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Q29122

- MYO6_PIG

UniProt

Q29122 - MYO6_PIG

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Protein

Unconventional myosin-VI

Gene
MYO6
Organism
Sus scrofa (Pig)
Status
Reviewed - 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. Required for structural integrity of inner ear hair cells By similarity.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi151 – 1588ATP Reviewed prediction

GO - Molecular functioni

  1. actin filament binding Source: UniProtKB
  2. ADP binding Source: UniProtKB
  3. ATP binding Source: UniProtKB-KW
  4. calmodulin binding Source: UniProtKB
  5. motor activity Source: UniProtKB

GO - Biological processi

  1. actin filament-based movement Source: UniProtKB
  2. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  3. endocytosis Source: UniProtKB
  4. intracellular protein transport Source: UniProtKB
  5. metabolic process Source: GOC
  6. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. regulation of secretion Source: UniProtKB
  8. sensory perception of sound Source: UniProtKB-KW
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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic membrane-bounded vesicle Source: UniProtKB
  4. DNA-directed RNA polymerase II, holoenzyme Source: UniProtKB
  5. filamentous actin Source: UniProtKB
  6. Golgi apparatus Source: UniProtKB
  7. myosin complex Source: UniProtKB-KW
  8. nuclear membrane Source: UniProtKB
  9. nucleoplasm Source: UniProtKB
  10. nucleus Source: UniProtKB
  11. perinuclear region of cytoplasm Source: UniProtKB
  12. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi406 – 4061T → E: Greatly reduced phosphorylation. Transports uncoated endocytic vesicles to clusters at distinct peripheral sites and alters actin filament structure. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12541254Unconventional myosin-VIPRO_0000271746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei406 – 4061Phosphothreonine1 Publication

Post-translational modificationi

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).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ29122.
PRIDEiQ29122.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi1149220. 2 interactions.
DIPiDIP-48994N.

Structurei

Secondary structure

1
1254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115
Turni12 – 143
Beta strandi15 – 2410
Beta strandi26 – 327
Turni34 – 363
Beta strandi41 – 444
Helixi45 – 473
Helixi62 – 643
Beta strandi65 – 673
Helixi70 – 8213
Beta strandi87 – 904
Beta strandi93 – 975
Turni104 – 1074
Helixi109 – 1157
Turni120 – 1223
Helixi127 – 14115
Beta strandi145 – 1506
Helixi157 – 17216
Beta strandi173 – 1753
Helixi181 – 1844
Helixi186 – 1938
Beta strandi201 – 2044
Beta strandi206 – 2149
Beta strandi220 – 2289
Helixi233 – 2353
Helixi246 – 2549
Helixi257 – 2626
Helixi268 – 2703
Helixi272 – 2754
Helixi285 – 2884
Helixi293 – 2953
Helixi298 – 3036
Helixi313 – 32715
Helixi331 – 34818
Beta strandi352 – 3543
Turni356 – 3594
Beta strandi360 – 3645
Helixi366 – 3683
Helixi369 – 3779
Helixi384 – 3929
Beta strandi393 – 3953
Beta strandi400 – 4034
Beta strandi409 – 4113
Helixi414 – 44128
Beta strandi450 – 4578
Beta strandi464 – 4663
Helixi469 – 48921
Helixi492 – 4998
Helixi513 – 5208
Turni522 – 5243
Helixi526 – 53510
Beta strandi536 – 5383
Helixi541 – 55111
Turni552 – 5543
Beta strandi556 – 5594
Helixi561 – 5633
Beta strandi564 – 5663
Helixi567 – 5693
Beta strandi576 – 5827
Beta strandi585 – 5906
Helixi594 – 5974
Helixi604 – 6118
Helixi616 – 6216
Helixi624 – 6296
Helixi634 – 6385
Helixi644 – 66017
Beta strandi662 – 6709
Helixi683 – 69210
Helixi695 – 7028
Beta strandi704 – 7063
Beta strandi707 – 7115
Helixi712 – 7198
Helixi720 – 7223
Helixi725 – 7284
Helixi732 – 74211
Helixi747 – 7493
Beta strandi750 – 7523
Beta strandi754 – 7596
Helixi764 – 7718
Helixi775 – 78814
Beta strandi818 – 8203
Turni822 – 8254
Helixi867 – 88620
Helixi893 – 91321

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BKHX-ray2.40A2-816[»]
2BKIX-ray2.90A1-859[»]
2V26X-ray1.75A5-789[»]
2VASX-ray2.40A2-816[»]
2VB6X-ray2.30A2-816[»]
2X51X-ray2.20A1-815[»]
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[»]
ProteinModelPortaliQ29122.
SMRiQ29122. Positions 2-826.

Miscellaneous databases

EvolutionaryTraceiQ29122.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 772716Myosin motorAdd
BLAST
Domaini814 – 84330IQAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni273 – 31745Responsible for slow ATPase activityAdd
BLAST
Regioni666 – 6738Actin-binding Reviewed prediction
Regioni783 – 81129Required for binding calmodulinAdd
BLAST
Regioni1085 – 10873Interaction with OPTN

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili847 – 1024178 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi921 – 1028108Glu-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 coiled-coil and a unique globular domain required for interaction with other proteins.

Sequence similaritiesi

Contains 1 IQ domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5022.
HOGENOMiHOG000007806.
HOVERGENiHBG003523.
KOiK10358.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q29122-1 [UniParc]FASTAAdd to Basket

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MEDGKPVWAP HPTDGFQVGN IVDIGPDSLT IEPLNQKGKT FLALINQVFP     50
AEEDSKKDVE DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY 100
FDIPKIYSSE TIKSYQGKSL GTMPPHVFAI ADKAFRDMKV LKLSQSIIVS 150
GESGAGKTEN TKFVLRYLTE SYGTGQDIDD RIVEANPLLE AFGNAKTVRN 200
NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK EERNYHIFYR 250
LCAGASEDIR ERLHLSSPDN FRYLNRGCTR YFANKETDKQ ILQNRKSPEY 300
LKAGSLKDPL LDDHGDFIRM CTAMKKIGLD DEEKLDLFRV VAGVLHLGNI 350
DFEEAGSTSG GCNLKNKSTQ ALEYCAEKLL GLDQDDLRVS LTTRVMLTTA 400
GGAKGTVIKV PLKVEQANNA RDALAKTVYS HLFDHVVNRV NQCFPFETSS 450
YFIGVLDIAG FEYFEHNSFE QFCINYCNEK LQQFFNERIL KEEQELYQKE 500
GLGVNEVHYV DNQDCIDLIE ARLVGILDIL DEENRLPQPS DQHFTSAGHQ 550
KHKDHFRLSI PRKSKLAIHR NIAYDEGFII RHFAGAVCYE TTQFVEKNND 600
ALHMSLESLI CESRDKFIRE LFESSTNNNK DTKQKAGKLS FISVGNKFKT 650
QLNLLLDKLR STGASFIRCI KPNLKMTSHH FEGAQILSQL QCSGMVSVLD 700
LMQGGFPSRA SFHEVYNMYK KSLPDKLARL DPRLFCKALF KALGLNEIDY 750
KFGLTKVFFR PGKFAEFDQI MKSDPDHLAE LVKRVNHWLI CSRWKKVQWC 800
SLSVIKLKNK IKYRAEACIK MQKTIRMWLC KRRHKPRIDG LVKVGTLKKR 850
LDKFNEVVSA LKDGKQEMSK QVKDLEISID ALMAKIKSTM MTREQIQKEY 900
DALVKSSAVL LSALQKKKQQ EEEAERLRRI QEEMEKERKR REEDEQRRRK 950
EEEERRMKLE MEAKRKQEEE ERKKREDDEK RIQAEVEAQL ARQREEESQQ 1000
QAVLEQERRD RELALRIAQS EAELISDEAQ ADPGLRRGPA VQATKAAAGT 1050
KKYDLSKWKY AELRDTINTS CDIELLAACR EEFHRRLKVY HAWKSKNKKR 1100
NTETEQRAPK SVTDYAQQNP AVQLPARQQE IEMNRQQRFF RIPFIRSADQ 1150
YKDPQNKKKG WWYAHFDGPW IARQMELHPD KPPILLVAGK DDMEMCELNL 1200
EETGLTRKRG AEILPRQFEE IWERCGGIQY LQNAIESRQA RPTYATAMLQ 1250
NLLK 1254
Length:1,254
Mass (Da):144,859
Last modified:November 1, 1996 - v1
Checksum:i0A72C1A7991CF763
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z35331 mRNA. Translation: CAA84559.1.
PIRiA54818.
RefSeqiNP_999186.1. NM_214021.1.
UniGeneiSsc.94.

Genome annotation databases

GeneIDi397085.
KEGGissc:397085.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z35331 mRNA. Translation: CAA84559.1 .
PIRi A54818.
RefSeqi NP_999186.1. NM_214021.1.
UniGenei Ssc.94.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BKH X-ray 2.40 A 2-816 [» ]
2BKI X-ray 2.90 A 1-859 [» ]
2V26 X-ray 1.75 A 5-789 [» ]
2VAS X-ray 2.40 A 2-816 [» ]
2VB6 X-ray 2.30 A 2-816 [» ]
2X51 X-ray 2.20 A 1-815 [» ]
3GN4 X-ray 2.70 A/E 771-918 [» ]
3L9I X-ray 2.20 A 2-816 [» ]
4ANJ X-ray 2.60 A 1-817 [» ]
4DBP X-ray 2.20 A 2-816 [» ]
4DBQ X-ray 2.60 A 2-816 [» ]
4DBR X-ray 1.95 A 5-790 [» ]
ProteinModelPortali Q29122.
SMRi Q29122. Positions 2-826.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1149220. 2 interactions.
DIPi DIP-48994N.

Proteomic databases

PaxDbi Q29122.
PRIDEi Q29122.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397085.
KEGGi ssc:397085.

Organism-specific databases

CTDi 4646.

Phylogenomic databases

eggNOGi COG5022.
HOGENOMi HOG000007806.
HOVERGENi HBG003523.
KOi K10358.

Miscellaneous databases

EvolutionaryTracei Q29122.

Family and domain databases

InterProi IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00063. Myosin_head. 1 hit.
[Graphical view ]
PRINTSi PR00193. MYOSINHEAVY.
SMARTi SM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. Cited for: PHOSPHORYLATION AT THR-406, CALCIUM-BINDING, MUTAGENESIS OF THR-406.
  4. Cited for: CALCIUM-CALMODULIN BINDING SITE.
  5. "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.
  6. "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.

Entry informationi

Entry nameiMYO6_PIG
AccessioniPrimary (citable) accession number: Q29122
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 93 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).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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