosin-IC)." El Mezgueldi M., Tang N., Rosenfeld S.S., Ostap E.M. J. Biol. Chem. 277:21514-21521(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ATP HYDROLYSIS, INTERACTION WITH F-ACTIN AND CALM.
[6]	"Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis." Krendel M., Osterweil E.K., Mooseker M.S. FEBS Lett. 581:644-650(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SYNJ1; DNM1 AND DNM2.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-980 AND SER-1002, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Myo1e binds anionic phospholipids with high affinity." Feeser E.A., Ignacio C.M., Krendel M., Ostap E.M. Biochemistry 49:9353-9360(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-980, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"A Genome-wide multidimensional RNAi screen reveals pathways controlling MHC class II antigen presentation." Paul P., van den Hoorn T., Jongsma M.L., Bakker M.J., Hengeveld R., Janssen L., Cresswell P., Egan D.A., van Ham M., Ten Brinke A., Ovaa H., Beijersbergen R.L., Kuijl C., Neefjes J. Cell 145:268-283(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARL14EP, TISSUE SPECIFICITY.
[12]	"MYO1E mutations and childhood familial focal segmental glomerulosclerosis." Mele C., Iatropoulos P., Donadelli R., Calabria A., Maranta R., Cassis P., Buelli S., Tomasoni S., Piras R., Krendel M., Bettoni S., Morigi M., Delledonne M., Pecoraro C., Abbate I., Capobianchi M.R., Hildebrandt F., Otto E. , Schaefer F., Macciardi F., Ozaltin F., Emre S., Ibsirlioglu T., Benigni A., Remuzzi G., Noris M. N. Engl. J. Med. 365:295-306(2011) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT FSGS6 PRO-159, VARIANTS GLY-185; VAL-221; ARG-795 AND HIS-1049, CHARACTERIZATION OF VARIANT FSGS6 PRO-159.
[13]	"Exome sequencing identified MYO1E and NEIL1 as candidate genes for human autosomal recessive steroid-resistant nephrotic syndrome." Sanna-Cherchi S., Burgess K.E., Nees S.N., Caridi G., Weng P.L., Dagnino M., Bodria M., Carrea A., Allegretta M.A., Kim H.R., Perry B.J., Gigante M., Clark L.N., Kisselev S., Cusi D., Gesualdo L., Allegri L., Scolari F. , D'Agati V., Shapiro L.S., Pecoraro C., Palomero T., Ghiggeri G.M., Gharavi A.G. Kidney Int. 80:389-396(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FSGS6 PRO-159.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14391 mRNA. Translation: AAA62667.1. AC092756 Genomic DNA. No translation available. L29139 mRNA. Translation: AAA20902.1.
IPI	IPI00329672.
PIR	S53601.
RefSeq	NP_004989.2. NM_004998.3.
UniGene	Hs.654506.
3D structure databases
ProteinModelPortal	Q12965.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-884N.
IntAct	Q12965. 1 interaction.
STRING	9606.ENSP00000288235.
PTM databases
PhosphoSite	Q12965.
Polymorphism databases
DMDM	215274106.
Proteomic databases
PaxDb	Q12965.
PRIDE	Q12965.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000288235; ENSP00000288235; ENSG00000157483.
GeneID	4643.
KEGG	hsa:4643.
UCSC	uc002aga.3. human.
Organism-specific databases
CTD	4643.
GeneCards	GC15M059428.
H-InvDB	HIX0038144.
HGNC	HGNC:7599. MYO1E.
HPA	HPA023886.
MIM	601479. gene. 614131. phenotype.
neXtProt	NX_Q12965.
Orphanet	93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKB	PA31401.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5022.
HOGENOM	HOG000260265.
HOVERGEN	HBG100702.
InParanoid	Q12965.
KO	K10356.
OMA	KLKKENW.
OrthoDB	EOG49W2DM.
PhylomeDB	Q12965.
Gene expression databases
ArrayExpress	Q12965.
Bgee	Q12965.
CleanEx	HS_MYO1C. HS_MYO1E.
Genevestigator	Q12965.
GermOnline	ENSG00000157483. Homo sapiens.
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
ChiTaRS	MYO1E. human.
GenomeRNAi	4643.
NextBio	17892.
SOURCE	Search...

Entry information

Entry name

MYO1E_HUMAN

Accession

Primary (citable) accession number: Q12965
Secondary accession number(s): Q14778

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.