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0APOD_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameAPOD
DescriptionApolipoprotein d precursor (apo-d) (apod).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005615 extracellular space (TAS)
0005319 lipid transporter activity (TAS)
0005515 protein binding (IPI)
0006629 lipid metabolism (TAS)

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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:
Proteins which transport small hydrophobic molecules such as steroids.ilins.etinoids.nd lipids share limitedregions of sequence homology and a common tertiary structure architecture . This is an eight stranded antiparallel beta-barrel with a repeated + 1 topology enclosinga internal ligand binding site . The name lipocalin has been proposed forthis protein family.ut cytosolic fatty-acid binding proteins are also included. The sequences of most members of the family.he core or kernal lipocalins.re characterized bythree short conserved stretches of residues.hile others.he outlier lipocalin group.hare only one or two of these. Proteins known to belong to this family include alpha-1-microglobulin (protein HC);alpha-1-acid glycoprotein (orosomucoid) ; aphrodisin; apolipoprotein D; beta-lactoglobulin; complementcomponent C8 gamma chain ; crustacyanin ; epididymal-retinoic acid binding protein(E-RABP) ; insectacyanin; odorant-binding protein (OBP); human pregnancy-associated endometrial alpha-2globulin; probasin (PB). rat prostatic protein; prostaglandin D synthase () ; purpurin; VonEbners gland protein (VEGP) ; and lizard epididymal secretory protein IV (LESP IV) .Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen.tings.rugs.r food) that.n most people.esult in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P..offmann D..oewenstein H..arsh D.G..latts-Mills T.A.E..homas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed ofthe first three letters of the genus; a space; the first letter of thespecies name; a space and an arabic number. In the event that two speciesnames have identical designations.hey are discriminated from one anotherby adding one or more letters (as necessary) to each species designation. The allergens in this family include allergens with the following designations: Bla g 4.os d 2.os d 5.an f 1.an f 2.qu c 1 and Equ c 2.
  IPR000566:Lipocalin-related protein and Bos/Can/Equ allergen
The lipocalins are a diverse.nteresting.et poorly understood family of proteins composed.n the main.f extracellular ligand-binding proteinsdisplaying high specificity for small hydrophobic molecules . Functionsof these proteins include transport of nutrients.ontrol of cell regulation.heromone transport.ryptic colouration.nd the enzymatic synthesisof prostaglandins.The crystal structures of several lipocalins have been solved and show a novel 8-stranded anti-parallel beta-barrel fold well conserved within thefamily. Sequence similarity within the family is at a much lower level andwould seem to be restricted to conserved disulphides and 3 motifs.hichform a juxtaposed cluster that may act as a common cell surface receptorsite . By contrast.t the more variable end of the fold are found an internal ligand binding site and a putative surface for the formation of macromolecular complexes . The anti-parallel beta-barrel fold is alsoexploited by the fatty acid-binding proteins.hich function similarly bybinding small hydrophobic molecules. Similarity at the sequence level.owever.s less obvious.eing confined to a single short N-terminal motif.
  IPR002345:Lipocalin
The outlier lipocalins form several smaller distinct subgroups: the OBPs.he von Ebners gland proteins.lpha-1-acid glycoproteins.ick histamine binding proteins and the nitrophorins.Apolipoprotein D (apoD) is a mammalian plasma protein. Although well characterised.ts precise biological function remains unclear. The majority of apoD constitutes a minor but significant protein component of high density lipoprotein particles (HDLs).epresenting about 5% of total HDL protein.nd that its interaction with other apolipoproteins is of considerableimportance . By contrast with most apolipoproteins.uman apoD is relatively small (189 residues.W 18500). ApoD is 18% glycosylated.teither or both of two asparagines (positions 65 and 98 ). Human apoD is distributed in a number of tissues.ncluding kidney.iver.ancreas.pleen.ntestine.lacenta.drenal gland and foetal brain tissue . There is some evidence that the expression of apoD is regulated by steroidhormones . ApoD is found in a number of mammalian species.ncluding humans and other primates.ats.abbits and goats.ut it is absent from pigs.ogs.ows andhorses. The gene sequences of human.at and rabbit apoD are of similar length and are well conserved.Analysis of the human sequence revealed that apoD is a lipocalin family member showing the greatest apparent similarity to insect colourant proteins.The expected 8-membered beta-barrel structure of ApoD contrasts with the structure of other apoliproteins. Apoliprotein A is a modular protein knownto be composed of several kringle domains.hilst apolipoprotein E and apophorin E are helix bundles. Membership of the lipocalin family suggests apoD may function by binding ahydrophobic ligand; the nature of this molecule remains uncertain.lthoughcholesterol.ilin.rogesterone and pregnenolone have all been suggested.Almost all apoD in plasma is found as part of a supramolecular complex. It is localised primarily in an HDL.ith most of the remainder in very high density lipoprotein (VHDL) particles.nd only trace amounts in low density lipoprotein (LDL) and very low density lipoprotein (VLDL) particles. TheapoD protein contains two distinct antigenic sites.hich are apparently shared by other.igher molecular weight plasma proteins .
  IPR002969:Apolipoprotein D
Calycins form a large protein superfamily that share similar beta-barrel structures. Calycins can be divided into families that include lipocalins.atty acid binding proteins.riabin.nd thrombin inhibitor . Of these families.he lipocalin family () is the largest and functionally the most diverse. Lipocalins are extracellular proteins that share several common recognition properties such as ligand binding.eceptor binding and the formation of complexes with other macromolecules. Lipocalins include the retinol binding protein.ipocalin allergen.phrodisin (a sex hormone).lpha-2U-globulin.rostaglandin D synthase.eta-lactoglobulin.ilin-binding protein.nd the nitrophorins .This entry represents calycin as well as some other proteins that share a similar calycin beta-barrel structure.ncluding two bacterial hypothetical proteins YodA from Escherichia coli and YwiB from bacillus subtilis. Part of the YodA hypothetical protein has a calycin-like structure .Please be aware that some of the protein hits may be false positives.
  IPR011038:Calycin-like
Calycins form a large protein superfamily that share similar beta-barrel structures. Calycins can be divided into families that include lipocalins.atty acid binding proteins.riabin.nd thrombin inhibitor . Of these families.he lipocalin family () is the largest and functionally the most diverse. Lipocalins are extracellular proteins that share several common recognition properties such as ligand binding.eceptor binding and the formation of complexes with other macromolecules. Lipocalins include the retinol binding protein.ipocalin allergen.phrodisin (a sex hormone).lpha-2U-globulin.rostaglandin D synthase.eta-lactoglobulin.ilin-binding protein.nd the nitrophorins .
  IPR012674:Calycin
IPR000566:Lipocalin 
Evalue:-13.3767509460449 
Location:43-184IPR002969:APOLIPOPROTD 
Evalue:0 
Location:20-34
SequencesProtein: APOD_HUMAN (189 aa)
mRNA: NM_001647
Local Annotation
Synapse Ontology
Microglias, one kind of glias in CNS, are responsible for removing most of the waste and cellular debris from the CNS
sdb:0267 removing metabolic mass  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 144 residues, 196776866-196777295Exon2: 31 residues, 196779436-196779525Exon3: 42 residues, 196782009-196782131Exon4: 54 residues, 196787498-196787655Exon5: 82 residues, 196792037-196792278Exon6: 2 residues, -Jump to APOD_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4655 197074632-197120277 ~-46K 27086(TNK2)(-)Loci: 4656 197260746-197293338 ~-33K 27090(TFRC)(-)Loci: 4654 196776866-196792278 ~-15K 27071(APOD)(-)Link out to UCSC