SynDB Home Page
SynDB Home Page

blue bulletSynDB protein details  

Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0MYO7A_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionMyosin-7a (myosin viia).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0000146 microfilament motor activity (NAS)
0030048 actin filament-based movement (NAS)
0007605 perception of sound (TAS)
0007601 visual perception (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/ [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The microtubule-based kinesin motors and actin-based myosin motors generate movements required for intracellular trafficking.ell division.nd muscle contraction. In general.hese proteins consist of a motor domain that generates movement and a tail region that varies widely from class to class and is thought to mediate many of the regulatory or cargo binding functions specific to each class of motor . The Myosin Tail Homology 4 (MyTH4) domain has been identified as a conserved domain in the tail domains of several different unconventional myosins and a plant kinesin-like protein .ut has more recently been found in several non-motor proteins . Although the function is not yet fully is an evidence that the MyTH4 domain of Myosin-X (Myo10) binds to microtubules and thus could provide a link between an actin-based motor protein and the microtubule cytoskeleton .The MyTH4 domain is found in one or two copies associatedwith other domains.uch as myosin head.inesin motor.ERM.H.H3 and IQ. The domain is predicted to be largely alpha-helical.nterrupted by three orfour turns. The MyTH4 domain contains four highly conserved regions designatedMGD (consensus sequence L(K/R)(F/Y)MGDhP.RDE (consensus LRDEhYCQhhKQHxxxN).GW (consensus RGWxLh).nd ELEA (RxxPPSxhELEA).here h indicates ahydrophobic residue and x is any residue .
  IPR000857:Unconventional myosin/plant kinesin-like protein/non-motor protein conserved region MyTH4
This domain is found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. It is a conserved N-terminal domain of about 150 residues .nvolved in the linkage of cytoplasmic proteins to the membrane.
  IPR000299:Band 4.1
SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues . They are found in a great variety of intracellular or membrane-associated proteins for example.n a variety of proteins with enzymatic activity.n adaptor proteins that lack catalytic sequences and in cytoskeletal proteins.uch as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices . The surface of the SH2-domain bears a flat.ydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions.The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins.ltering their subcellular location and mediating the assembly of large multiprotein complexes .
  IPR001452:Src homology-3
Calmodulin (CaM) is recognized as a major calcium sensor and orchestrator of regulatory events through its interaction with a diverse group of cellular proteins. Three classes of recognition motifs exist for many of the known CaM binding proteins; the IQ motif as a consensus for Ca2+-independent binding and two related motifs for Ca2+-dependent binding.ermed18-14 and 1-5-10 based on the position of conserved hydrophobic residues .The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca2+-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains.ccounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule .
  IPR000048:IQ calmodulin-binding region
Muscle contraction is caused by sliding between the thick and thin filaments of the myofibril. Myosin is a major component of thick filaments and exists as a hexamer of 2 heavy chains . alkali light chains.nd 2 regulatory light chains. The heavy chain can be subdivided into the N-terminal globular head and the C-terminal coiled-coil rod-like tail.lthough some forms have a globular region in their C-terminal. There are many cell-specific isoforms of myosin heavy chains.oded for by a multi-gene family . Myosin interacts with actin to convert chemical energy.n the form of ATP.o mechanical energy . The 3-D structure of the head portion of myosin has been determined and a model for actin-myosin complex has been constructed .The globular head is well conserved.ome highly-conserved regions possibly relating to functional and structural domains . The rod-like tail starts with an invariant proline residue.nd contains many repeats of a 28 residue region.nterrupted at 4 regularly-spaced points known as skip residues. Although the sequence of the tail is not well conserved.he chemical character is.ydrophobic.harged and skip residues occuring in a highly ordered and repeated fashion .
  IPR001609:Myosin head, motor region
FERM domains (band F ezrin-radixin-moesin homology domains) are a common membrane-binding module involved in localising proteins to the plasma membrane . Proteins containing a FERM domain include cytoskeletal proteins such as erythrocyte membrane protein 4.1R.alin.nd the ezrin-radixin-moesin protein family.s well as several protein tyrosine kinases and phosphatases.nd the neurofibromatosis 2 tumour suppressor protein merlin. The ezrin-radixin-moesin protein family function to crosslink the actin filaments of cytoskeletal structures to the plasma membrane.
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
SequencesProtein: MYO7A_HUMAN (2215 aa)
mRNA: NM_000260
Local Annotation
Synapse Ontology
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 76 residues, 76516957-76517183Exon2: 23 residues, 76519282-76519346Exon3: 40 residues, 76531402-76531516Exon4: 53 residues, 76536491-76536644Exon5: 63 residues, 76544600-76544785Exon6: 42 residues, 76545353-76545475Exon7: 49 residues, 76545555-76545698Exon8: 40 residues, 76545972-76546086Exon9: 53 residues, 76546970-76547124Exon10: 27 residues, 76548140-76548217Exon11: 42 residues, 76548856-76548976Exon12: 49 residues, 76549666-76549809Exon13: 72 residues, 76550813-76551024Exon14: 47 residues, 76551546-76551682Exon15: 37 residues, 76554749-76554856Exon16: 48 residues, 76561441-76561579Exon17: 55 residues, 76563449-76563608Exon18: 33 residues, 76564065-76564158Exon19: 33 residues, 76566242-76566337Exon20: 30 residues, 76567738-76567823Exon21: 75 residues, 76568428-76568647Exon22: 38 residues, 76569067-76569175Exon23: 72 residues, 76570073-76570283Exon24: 70 residues, 76570644-76570848Exon25: 61 residues, 76571116-76571293Exon26: 32 residues, 76571760-76571850Exon27: 44 residues, 76573280-76573408Exon28: 44 residues, 76578036-76578163Exon29: 42 residues, 76578712-76578832Exon30: 60 residues, 76579389-76579563Exon31: 78 residues, 76580743-76580971Exon32: 59 residues, 76583046-76583217Exon33: 41 residues, 76586173-76586291Exon34: 44 residues, 76587187-76587314Exon35: 96 residues, 76588227-76588511Exon36: 65 residues, 76590140-76590331Exon37: 43 residues, 76590992-76591117Exon38: 54 residues, 76591752-76591910Exon39: 53 residues, 76592768-76592922Exon40: 54 residues, 76594154-76594310Exon41: 37 residues, 76594789-76594895Exon42: 40 residues, 76595981-76596095Exon43: 31 residues, 76597122-76597210Exon44: 37 residues, 76597389-76597496Exon45: 64 residues, 76599844-76600030Exon46: 41 residues, 76600513-76600630Exon47: 30 residues, 76601644-76601728Exon48: 42 residues, 76602552-76602672Exon49: 212 residues, 76603299-76603931Exon50: 2 residues, -Jump to MYO7A_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2694 76516957-76603931 ~-87K 7455(MYO7A)(+)Loci: 2693 76455639-76514844 ~-59K 7451(CAPN5)(+)Link out to UCSC