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Protein

Unconventional myosin-VI

Gene

MYO6

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -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

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

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

Keywordsi

Molecular functionActin-binding, Calmodulin-binding, Motor protein, Myosin
Biological processEndocytosis, Hearing, Protein transport, Transport
LigandATP-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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi1149220, 2 interactors
DIPiDIP-48994N
IntActiQ29122, 2 interactors
STRINGi9823.ENSSSCP00000004831

Structurei

Secondary structure

11254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ29122
SMRiQ29122
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29122

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 53Myosin N-terminal SH3-likePROSITE-ProRule annotationAdd BLAST52
Domaini57 – 772Myosin motorPROSITE-ProRule annotationAdd 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

Phylogenomic databases

eggNOGiKOG0163 Eukaryota
COG5022 LUCA
HOGENOMiHOG000007806
HOVERGENiHBG003523
InParanoidiQ29122
KOiK10358

Family and domain databases

CDDicd01382 MYSc_Myo6, 1 hit
Gene3Di2.30.30.360, 1 hit
3.40.850.10, 3 hits
InterProiView protein in InterPro
IPR036961 Kinesin_motor_dom_sf
IPR032412 Myosin-VI_CBD
IPR001609 Myosin_head_motor_dom
IPR004009 Myosin_N
IPR008989 Myosin_S1_N
IPR036114 MYSc_Myo6
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF16521 Myosin-VI_CBD, 1 hit
PF00063 Myosin_head, 1 hit
PRINTSiPR00193 MYOSINHEAVY
SMARTiView protein in SMART
SM00242 MYSc, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51456 MYOSIN_MOTOR, 1 hit
PS51844 SH3_LIKE, 1 hit

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

Similar proteinsi

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[»]
6BNPelectron microscopy4.60I/J/K/L/M/N2-706[»]
6BNQelectron microscopy5.50I/J/K/L/M/N2-706[»]
6BNVelectron microscopy4.60I/J/K/L/M/N2-818[»]
6BNWelectron microscopy5.50I/J/K/L/M/N2-818[»]
ProteinModelPortaliQ29122
SMRiQ29122
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1149220, 2 interactors
DIPiDIP-48994N
IntActiQ29122, 2 interactors
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

CDDicd01382 MYSc_Myo6, 1 hit
Gene3Di2.30.30.360, 1 hit
3.40.850.10, 3 hits
InterProiView protein in InterPro
IPR036961 Kinesin_motor_dom_sf
IPR032412 Myosin-VI_CBD
IPR001609 Myosin_head_motor_dom
IPR004009 Myosin_N
IPR008989 Myosin_S1_N
IPR036114 MYSc_Myo6
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF16521 Myosin-VI_CBD, 1 hit
PF00063 Myosin_head, 1 hit
PRINTSiPR00193 MYOSINHEAVY
SMARTiView protein in SMART
SM00242 MYSc, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51456 MYOSIN_MOTOR, 1 hit
PS51844 SH3_LIKE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMYO6_PIG
AccessioniPrimary (citable) accession number: Q29122
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: October 10, 2018
This is version 126 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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