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Protein

Unconventional myosin-VI

Gene

MYO6

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi151 – 158ATPSequence analysis8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Unconventional myosin-VI
Alternative name(s):
Unconventional myosin-6
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MYO6
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008227 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002717461 – 1254Unconventional myosin-VIAdd BLAST1254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei267PhosphoserineBy similarity1
Modified residuei406Phosphothreonine1 Publication1
Modified residuei605PhosphoserineBy similarity1
Modified residuei1026PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q29122

PeptideAtlas

More...
PeptideAtlasi
Q29122

PRoteomics IDEntifications database

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PRIDEi
Q29122

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q29122

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
1149220, 2 interactors

Database of interacting proteins

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DIPi
DIP-48994N

Protein interaction database and analysis system

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IntActi
Q29122, 2 interactors

STRING: functional protein association networks

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STRINGi
9823.ENSSSCP00000004831

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
5O2LX-ray2.20A5-790[»]
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[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q29122

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q29122

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q29122

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 53Myosin N-terminal SH3-likePROSITE-ProRule annotationAdd BLAST52
Domaini57 – 772Myosin motorPROSITE-ProRule annotationAdd BLAST716
Domaini814 – 843IQAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi921 – 1028Glu-richAdd BLAST108

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0163 Eukaryota
COG5022 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000007806

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG003523

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q29122

KEGG Orthology (KO)

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KOi
K10358

Database of Orthologous Groups

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OrthoDBi
122881at2759

Family and domain databases

Conserved Domains Database

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CDDi
cd01382 MYSc_Myo6, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.30.30.360, 1 hit
3.40.850.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

Pfam protein domain database

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Pfami
View protein in Pfam
PF16521 Myosin-VI_CBD, 1 hit
PF00063 Myosin_head, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00193 MYOSINHEAVY

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00242 MYSc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51456 MYOSIN_MOTOR, 1 hit
PS51844 SH3_LIKE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0A72C1A7991CF763
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
Z35331 mRNA Translation: CAA84559.1

Protein sequence database of the Protein Information Resource

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PIRi
A54818

NCBI Reference Sequences

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RefSeqi
NP_999186.1, NM_214021.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Ssc.94

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
397085

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:397085

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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[»]
5O2LX-ray2.20A5-790[»]
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

Comparative Toxicogenomics Database

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CTDi
4646

Phylogenomic databases

eggNOGiKOG0163 Eukaryota
COG5022 LUCA
HOGENOMiHOG000007806
HOVERGENiHBG003523
InParanoidiQ29122
KOiK10358
OrthoDBi122881at2759

Miscellaneous databases

EvolutionaryTraceiQ29122

Family and domain databases

CDDicd01382 MYSc_Myo6, 1 hit
Gene3Di2.30.30.360, 1 hit
3.40.850.10, 1 hit
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, 1 hit
PROSITEiView protein in PROSITE
PS51456 MYOSIN_MOTOR, 1 hit
PS51844 SH3_LIKE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMYO6_PIG
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q29122
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: January 16, 2019
This is version 129 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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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