OBP odorant binding protein [Sus scrofa (pig)] - Gene

Summary

Gene symbol: OBP
Gene description: odorant binding protein
See related: Ensembl:ENSSSCG00000012095
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Sus scrofa
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus
Annotation information: Annotation category: partial on reference assembly
Expression: Low expression observed in reference dataset See more
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Genomic context

Location:: chromosome: X, chromosome: Y

Exon count:: 6

Annotation release	Status	Assembly	Chr	Location
106	current	Sscrofa11.1 (GCF_000003025.6)	X	NC_010461.5 (2012066..2019074)
106	current	Sscrofa11.1 (GCF_000003025.6)	Y	NC_010462.3 (1145927..1179835)
105	previous assembly	Sscrofa10.2 (GCF_000003025.5)	X	NC_010461.4 (1958110..1965119)

Chromosome X - NC_010461.5 Genomic Context describing neighboring genes

Chromosome Y - NC_010462.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Transcriptome data used for gene annotation Transcriptome data used for gene annotation
Description: Nine kinds of tissues and a mixture of multiple tissues were sequenced for genome annotation
BioProject: PRJNA311523
Publication: PMID 27646534
Analysis date: Thu Dec 14 17:10:49 2017

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

the role of phosphorylation in the binding capacities of OBP isoforms
Title: Binding specificity of recombinant odorant-binding protein isoforms is driven by phosphorylation.
The experimental results indicated that both Phe 35 & Tyr 82 are involved in the uptake of ligand as 3 mutated proteins were unable to bind 1-AMA, contrary to the wild type recombinant pOBP that bound 1-AMA with the expected affinity.
Title: Phenylalanine 35 and tyrosine 82 are involved in the uptake and release of ligand by porcine odorant-binding protein.
determionation of structural properties of OBP by mass spectrometry experiments; data allow us to hypothesize that specific deamidation mechanisms of specific amino acid residues can be responsible for the binding properties of this class of proteins
Title: Is asparagine deamidation in the porcine odorant-binding protein related to the odor molecules binding?
Data indicate that OBPs bind several aromatic polycyclic compounds with good affinities, that the specificity of these proteins can be easily modified by changing specific amino acid residues.
Title: Binding of polycyclic aromatic hydrocarbons to mutants of odorant-binding protein: a first step towards biosensors for environmental monitoring.
the amino acid residues that contribute to the protein dynamics and stability; the important role of ion pair interactions as well as the molecular motifs that are responsible for the high thermal stability; reasons for aggregation at high temperature
Title: Hydrophobic interactions and ionic networks play an important role in thermal stability and denaturation mechanism of the porcine odorant-binding protein.
Odorant-binding protein is very stable to the denaturing action of GdnHCl.
Title: Stability and dynamics of the porcine odorant-binding protein.
the important role played by the disulphide bridge on the stability and function of this protein
Title: Role of the disulphide bridge in folding, stability and function of porcine odorant binding protein: spectroscopic equilibrium studies on C63A/C155A double mutant.
involvement in the detection of appeasing compounds in the nasal mucosa and the vomeronasal organ of pre-pubertal pigs
Title: Functional characterization of olfactory binding proteins for appeasing compounds and molecular cloning in the vomeronasal organ of pre-pubertal pigs.
Lipocalin strand pair opening in the presence of ligand is observed, consistent with potential role in olfactive receptor recognition.
Title: Odorant binding and conformational dynamics in the odorant-binding protein.

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General gene information

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Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables odorant binding	IEA Inferred from Electronic Annotation more info	PubMed
enables small molecule binding	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
located_in extracellular space	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: odorant-binding protein

Names: lipocaline

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.