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1Q6ZSR4_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionHypothetical protein flj45273.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005576 extracellular region (IEA)
0000151 ubiquitin ligase complex (IEA)
0004176 ATP-dependent peptidase activity (IEA)
0005488 binding (IEA)
0046872 metal ion binding (IEA)
0005185 neurohypophyseal hormone activity (IEA)
0004842 ubiquitin-protein ligase activity (IEA)
0008270 zinc ion binding (IEA)
0006510 ATP-dependent proteolysis (IEA)
0016567 protein ubiquitination (IEA)

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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:
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This signature defines the N-terminal domain of the archael.acterial and eukaryotic lon proteases.hich are ATP-dependent serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family.lan SF). In the eukaryotes the majority of the proteins are located in the mitochondrial matrix . In yeast.im1.s located in the mitochondrial matrix.s required for mitochondrial function.s constitutively expressed but is increased after thermal stress.uggesting that Pim1 may play a role in the heat shock response .
  IPR003111:Peptidase S16, lon N-terminal
Quality control of intracellular proteins is essential for cellular homeostasis. Molecular chaperones recognise and contribute to the refolding of misfolded or unfolded proteins.hereas the ubiquitin-proteasome system mediates the degradation of such abnormal proteins. Ubiquitin-protein ligases (E3s) determine the substrate specificity for ubiquitylation and have been classified into HECT and RING-finger families. More recently.owever.-box proteins.hich contain a domain (the U box) of about 70 amino acids that is conserved from yeast to humans.ave been identified as a new type of E3 .The RING-finger is a specialised 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. The RING domain is a protein interaction domain which has been implicated in a range of diverse biological processes.E3 ubiquitin-protein ligase activity is intrinsic to the RING domain ofc-Cbl and is likely to be a general function of this domain; Various RINGfingers exhibit binding to E2 ubiquitin-conjugating enzymes (Ubcs) .Several 3D-structures for RING-fingers are known . The 3D structure of the zinc ligation system is unique to the RING domain and is referred to as the cross-brace motif. The spacing of the cysteines in such a domain is C-x(2)-C-x(9 to 39)-C-x(1 to 3)-H-x(2 to 3)-C-x(2)-C-x(4 to 48)-C-x(2)-C. Metal ligand pairs one and three co-ordinate to bind one zinc ion.hilst pairs two and four bind the second.s illustrated in the following schematic representation:Note that in the older literature.ome RING-fingers are denoted as LIM-domains. The LIM-domain Zn-finger is a fundamentally different family.lbeit with similar Cys-spacing (see ).
  IPR001841:Zinc finger, RING-type
Oxytocin and vasopressin are nine-residue.tructurally and functionally related neurohypophysial peptide hormones. Oxytocin mediates contraction of the smooth muscle of the uterus and mammary gland.hile vasopressin has antidiuretic action on the kidney.nd mediates vasoconstriction of the peripheral vessels . In common with most active peptides.oth hormones are synthesised as larger protein precursors that are enzymatically converted to their mature forms. Members of this family are found in birds.ish.eptiles and amphibians (mesotocin.sotocin.alitocin.lumitocin.spargtocin.asotocin.eritocin.svatocin.hasvatocin).n worms (annetocin).ctopi (cephalotocin).ocust (locupressin or neuropeptideF1/F2) and in molluscs (conopressins G and S) .
  IPR000981:Neurohypophysial hormone
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix.here the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
IPR003111:LON 
Evalue:-6.49485015869141 
Location:287-495IPR001841:zf-C3HC4 
Evalue:-6.34678745269775 
Location:206-243IPR011990:TPR-like_helical 
Evalue:0 
Location:1-54
SequencesProtein: Q6ZSR4_HUMAN (511 aa)
mRNA: NM_198461
Local Annotation
Synapse Ontology
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)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 318 residues, 100266435-100267386Exon2: 52 residues, 100269807-100269957Exon3: 56 residues, 100273151-100273314Exon4: 55 residues, 100277122-100277281Exon5: 42 residues, 100278325-100278447Exon6: 40 residues, 100281729-100281844Exon7: 33 residues, 100282119-100282213Exon8: 69 residues, 100282610-100282812Exon9: 50 residues, 100283537-100283681Exon10: 43 residues, 100285814-100285937Exon11: 41 residues, 100292000-100292119Exon12: 9 residues, 100292378-100292399Exon13: 2 residues, -Jump to Q6ZSR4_HUMAN  
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