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1Q9BTV5_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
DescriptionFibronectin type iii and spry domain containing 1 (microtubule- associated protein glfnd).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005622 intracellular (IEA)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The SPRY domain is of unknown function. Distant homologues are domains inbutyrophilin/marenostrin/pyrin .Ca2+-release from the sarcoplasmic or endoplasmic reticulum.he intracellular Ca2+ store.s mediated by the ryanodine receptor (RyR) and/or the inositol trisphosphate receptor (IP3R).
  IPR003877:SPla/RYanodine receptor SPRY
The B-box C-terminal domain is a coiled coil region C-terminal to (some) B-Box domains. It is found in transcription intermediary factor 1-alpha.hich associates with DNA-bound estrogen receptors; ring finger protein. putative transcriptional regulator; and the GTP-binding protein Ard-1.
  IPR003649:B-box, C-terminal
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003961:Fibronectin, type III
Several proteins that contain RING fingers also contain a well-conserved40-residue cysteine-rich domain termed a B-box zinc finger. or two copies of the B-box are associated with a coiled coil domain in additionto the ring finger.orming a tripartite motif. The tripartite motif is found in transcription factors.ibonucleoproteins and proto-oncoproteins.ut no function has yet been ascribed to the domain . The solution structure of the B-box motif has been determined by NMR. The protein is a monomer.ith 2 beta-strands. helical turns and 3extended loop regions packed in a novel topology . Of 7 potential zincligands.nly 4 are used.inding a single zinc atom in a C2-H2 tetrahedral arrangement. The B-box structure differs in tertiary fold from allother known zinc-binding motifs.A group of proteins that contain the B-box motif also host a well conserveddomain of unknown function (DUF). Proteins that include this domain are..g.: butyrophilin.he RET finger protein.he 52kDa Ro protein and theXenopus nuclear factor protein. The C-terminal portion of this region hasbeen termed the SPRY domain (after SPla and the RYanodine Receptor) .
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
SequencesProtein: Q9BTV5_HUMAN (496 aa)
mRNA: NM_024333
Local Annotation
Synapse Ontology
microtubules of the presynaptic compartment function as the tracks for the intense traffic of organelles from cell body to axon terminals and vice versa. It is generally excluded from the presynaptic vesicle cluster.Microtubules do not directly regulate synapse morphology or function
sdb:0087 microtubules  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 23 residues, 4255690-4255758Exon2: 34 residues, 4256942-4257038Exon3: 46 residues, 4257194-4257326Exon4: 36 residues, 4258878-4258980Exon5: 9 residues, 4261269-4261292Exon6: 42 residues, 4261471-4261593Exon7: 72 residues, 4262838-4263048Exon8: 35 residues, 4268178-4268277Exon9: 55 residues, 4269342-4269502Exon10: 28 residues, 4269868-4269948Exon11: 86 residues, 4273982-4274234Exon12: 31 residues, 4274344-4274433Exon13: 105 residues, 4274529-4274838Exon14: 2 residues, -Jump to Q9BTV5_HUMAN  
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Loci Cluster (Details)Loci: 4354 4311367-4351471 ~-40K 17708(SH3GL1)(-)Loci: 3081 4255690-4274838 ~-19K 17702(+)Link out to UCSC