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Q29122

- MYO6_PIG

UniProt

Q29122 - MYO6_PIG

Protein

Unconventional myosin-VI

Gene

MYO6

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.By similarity

    Regions

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

    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

    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 By similarity; 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.By similarity

    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

    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.By similarity

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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-bindingSequence Analysis
    Regioni783 – 81129Required for binding calmodulinAdd
    BLAST
    Regioni1085 – 10873Interaction with OPTN

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili847 – 1024178Sequence AnalysisAdd
    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.Curated
    Contains 1 myosin motor domain.Curated

    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

    « Hide

    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: October 1, 2014
    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

    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