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
0MEFV_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionPyrin (marenostrin).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005875 microtubule associated complex (IDA)
0005634 nucleus (IDA)
0003779 actin binding (IDA)
0008270 zinc ion binding (NAS)
0006954 inflammatory response (IDA)

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 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
Pyrin domain was identified as putative proteinprotein interaction domain at the N-terminal region of several proteins thought to function in apoptotic and inflammatory signaling pathways. Using secondary structure prediction and potential-based fold recognition methods.he PYRIN domain is predicted to be a member of the six-helix bundle death domain-fold superfamily that includes death domains (DDs).eath effector domains (DEDs).nd caspase recruitment domains (CARDs). Members of the death domain-fold superfamily are well established mediators of proteinprotein interactions found in many proteins involved in apoptosis and inflammation.ndicating further that the PYRIN domains serve a similar function. Comparison of a circular dichroism spectrum of the PYRIN domain of CARD7/DEFCAP/NAC/NALP1 with spectra of several proteins known to adopt the death domain-fold provides experimental support for the structure prediction. It is found in interferon-inducible proteins.yrin and myeloid cell nuclear differentiation antigen.
PRY is a domain associated with SPRY domains. The SPRY domain () is of unknown function however distant homologues are domains in butyrophilin/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).The proteins identified by the PRY domain.learly fall into 3 sets which can be defined by their combination of signatures:This group contains an immunoglobulin domain N-terminal to the PRY and butyrophilin domains. Butyrophilins are glycoproteins that are expressed on the apical surfaces of secretory cells in lactating mammary tissue and which may function in the secretion of milk-fat droplets.This group contain a RING-finger domain N-terminal to the PRY domain. The RING-finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc.nd is probably involved in mediating protein-protein interactions. There are two different variants.he C3HC4-type and a C3H2C3-type.hich is clearly related despite the different cysteine/histidine pattern. The latter type is sometimes referred to as RING-H2 finger is not found associated with this group of proteins. This set of proteins are described as TRIM (TRIpartite Motif) family members and are involved in cellular compartmentalisation . The TRIM family sequences are defined by a Ring finger domain. B-box type1 (B1) and a B-box type 2 (B2) followed by a coiled-coil (CC) region . Genes belonging to this family are implicated in a variety of processes such as development and cell growth and are involved in human disease. Many of these proteins.f not all of those with the PRY domain have a number of C-terminal signatures.PRY.FP-like (B30.2) and butyrophilin domain. The B30.2-like domain is a well conserved C-terminal domain of 160-170 amino acids which is found in nuclear and cytoplasmic proteins.s well as transmembrane and secreted proteins. The function of the B30.2-like domain is not known.ut the cytoplasmic B30.2-like domain of butyrophilin has been shown to interact with xanthine oxidase .The third set of proteins have the C-terminal signatures but have no N-terminal RING-finger or immunoglobulin domain signatures. These proteins have not been functionally described.
The B-box zinc finger is an around 40 amino acids domain. One or two copies ofthis motif are generally associated with a ring finger and a coiled coil motifto form the so-called tripartite motif. It is found essentially intranscription factors.ibonucleoproteins and protooncoproteins.ut nofunction is clearly assigned to this domain . It has been shown to beessential but not sufficient to localize the PML protein in a punctate patternin interphase nuclei . Among the 7 possible ligands for the zinc atomcontained in a B-box.nly 4 are used and bind one zinc atom in a Cys2-His2tetrahedral arrangement. The NMR analysis reveals that the B-box structurecomprises two beta-strands.wo helical turns and three extended loop regionsdifferent from any other zinc binding motif .
  IPR000315:Zinc finger, B-box
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) .
SequencesProtein: MEFV_HUMAN (781 aa)
mRNA: NM_000243
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)
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 556 residues, 3232028-3233695Exon2: 13 residues, 3233860-3233893Exon3: 13 residues, 3234254-3234287Exon4: 40 residues, 3234473-3234589Exon5: 9 residues, 3236525-3236548Exon6: 79 residues, 3237016-3237247Exon7: 34 residues, 3238909-3239005Exon8: 118 residues, 3239431-3239781Exon9: 213 residues, 3244158-3244791Exon10: 107 residues, 3246311-3246628Exon11: 2 residues, -Jump to MEFV_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2919 3036682-3050723 ~-14K 13385(MMP25)(+)Loci: 4203 3232028-3246628 ~-15K 13403(MEFV)(-)Loci: 2920 3273487-3281456 ~-8K 13405(ZNF263)(+)Loci: 4204 3571183-3601586 ~-30K 13423(BTBD12)(-)Loci: 4205 3648039-3707514 ~-59K 13426(TRAP1)(-)Loci: 4206 3717719-3870723 ~-153K 13429(CREBBP)(-)Loci: 4202 2962794-2970475 ~-8K 13372(PKMYT1)(-)Link out to UCSC