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Protein

Unconventional myosin-VI

Gene

MYO6

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi151 – 1588ATPSequence analysis

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • ADP binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: UniProtKB
  • motor activity Source: UniProtKB
  • plus-end directed microfilament motor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Endocytosis, Hearing, Protein transport, Transport

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-VI
Alternative name(s):
Unconventional myosin-6
Gene namesi
Name:MYO6
Synonyms:CMY6
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: UniProtKB
  • cell cortex Source: UniProtKB
  • clathrin-coated vesicle Source: UniProtKB
  • clathrin-coated vesicle membrane Source: UniProtKB-SubCell
  • coated pit Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB
  • DNA-directed RNA polymerase II, holoenzyme Source: UniProtKB
  • filamentous actin Source: UniProtKB
  • filopodium Source: UniProtKB-SubCell
  • Golgi apparatus Source: UniProtKB
  • microvillus Source: UniProtKB-SubCell
  • myosin complex Source: UniProtKB-KW
  • nuclear membrane Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • ruffle Source: UniProtKB
  • ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Coated pit, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1088 – 10881T → A: No effect on binding to OPTN; when associated with A-1091. 1 Publication
Mutagenesisi1088 – 10881T → E: Abolishes binding to OPTN; when associated with E-1091. 1 Publication
Mutagenesisi1091 – 10911T → A: No effect on binding to OPTN; when associated with A-1088. 1 Publication
Mutagenesisi1091 – 10911T → E: Abolishes binding to OPTN; when associated with E-1088. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12761276Unconventional myosin-VIPRO_0000271747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei405 – 4051PhosphothreonineBy similarity
Modified residuei1088 – 10881Phosphothreonine1 Publication
Modified residuei1091 – 10911Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylation in the motor domain, induced by EGF, results in translocation of MYO6 from the cell surface to membrane ruffles. Phosphorylated in vitro by p21-activated kinase (PAK).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9I8D1.
PRIDEiQ9I8D1.

PTM databases

iPTMnetiQ9I8D1.

Interactioni

Subunit structurei

Homodimer; dimerization seems to implicate the unfolding of the three-helix bundle region creating an additional calmodulin binding site, and cargo binding (By similarity). Binding to calmodulin through a unique insert, not found in other myosins, located in the neck region between the motor domain and the IQ domain appears to contribute to the directionality reversal. This interaction occurs only if the C-terminal lobe of calmodulin is occupied by calcium. Interacts with DAB2. In vitro, the C-terminal globular tail binds a C-terminal region of DAB2 (By similarity). Interacts with OPTN.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Dab2P980782EBI-6307292,EBI-1391846From a different organism.

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • calmodulin binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ9I8D1. 4 interactions.
STRINGi9031.ENSGALP00000031021.

Structurei

3D structure databases

ProteinModelPortaliQ9I8D1.
SMRiQ9I8D1. Positions 2-825.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 771715Myosin motorAdd
BLAST
Domaini813 – 84230IQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni273 – 31745Responsible for slow ATPase activityBy similarityAdd
BLAST
Regioni665 – 6728Actin-bindingSequence analysis
Regioni782 – 81029Required for binding calmodulinBy similarityAdd
BLAST
Regioni835 – 91682Three-helix bundleBy similarityAdd
BLAST
Regioni917 – 98468SAHBy similarityAdd
BLAST
Regioni1107 – 11093Interaction with OPTN

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi920 – 1027108Glu-richAdd
BLAST

Domaini

Divided into three regions: a N-terminal motor (head) domain, followed by a neck domain consisting of a calmodulin-binding linker domain and a single IQ motif, and a C-terminal tail region with a three-helix bundle region, a SAH domain and a unique globular domain required for interaction with other proteins such as cargo-binding.Curated
The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0163. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000007806.
HOVERGENiHBG003523.
InParanoidiQ9I8D1.
KOiK10358.
PhylomeDBiQ9I8D1.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR032412. Myosin-VI_CBD.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF16521. Myosin-VI_CBD. 1 hit.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9I8D1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEDGKPVWAP HPTDGFQMGM IVDIGTDYLT IEPLNQKGKT FQAAINQVFP
60 70 80 90 100
AEEDSKKDVE DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY
110 120 130 140 150
FDIPKFYSSD AIKKYQGRSL GTLPPHVFAI ADKAYRDMKV LKMSQSIIVS
160 170 180 190 200
GESGAGKTEN TKFVLRYLTE SYGTGQDIDD RIVEANPLLE AFGNAKTIRN
210 220 230 240 250
NNSSRFGKFV EIHFNEKNSV VGGFVSHYLL EKSRICVQGK EERNYHIFYR
260 270 280 290 300
LCAGAPEDIR EKLYLSSPDS FRYLNRGCTR YFATKETDKQ ILQNRKSPEY
310 320 330 340 350
LKAGSLKDPL LDDHGDFNRM CTAMKKIGLD DAEKLDLFRV VAGVLHLGNI
360 370 380 390 400
DFEEAGSTSG GCTLKAQSQP ALECCAALLG LDEEDLRVSL TTRVMLTTAG
410 420 430 440 450
GAKGTVIKVP LKVEQANNAR DALAKTVYSH LFDHVVNRVN QCFPFETSSF
460 470 480 490 500
FIGVLDIAGF EYFEHNSFEQ FCINYCNEKL QQFFNERILK EEQELYQKEG
510 520 530 540 550
LGVNEVRYVD NQDCIDLIEA KLIGVLDILD EENRLPQPSD QHFTSVVHQK
560 570 580 590 600
HKDHFRLSIP RKSKLAVHRN VRDDEGFIIR HFAGAVCYET TQFVEKNNDA
610 620 630 640 650
LHMSLESLIC ESKDKFVRQL FESNTNNNKD PKQKAGKLSF ISVGNKFKTQ
660 670 680 690 700
LNLLLEKLHS TGSSFIRCIF PNLKMTSHHF EGGQILSQLQ CSGMVSVLDL
710 720 730 740 750
MQGGFPSRAS FHELYNMYKK YLPEKLARLD PRLFCKALFK ALGLNEIDYK
760 770 780 790 800
FGLTKVFFRP GKFAEFDQIM KSDPDHLAEL VKRVNHWLIC SRWKKVQWCS
810 820 830 840 850
LSVIKLKNKI KYRASACIKI QKTIRMWLCK RKHKPRIDGL IKVRTLKKRL
860 870 880 890 900
DKFNEVVSAL KEGKAETSKQ IKELEYSIDA SMTKIKTTMM TREQIMKEYD
910 920 930 940 950
ALVRSSEQLL SALQKKKQQE EEAERLRRIQ EEMEKERKRR EEEEKRRRKE
960 970 980 990 1000
EEERRLKSEI EAKRKQEEEE RKKREEEEKR IQAEIEAQLA REREEETQHQ
1010 1020 1030 1040 1050
AILEQERRDR ELAMRIAQTG AELSTEETKL DVGLCRANGT KLQMTAEQMA
1060 1070 1080 1090 1100
KEMSEMLSRG PAVQATKAAA GAKKHDLSKW KYAELRDTIN TSCDIELLAA
1110 1120 1130 1140 1150
CREEFHRRLK VYHAWKSKNK KRNAETEQRA PKSVTDYAQQ NPTAQLPMRQ
1160 1170 1180 1190 1200
QEIEINRQQR YFRIPFIRPM DQYKDPQNKK KGWWYAHFDG PWIARQMELH
1210 1220 1230 1240 1250
PDKAPILLVA GKDDMDMCEL NLEETGLTRK RGAEILPRQF EEIWERCGGI
1260 1270
QYLQNAIESR QARPTYATAM LQNLLK
Length:1,276
Mass (Da):147,604
Last modified:October 1, 2000 - v1
Checksum:i5F6AEE43A6FB260F
GO
Isoform 2 (identifier: Q9I8D1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1036-1058: Missing.

Show »
Length:1,253
Mass (Da):145,036
Checksum:iFDCA2D6B56BFB4D3
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1036 – 105823Missing in isoform 2. 1 PublicationVSP_022331Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278608 mRNA. Translation: CAB96536.1.
RefSeqiNP_990066.1. NM_204735.1. [Q9I8D1-1]
UniGeneiGga.3147.

Genome annotation databases

GeneIDi395487.
KEGGigga:395487.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278608 mRNA. Translation: CAB96536.1.
RefSeqiNP_990066.1. NM_204735.1. [Q9I8D1-1]
UniGeneiGga.3147.

3D structure databases

ProteinModelPortaliQ9I8D1.
SMRiQ9I8D1. Positions 2-825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9I8D1. 4 interactions.
STRINGi9031.ENSGALP00000031021.

PTM databases

iPTMnetiQ9I8D1.

Proteomic databases

PaxDbiQ9I8D1.
PRIDEiQ9I8D1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi395487.
KEGGigga:395487.

Organism-specific databases

CTDi4646.

Phylogenomic databases

eggNOGiKOG0163. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000007806.
HOVERGENiHBG003523.
InParanoidiQ9I8D1.
KOiK10358.
PhylomeDBiQ9I8D1.

Miscellaneous databases

PROiQ9I8D1.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR032412. Myosin-VI_CBD.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF16521. Myosin-VI_CBD. 1 hit.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The localization of myosin VI at the Golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation."
    Buss F., Kendrick-Jones J., Lionne C., Knight A.E., Cote G.P., Paul Luzio J.
    J. Cell Biol. 143:1535-1545(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, PHOSPHORYLATION.
    Tissue: Intestine.
  2. "Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis."
    Buss F., Arden S.D., Lindsay M., Luzio J.P., Kendrick-Jones J.
    EMBO J. 20:3676-3684(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  3. "Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis."
    Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J., Luzio J.P., Kendrick-Jones J., Buss F.
    J. Cell Biol. 169:285-295(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH OPTN, PHOSPHORYLATION AT THR-1088 AND THR-1091, MUTAGENESIS OF THR-1088 AND THR-1091.

Entry informationi

Entry nameiMYO6_CHICK
AccessioniPrimary (citable) accession number: Q9I8D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 94 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-6 (MYH6).Curated
Originally predicted to contain a coiled coil domain but generally accepted to contain a stable SAH domain instead.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.