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Q29122 (MYO6_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional myosin-VI
Alternative name(s):
Unconventional myosin-6
Gene names
Name:MYO6
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length1254 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Required for structural integrity of inner ear hair cells By similarity. Ref.6

Subunit structure

Homodimer. 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. Interaction with F-actin/ACTN1 occurs only at the apical brush border domain of the proximal tubule cells. Interacts with DAB2. In vitro, the C-terminal globular tail binds a C-terminal region of DAB2. Interacts with CFTR. Forms a complex with CFTR and DAB2 in the apical membrane of epithelial cells. Interacts with OPTN By similarity. Ref.1

Subcellular location

Golgi apparatustrans-Golgi network membrane; Peripheral membrane protein By similarity. Golgi apparatus By similarity. Nucleus By similarity. Cytoplasmperinuclear region By similarity. Note: Also present in endocyctic vesicles, and membrane ruffles. Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage. Recruited into membrane ruffles from cell surface by EGF-stimulation. Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane By similarity. Ref.1 Ref.6

Tissue specificity

Expressed in all tissues examined including kidney cortex, intestinal mucosa, liver, lung, heart, jowl muscle, brain cortex and medulla, and in the epithelial cell line, LLC-PK1. In the kidney, located to the brush border of adult kidney proximal tubule cells. Ref.1

Developmental stage

Locates to the apical domain only during the final stages of kidney proximal tubule development.

Domain

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 coiled-coil and a unique globular domain required for interaction with other proteins.

Post-translational modification

Phosphorylation in the motor domain, induced by EGF, results in translocation of MYO6 from the cell surface to membrane ruffles and affects F-actin dynamics. Phosphorylated in vitro by p21-activated kinase (PAK). Ref.4

Sequence similarities

Contains 1 IQ domain.

Contains 1 myosin head-like domain.

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-6 (MYH6).

Ontologies

Keywords
   Biological processEndocytosis
Hearing
Protein transport
Transport
   Cellular componentCytoplasm
Golgi apparatus
Membrane
Nucleus
   DomainCoiled coil
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament-based movement

Inferred from direct assay PubMed 10519557. Source: UniProtKB

endocytosis

Inferred from mutant phenotype PubMed 12857860. Source: UniProtKB

intracellular protein transport

Inferred from mutant phenotype PubMed 12857860. Source: UniProtKB

metabolic process

Inferred from direct assay PubMed 10519557. Source: GOC

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of secretion

Inferred from sequence or structural similarity. Source: UniProtKB

sensory perception of sound

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentDNA-directed RNA polymerase II, holoenzyme

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

cell cortex

Inferred from direct assay PubMed 12857860. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 12857860. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

filamentous actin

Inferred from direct assay PubMed 10519557. Source: UniProtKB

myosin complex

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear membrane

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 12857860. Source: UniProtKB

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionADP binding

Inferred from direct assay PubMed 10519557. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

actin filament binding

Inferred from direct assay PubMed 10519557. Source: UniProtKB

calmodulin binding

Inferred from physical interaction Ref.5. Source: UniProtKB

motor activity

Inferred from direct assay PubMed 10519557. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12541254Unconventional myosin-VI
PRO_0000271746

Regions

Domain59 – 760702Myosin head-like
Domain814 – 84330IQ
Nucleotide binding151 – 1588ATP Potential
Region273 – 31745Responsible for slow ATPase activity
Region666 – 6738Actin-binding Potential
Region783 – 81129Required for binding calmodulin
Region1085 – 10873Interaction with OPTN
Coiled coil847 – 1024178 Potential
Compositional bias921 – 1028108Glu-rich

Amino acid modifications

Modified residue4061Phosphothreonine Ref.4

Experimental info

Mutagenesis4061T → E: Greatly reduced phosphorylation. Transports uncoated endocytic vesicles to clusters at distinct peripheral sites and alters actin filament structure. Ref.4 Ref.6

Secondary structure

......................................................................................................................................................... 1254
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q29122 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0A72C1A7991CF763

FASTA1,254144,859
        10         20         30         40         50         60 
MEDGKPVWAP HPTDGFQVGN IVDIGPDSLT IEPLNQKGKT FLALINQVFP AEEDSKKDVE 

        70         80         90        100        110        120 
DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY FDIPKIYSSE TIKSYQGKSL 

       130        140        150        160        170        180 
GTMPPHVFAI ADKAFRDMKV LKLSQSIIVS GESGAGKTEN TKFVLRYLTE SYGTGQDIDD 

       190        200        210        220        230        240 
RIVEANPLLE AFGNAKTVRN NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK 

       250        260        270        280        290        300 
EERNYHIFYR LCAGASEDIR ERLHLSSPDN FRYLNRGCTR YFANKETDKQ ILQNRKSPEY 

       310        320        330        340        350        360 
LKAGSLKDPL LDDHGDFIRM CTAMKKIGLD DEEKLDLFRV VAGVLHLGNI DFEEAGSTSG 

       370        380        390        400        410        420 
GCNLKNKSTQ ALEYCAEKLL GLDQDDLRVS LTTRVMLTTA GGAKGTVIKV PLKVEQANNA 

       430        440        450        460        470        480 
RDALAKTVYS HLFDHVVNRV NQCFPFETSS YFIGVLDIAG FEYFEHNSFE QFCINYCNEK 

       490        500        510        520        530        540 
LQQFFNERIL KEEQELYQKE GLGVNEVHYV DNQDCIDLIE ARLVGILDIL DEENRLPQPS 

       550        560        570        580        590        600 
DQHFTSAGHQ KHKDHFRLSI PRKSKLAIHR NIAYDEGFII RHFAGAVCYE TTQFVEKNND 

       610        620        630        640        650        660 
ALHMSLESLI CESRDKFIRE LFESSTNNNK DTKQKAGKLS FISVGNKFKT QLNLLLDKLR 

       670        680        690        700        710        720 
STGASFIRCI KPNLKMTSHH FEGAQILSQL QCSGMVSVLD LMQGGFPSRA SFHEVYNMYK 

       730        740        750        760        770        780 
KSLPDKLARL DPRLFCKALF KALGLNEIDY KFGLTKVFFR PGKFAEFDQI MKSDPDHLAE 

       790        800        810        820        830        840 
LVKRVNHWLI CSRWKKVQWC SLSVIKLKNK IKYRAEACIK MQKTIRMWLC KRRHKPRIDG 

       850        860        870        880        890        900 
LVKVGTLKKR LDKFNEVVSA LKDGKQEMSK QVKDLEISID ALMAKIKSTM MTREQIQKEY 

       910        920        930        940        950        960 
DALVKSSAVL LSALQKKKQQ EEEAERLRRI QEEMEKERKR REEDEQRRRK EEEERRMKLE 

       970        980        990       1000       1010       1020 
MEAKRKQEEE ERKKREDDEK RIQAEVEAQL ARQREEESQQ QAVLEQERRD RELALRIAQS 

      1030       1040       1050       1060       1070       1080 
EAELISDEAQ ADPGLRRGPA VQATKAAAGT KKYDLSKWKY AELRDTINTS CDIELLAACR 

      1090       1100       1110       1120       1130       1140 
EEFHRRLKVY HAWKSKNKKR NTETEQRAPK SVTDYAQQNP AVQLPARQQE IEMNRQQRFF 

      1150       1160       1170       1180       1190       1200 
RIPFIRSADQ YKDPQNKKKG WWYAHFDGPW IARQMELHPD KPPILLVAGK DDMEMCELNL 

      1210       1220       1230       1240       1250 
EETGLTRKRG AEILPRQFEE IWERCGGIQY LQNAIESRQA RPTYATAMLQ NLLK 

« Hide

References

[1]"Porcine myosin-VI: characterization of a new mammalian unconventional myosin."
Hasson T., Mooseker M.S.
J. Cell Biol. 127:425-440(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH ACTN1, SUBCELLULAR LOCATION.
Tissue: Kidney.
[2]"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].
Tissue: Kidney.
[3]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]
[4]"Calcium functionally uncouples the heads of myosin VI."
Morris C.A., Wells A.L., Yang Z., Chen L.Q., Baldacchino C.V., Sweeney H.L.
J. Biol. Chem. 278:23324-23330(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-406, CALCIUM-BINDING, MUTAGENESIS OF THR-406.
[5]"The unique insert in myosin VI is a structural calcium-calmodulin binding site."
Bahloul A., Chevreux G., Wells A.L., Martin D., Nolt J., Yang Z., Chen L.-Q., Potier N., van Dorsselaer A., Rosenfeld S., Houdusse A., Sweeney H.L.
Proc. Natl. Acad. Sci. U.S.A. 101:4787-4792(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CALCIUM-CALMODULIN BINDING SITE.
[6]"Myosin VI altered at threonine 406 stabilizes actin filaments in vivo."
Naccache S.N., Hasson T.
Cell Motil. Cytoskeleton 63:633-645(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF THR-406, POSSIBLE FUNCTION, SUBCELLULAR LOCATION.
[7]"The structure of the myosin VI motor reveals the mechanism of directionality reversal."
Menetrey J., Bahloul A., Wells A.L., Yengo C.M., Morris C.A., Sweeney H.L., Houdusse A.
Nature 435:779-785(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-859 IN COMPLEX WITH CALMODULIN, ATPASE ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z35331 mRNA. Translation: CAA84559.1.
PIRA54818.
RefSeqNP_999186.1. NM_214021.1.
UniGeneSsc.94.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BKHX-ray2.40A2-816[»]
2BKIX-ray2.90A1-859[»]
2V26X-ray1.75A5-789[»]
2VASX-ray2.40A2-816[»]
2VB6X-ray2.30A2-816[»]
2X51X-ray2.20A1-816[»]
3GN4X-ray2.70A/E771-918[»]
3L9IX-ray2.20A2-816[»]
4ANJX-ray2.60A1-817[»]
4DBPX-ray2.20A2-816[»]
4DBQX-ray2.60A2-816[»]
4DBRX-ray1.95A5-790[»]
ProteinModelPortalQ29122.
SMRQ29122. Positions 2-826.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1149220. 2 interactions.
DIPDIP-48994N.

Proteomic databases

PaxDbQ29122.
PRIDEQ29122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397085.
KEGGssc:397085.

Organism-specific databases

CTD4646.

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000007806.
HOVERGENHBG003523.
KOK10358.

Family and domain databases

InterProIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ29122.

Entry information

Entry nameMYO6_PIG
AccessionPrimary (citable) accession number: Q29122
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references