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Protein

Unconventional myosin-VI

Gene

MYO6

Organism
Sus scrofa (Pig)
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. Required for structural integrity of inner ear hair cells (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi151 – 158ATPSequence analysis8

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • ADP binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: UniProtKB
  • motor activity Source: UniProtKB

GO - Biological processi

  • actin filament-based movement Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  • endocytosis Source: UniProtKB
  • intracellular protein transport Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of secretion Source: UniProtKB
  • 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
Proteomesi
  • UP000008227 Componenti: 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

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

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi406T → E: Greatly reduced phosphorylation. Transports uncoated endocytic vesicles to clusters at distinct peripheral sites and alters actin filament structure. 2 Publications1
Mutagenesisi851L → A: Abolishes additional calmodulin-binding upon unfolding three-helix bundle; when associated with A-854, A-857, A-858 and A-861. 1 Publication1
Mutagenesisi854F → A: Abolishes additional calmodulin-binding upon unfolding three-helix bundle; when associated with A-851, A-857, A-858 and A-861. 1 Publication1
Mutagenesisi857V → A: Abolishes additional calmodulin-binding upon unfolding three-helix bundle; when associated with A-851, A-854, A-858 and A-861. 1 Publication1
Mutagenesisi858V → A: Abolishes additional calmodulin-binding upon unfolding three-helix bundle; when associated with A-851, A-851, A-857 and A-861. 1 Publication1
Mutagenesisi861L → A: Abolishes additional calmodulin-binding upon unfolding three-helix bundle; when associated with A-851, A-854, A-857 and A-858. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002717461 – 1254Unconventional myosin-VIAdd BLAST1254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei267PhosphoserineBy similarity1
Modified residuei406Phosphothreonine1 Publication1
Modified residuei605PhosphoserineBy similarity1
Modified residuei1026PhosphoserineBy similarity1

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.
PeptideAtlasiQ29122.
PRIDEiQ29122.

PTM databases

iPTMnetiQ29122.

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; dimerization seems to implicate the unfolding of the three-helix bundle region creating an additional calmodulin binding site, and cargo binding (PubMed:25122759, PubMed:19664948, PubMed:25159143). 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 similarity2 Publications

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi1149220. 2 interactors.
DIPiDIP-48994N.
STRINGi9823.ENSSSCP00000004831.

Structurei

Secondary structure

11254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Turni12 – 14Combined sources3
Beta strandi15 – 24Combined sources10
Beta strandi26 – 32Combined sources7
Turni34 – 36Combined sources3
Beta strandi41 – 44Combined sources4
Helixi45 – 47Combined sources3
Helixi62 – 64Combined sources3
Beta strandi65 – 67Combined sources3
Helixi70 – 82Combined sources13
Beta strandi87 – 90Combined sources4
Beta strandi93 – 97Combined sources5
Turni104 – 107Combined sources4
Helixi109 – 115Combined sources7
Turni120 – 122Combined sources3
Helixi127 – 141Combined sources15
Beta strandi145 – 150Combined sources6
Helixi157 – 172Combined sources16
Beta strandi173 – 175Combined sources3
Helixi181 – 184Combined sources4
Helixi186 – 193Combined sources8
Beta strandi201 – 204Combined sources4
Beta strandi206 – 214Combined sources9
Beta strandi220 – 228Combined sources9
Helixi233 – 235Combined sources3
Helixi246 – 254Combined sources9
Helixi257 – 262Combined sources6
Helixi268 – 270Combined sources3
Helixi272 – 275Combined sources4
Helixi285 – 288Combined sources4
Helixi293 – 295Combined sources3
Helixi298 – 303Combined sources6
Helixi313 – 327Combined sources15
Helixi331 – 348Combined sources18
Beta strandi352 – 354Combined sources3
Turni356 – 359Combined sources4
Beta strandi360 – 364Combined sources5
Helixi366 – 368Combined sources3
Helixi369 – 377Combined sources9
Helixi384 – 392Combined sources9
Beta strandi393 – 395Combined sources3
Beta strandi400 – 403Combined sources4
Beta strandi409 – 411Combined sources3
Helixi414 – 441Combined sources28
Beta strandi450 – 457Combined sources8
Beta strandi465 – 467Combined sources3
Helixi469 – 489Combined sources21
Helixi492 – 499Combined sources8
Helixi513 – 520Combined sources8
Turni522 – 524Combined sources3
Helixi526 – 535Combined sources10
Beta strandi536 – 538Combined sources3
Helixi541 – 551Combined sources11
Turni552 – 554Combined sources3
Beta strandi556 – 559Combined sources4
Helixi561 – 563Combined sources3
Beta strandi564 – 566Combined sources3
Helixi567 – 569Combined sources3
Beta strandi576 – 582Combined sources7
Beta strandi585 – 590Combined sources6
Helixi594 – 597Combined sources4
Helixi604 – 611Combined sources8
Helixi616 – 621Combined sources6
Helixi624 – 629Combined sources6
Helixi634 – 638Combined sources5
Helixi644 – 660Combined sources17
Beta strandi662 – 670Combined sources9
Helixi683 – 692Combined sources10
Helixi695 – 702Combined sources8
Beta strandi704 – 706Combined sources3
Beta strandi707 – 711Combined sources5
Helixi712 – 719Combined sources8
Helixi720 – 722Combined sources3
Helixi725 – 728Combined sources4
Helixi732 – 742Combined sources11
Helixi747 – 749Combined sources3
Beta strandi750 – 752Combined sources3
Beta strandi754 – 759Combined sources6
Helixi764 – 771Combined sources8
Helixi775 – 788Combined sources14
Beta strandi818 – 820Combined sources3
Turni822 – 825Combined sources4
Helixi867 – 886Combined sources20
Helixi893 – 913Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ29122.
SMRiQ29122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29122.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini57 – 772Myosin motorAdd BLAST716
Domaini814 – 843IQAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni273 – 317Responsible for slow ATPase activityAdd BLAST45
Regioni666 – 673Actin-bindingSequence analysis8
Regioni783 – 811Required for binding calmodulinAdd BLAST29
Regioni836 – 917Three-helix bundle1 PublicationAdd BLAST82
Regioni918 – 985SAHBy similarityAdd BLAST68
Regioni1085 – 1087Interaction with OPTN3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi921 – 1028Glu-richAdd BLAST108

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. Its contribution to the mechanism confering the myosin movement on actin filaments is debated.By similarity1 Publication

Sequence similaritiesi

Contains 1 IQ domain.Curated
Contains 1 myosin motor domain.Curated

Phylogenomic databases

eggNOGiKOG0163. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000007806.
HOVERGENiHBG003523.
InParanoidiQ29122.
KOiK10358.

Family and domain databases

InterProiIPR032412. 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.
PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q29122-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDGKPVWAP HPTDGFQVGN IVDIGPDSLT IEPLNQKGKT FLALINQVFP
60 70 80 90 100
AEEDSKKDVE DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY
110 120 130 140 150
FDIPKIYSSE TIKSYQGKSL GTMPPHVFAI ADKAFRDMKV LKLSQSIIVS
160 170 180 190 200
GESGAGKTEN TKFVLRYLTE SYGTGQDIDD RIVEANPLLE AFGNAKTVRN
210 220 230 240 250
NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK EERNYHIFYR
260 270 280 290 300
LCAGASEDIR ERLHLSSPDN FRYLNRGCTR YFANKETDKQ ILQNRKSPEY
310 320 330 340 350
LKAGSLKDPL LDDHGDFIRM CTAMKKIGLD DEEKLDLFRV VAGVLHLGNI
360 370 380 390 400
DFEEAGSTSG GCNLKNKSTQ ALEYCAEKLL GLDQDDLRVS LTTRVMLTTA
410 420 430 440 450
GGAKGTVIKV PLKVEQANNA RDALAKTVYS HLFDHVVNRV NQCFPFETSS
460 470 480 490 500
YFIGVLDIAG FEYFEHNSFE QFCINYCNEK LQQFFNERIL KEEQELYQKE
510 520 530 540 550
GLGVNEVHYV DNQDCIDLIE ARLVGILDIL DEENRLPQPS DQHFTSAGHQ
560 570 580 590 600
KHKDHFRLSI PRKSKLAIHR NIAYDEGFII RHFAGAVCYE TTQFVEKNND
610 620 630 640 650
ALHMSLESLI CESRDKFIRE LFESSTNNNK DTKQKAGKLS FISVGNKFKT
660 670 680 690 700
QLNLLLDKLR STGASFIRCI KPNLKMTSHH FEGAQILSQL QCSGMVSVLD
710 720 730 740 750
LMQGGFPSRA SFHEVYNMYK KSLPDKLARL DPRLFCKALF KALGLNEIDY
760 770 780 790 800
KFGLTKVFFR PGKFAEFDQI MKSDPDHLAE LVKRVNHWLI CSRWKKVQWC
810 820 830 840 850
SLSVIKLKNK IKYRAEACIK MQKTIRMWLC KRRHKPRIDG LVKVGTLKKR
860 870 880 890 900
LDKFNEVVSA LKDGKQEMSK QVKDLEISID ALMAKIKSTM MTREQIQKEY
910 920 930 940 950
DALVKSSAVL LSALQKKKQQ EEEAERLRRI QEEMEKERKR REEDEQRRRK
960 970 980 990 1000
EEEERRMKLE MEAKRKQEEE ERKKREDDEK RIQAEVEAQL ARQREEESQQ
1010 1020 1030 1040 1050
QAVLEQERRD RELALRIAQS EAELISDEAQ ADPGLRRGPA VQATKAAAGT
1060 1070 1080 1090 1100
KKYDLSKWKY AELRDTINTS CDIELLAACR EEFHRRLKVY HAWKSKNKKR
1110 1120 1130 1140 1150
NTETEQRAPK SVTDYAQQNP AVQLPARQQE IEMNRQQRFF RIPFIRSADQ
1160 1170 1180 1190 1200
YKDPQNKKKG WWYAHFDGPW IARQMELHPD KPPILLVAGK DDMEMCELNL
1210 1220 1230 1240 1250
EETGLTRKRG AEILPRQFEE IWERCGGIQY LQNAIESRQA RPTYATAMLQ

NLLK
Length:1,254
Mass (Da):144,859
Last modified:November 1, 1996 - v1
Checksum:i0A72C1A7991CF763
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
Z35331 mRNA. Translation: CAA84559.1.
PIRiA54818.
RefSeqiNP_999186.1. NM_214021.1.
UniGeneiSsc.94.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ29122.
SMRiQ29122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1149220. 2 interactors.
DIPiDIP-48994N.
STRINGi9823.ENSSSCP00000004831.

PTM databases

iPTMnetiQ29122.

Proteomic databases

PaxDbiQ29122.
PeptideAtlasiQ29122.
PRIDEiQ29122.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397085.
KEGGissc:397085.

Organism-specific databases

CTDi4646.

Phylogenomic databases

eggNOGiKOG0163. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000007806.
HOVERGENiHBG003523.
InParanoidiQ29122.
KOiK10358.

Miscellaneous databases

EvolutionaryTraceiQ29122.

Family and domain databases

InterProiIPR032412. 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.
PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 115 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

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

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.