RBP3: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +))
 
imported>BD2412
m (→‎Application: clean up from page move, replaced: taxonomic → taxonomic using AWB)
 
(One intermediate revision by one other user not shown)
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Retinol-binding protein 3, interstitial''' ('''RBP3'''), also known as '''IRBP''' is a [[protein]] that in humans is encoded by the ''RBP3'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RBP3 retinol binding protein 3, interstitial| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5949| accessdate = }}</ref>  RBP3 [[orthologs]] <ref name="OrthoMaM">{{cite web | title = OrthoMaM phylogenetic marker: RBP3 gene, exon 1| url = http://www.orthomam.univ-montp2.fr/orthomam/data/exons/detailMarkers/ENSG00000107618_RBP3_000.xml }}</ref> have been identified in most [[eutherians]] except [[tenrecs]] and [[armadillos]].
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Retinol binding protein 3, interstitial
| HGNCid = 9921
| Symbol = RBP3
| AltSymbols =; IRBP; D10S64; D10S65; D10S66; RBPI
| OMIM = 180290
| ECnumber = 
| Homologene = 9261
| MGIid = 97878
| GeneAtlas_image1 = PBB_GE_RBP3_210318_at_tn.png
| Function = {{GNF_GO|id=GO:0005504 |text = fatty acid binding}} {{GNF_GO|id=GO:0008236 |text = serine-type peptidase activity}} {{GNF_GO|id=GO:0016918 |text = retinal binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007601 |text = visual perception}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5949
    | Hs_Ensembl = ENSG00000107618
    | Hs_RefseqProtein = NP_002891
    | Hs_RefseqmRNA = NM_002900
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 48001493
    | Hs_GenLoc_end = 48010997
    | Hs_Uniprot = P10745
    | Mm_EntrezGene = 19661
    | Mm_Ensembl = ENSMUSG00000041534
    | Mm_RefseqmRNA = NM_015745
    | Mm_RefseqProtein = NP_056560
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 32783114
    | Mm_GenLoc_end = 32793308
    | Mm_Uniprot = P49194
  }}
}}
'''Retinol binding protein 3, interstitial''', also known as '''RBP3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RBP3 retinol binding protein 3, interstitial| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5949| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The inter-[[Photoreceptor cell|photoreceptor]] [[retinoid]]-binding protein is a large [[glycoprotein]] known to bind retinoids and found primarily in the [[interphotoreceptor matrix]] of the retina between the retinal pigment epithelium and the photoreceptor cells. It is thought to transport retinoids between the retinal pigment epithelium and the photoreceptors, a critical role in the visual process.
{{PBB_Summary
| section_title =
| summary_text = Interphotoreceptor retinol-binding protein is a large glycoprotein known to bind retinoids and found primarily in the interphotoreceptor matrix of the retina between the retinal pigment epithelium and the photoreceptor cells. It is thought to transport retinoids between the retinal pigment epithelium and the photoreceptors, a critical role in the visual process.The human IRBP gene is approximately 9.5 kbp in length and consists of four exons separated by three introns. The introns are 1.6-1.9 kbp long. The gene is transcribed by photoreceptor and retinoblastoma cells into an approximately 4.3-kilobase mRNA that is translated and processed into a glycosylated protein of 135,000 Da. The amino acid sequence of human IRBP can be divided into four contiguous homology domains with 33-38% identity, suggesting a series of gene duplication events. In the gene, the boundaries of these domains are not defined by exon-intron junctions, as might have been expected. The first three homology domains and part of the fourth are all encoded by the first large exon, which is 3,180 base pairs long. The remainder of the fourth domain is encoded in the last three exons, which are 191, 143, and approximately 740 base pairs long, respectively.<ref name="entrez">{{cite web | title = Entrez Gene: RBP3 retinol binding protein 3, interstitial| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5949| accessdate = }}</ref>
}}


==References==
== Gene ==
{{reflist|2}}
 
==Further reading==
The human IRBP gene is approximately 9.5 kbp in length and consists of four [[exons]] separated by three [[introns]]. The introns are 1.6-1.9 kbp long. The gene is transcribed by photoreceptor and retinoblastoma cells into an approximately 4.3-kilobase mRNA that is translated and processed into a glycosylated protein of 135,000 Da.
{{refbegin | 2}}
 
{{PBB_Further_reading
== Structure ==
| citations =
 
*{{cite journal  | author=Fong SL, Fong WB, Morris TA, ''et al.'' |title=Characterization and comparative structural features of the gene for human interstitial retinol-binding protein. |journal=J. Biol. Chem. |volume=265 |issue= 7 |pages= 3648-53 |year= 1990 |pmid= 2303470 |doi= }}
The amino acid sequence of human IRBP can be divided into four contiguous [[homology (biology)|homology]] domains with 33-38% identity, suggesting a series of gene duplication events. In the gene, the boundaries of these domains are not defined by exon-intron junctions, as might have been expected. The first three homology domains and part of the fourth are all encoded by the first large exon, which is 3,180 base pairs long. The remainder of the fourth domain is encoded in the last three exons, which are 191, 143, and approximately 740 base pairs long, respectively.<ref name="entrez"/>
*{{cite journal  | author=Albini A, Toffenetti J, Zhu Z, ''et al.'' |title=Hypomethylation of the interphotoreceptor retinoid-binding protein (IRBP) promotor and first exon is linked to expression of the gene. |journal=Nucleic Acids Res. |volume=18 |issue= 17 |pages= 5181-7 |year= 1990 |pmid= 2402443 |doi= }}
 
*{{cite journal  | author=Liou GI, Ma DP, Yang YW, ''et al.'' |title=Human interstitial retinoid-binding protein. Gene structure and primary structure. |journal=J. Biol. Chem. |volume=264 |issue= 14 |pages= 8200-6 |year= 1989 |pmid= 2542268 |doi=  }}
== Application ==
*{{cite journal  | author=Si JS, Borst DE, Redmond TM, Nickerson JM |title=Cloning of cDNAs encoding human interphotoreceptor retinoid-binding protein (IRBP) and comparison with bovine IRBP sequences. |journal=Gene |volume=80 |issue= 1 |pages= 99-108 |year= 1989 |pmid= 2792773 |doi= }}
 
*{{cite journal | author=Nakamura Y, Lathrop M, Bragg T, ''et al.'' |title=An extended genetic linkage map of markers for human chromosome 10. |journal=Genomics |volume=3 |issue= 4 |pages= 389-92 |year= 1989 |pmid= 2907505 |doi= }}
The '''''rbp3''''' gene is commonly used in animals as a [[nuclear DNA]] phylogenetic marker.<ref name="OrthoMaM"/> The exon 1 has first been used in a pioneer study to provide evidence for [[monophyly]] of [[Chiroptera]].<ref name="pmid1342928">{{cite journal | vauthors = Stanhope MJ, Czelusniak J, Si JS, Nickerson J, Goodman M | title = A molecular perspective on mammalian evolution from the gene encoding interphotoreceptor retinoid binding protein, with convincing evidence for bat monophyly | journal = Molecular Phylogenetics and Evolution | volume = 1 | issue = 2 | pages = 148–60 | date = Jun 1992 | pmid = 1342928 | doi = 10.1016/1055-7903(92)90026-D }}</ref> Then, it has been used to infer the [[phylogeny]] of  [[placental]] [[mammal]] orders,<ref name="pmid8660440">{{cite journal | vauthors = Stanhope MJ, Smith MR, Waddell VG, Porter CA, Shivji MS, Goodman M | title = Mammalian evolution and the interphotoreceptor retinoid binding protein (IRBP) gene: convincing evidence for several superordinal clades | journal = Journal of Molecular Evolution | volume = 43 | issue = 2 | pages = 83–92 | date = Aug 1996 | pmid = 8660440 | doi = 10.1007/BF02337352 }}</ref><ref name="pmid11214318">{{cite journal | vauthors = Madsen O, Scally M, Douady CJ, Kao DJ, DeBry RW, Adkins R, Amrine HM, Stanhope MJ, de Jong WW, Springer MS | title = Parallel adaptive radiations in two major clades of placental mammals | journal = Nature | volume = 409 | issue = 6820 | pages = 610–4 | date = Feb 2001 | pmid = 11214318 | doi = 10.1038/35054544 }}</ref> and of the major [[clades]] of [[Rodent]]ia,<ref name="pmid12082125">{{cite journal | vauthors = Huchon D, Madsen O, Sibbald MJ, Ament K, Stanhope MJ, Catzeflis F, de Jong WW, Douzery EJ | title = Rodent phylogeny and a timescale for the evolution of Glires: evidence from an extensive taxon sampling using three nuclear genes | journal = Molecular Biology and Evolution | volume = 19 | issue = 7 | pages = 1053–65 | date = Jul 2002 | pmid = 12082125 | doi = 10.1093/oxfordjournals.molbev.a004164 }}</ref> [[Macroscelidea]],<ref name="pmid12821774">{{cite journal | vauthors = Douady CJ, Catzeflis F, Raman J, Springer MS, Stanhope MJ | title = The Sahara as a vicariant agent, and the role of Miocene climatic events, in the diversification of the mammalian order Macroscelidea (elephant shrews) | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 100 | issue = 14 | pages = 8325–30 | date = Jul 2003 | pmid = 12821774 | pmc = 166228 | doi = 10.1073/pnas.0832467100 }}</ref> and [[Primates]].<ref name="pmid15085543">{{cite journal | vauthors = Poux C, Douzery EJ | title = Primate phylogeny, evolutionary rate variations, and divergence times: a contribution from the nuclear gene IRBP | journal = American Journal of Physical Anthropology | volume = 124 | issue = 1 | pages = 1–16 | date = May 2004 | pmid = 15085543 | doi = 10.1002/ajpa.10322 }}</ref> RBP3 is also useful at lower [[Taxonomy (biology)|taxonomic]] levels, ''e.g.'', in muroid rodents<ref name="pmid15019624">{{cite journal | vauthors = Jansa SA, Weksler M | title = Phylogeny of muroid rodents: relationships within and among major lineages as determined by IRBP gene sequences | journal = Molecular Phylogenetics and Evolution | volume = 31 | issue = 1 | pages = 256–76 | date = Apr 2004 | pmid = 15019624 | doi = 10.1016/j.ympev.2003.07.002 }}</ref> and Malagasy primates,<ref name="pmid18245770">{{cite journal | vauthors = Horvath JE, Weisrock DW, Embry SL, Fiorentino I, Balhoff JP, Kappeler P, Wray GA, Willard HF, Yoder AD | title = Development and application of a phylogenomic toolkit: resolving the evolutionary history of Madagascar's lemurs | journal = Genome Research | volume = 18 | issue = 3 | pages = 489–99 | date = Mar 2008 | pmid = 18245770 | pmc = 2259113 | doi = 10.1101/gr.7265208 }}</ref> at the [[phylogeography]] level in ''Geomys'' and ''Apodemus'' rodents,<ref>{{cite journal | vauthors = Genoways HH, Hamilton MJ, Bell DM, Chambers RR, Bradley RD | year = 2008 | title = Hybrid zones, genetic isolation, and systematics of pocket gophers (genus ''Geomys'') in Nebraska | url = | journal = J. Mammal. | volume = 89 | issue = | pages = 826–836 | doi=10.1644/07-mamm-a-408.1}}</ref><ref name="pmid18393564">{{cite journal | vauthors = Tomozawa M, Suzuki H | title = A trend of central versus peripheral structuring in mitochondrial and nuclear gene sequences of the Japanese wood mouse, Apodemus speciosus | journal = Zoological Science | volume = 25 | issue = 3 | pages = 273–85 | date = Mar 2008 | pmid = 18393564 | doi = 10.2108/zsj.25.273 }}</ref> and even for [[carnivora]] species identification purposes.<ref name ="Oliveira_2009">{{cite journal | vauthors = Oliveira R, Castro D, Godinho R, Luikart G, Alves PC | title = Species identification using a small nuclear gene: application to sympatric wild carnivores from South-western Europe | journal = Conserv. Genet. | volume = 11| issue = 3| pages = 1023–1032|date=June 2009 | pmid = | doi = 10.1007/s10592-009-9947-4 | url = | issn = }}</ref>
*{{cite journal | author=Fong SL, Bridges CD |title=Internal quadruplication in the structure of human interstitial retinol-binding protein deduced from its cloned cDNA. |journal=J. Biol. Chem. |volume=263 |issue= 30 |pages= 15330-4 |year= 1988 |pmid= 3170584 |doi= }}
 
*{{cite journal | author=Liou GI, Fong SL, Gosden J, ''et al.'' |title=Human interstitial retinol-binding protein (IRBP): cloning, partial sequence, and chromosomal localization. |journal=Somat. Cell Mol. Genet. |volume=13 |issue= 4 |pages= 315-23 |year= 1988 |pmid= 3455009 |doi= }}
Note that the RBP3 intron 1 has also been used to investigate the [[platyrrhine]] primates phylogenetics.<ref name="pmid8771309">{{cite journal | vauthors = Schneider H, Sampaio I, Harada ML, Barroso CM, Schneider MP, Czelusniak J, Goodman M | title = Molecular phylogeny of the New World monkeys (Platyrrhini, primates) based on two unlinked nuclear genes: IRBP intron 1 and epsilon-globin sequences | journal = American Journal of Physical Anthropology | volume = 100 | issue = 2 | pages = 153–79 | date = Jun 1996 | pmid = 8771309 | doi = 10.1002/(SICI)1096-8644(199606)100:2<153::AID-AJPA1>3.0.CO;2-Z }}</ref>
*{{cite journal | author=Fong SL, Cook RG, Alvarez RA, ''et al.'' |title=N-terminal sequence homologies in interstitial retinol-binding proteins from 10 vertebrate species. |journal=FEBS Lett. |volume=205 |issue= 2 |pages= 309-12 |year= 1986 |pmid= 3743780 |doi= }}
 
*{{cite journal | author=Redmond TM, Wiggert B, Robey FA, Chader GJ |title=Interspecies conservation of structure of interphotoreceptor retinoid-binding protein. Similarities and differences as adjudged by peptide mapping and N-terminal sequencing. |journal=Biochem. J. |volume=240 |issue= 1 |pages= 19-26 |year= 1987 |pmid= 3827838 |doi= }}
== References ==
*{{cite journal | author=Chen Y, Houghton LA, Brenna JT, Noy N |title=Docosahexaenoic acid modulates the interactions of the interphotoreceptor retinoid-binding protein with 11-cis-retinal. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20507-15 |year= 1996 |pmid= 8702792 |doi= }}
{{reflist|33em}}
*{{cite journal | author=Shaw NS, Noy N |title=Interphotoreceptor retinoid-binding protein contains three retinoid binding sites. |journal=Exp. Eye Res. |volume=72 |issue= 2 |pages= 183-90 |year= 2001 |pmid= 11161734 |doi= 10.1006/exer.2000.0945 }}
 
*{{cite journal | author=Foltz DR, Nye JS |title=Hyperphosphorylation and association with RBP of the intracellular domain of Notch1. |journal=Biochem. Biophys. Res. Commun. |volume=286 |issue= 3 |pages= 484-92 |year= 2001 |pmid= 11511084 |doi= 10.1006/bbrc.2001.5421 }}
== Further reading ==
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
{{refbegin|33em}}
*{{cite journal | author=Howard OM, Dong HF, Su SB, ''et al.'' |title=Autoantigens signal through chemokine receptors: uveitis antigens induce CXCR3- and CXCR5-expressing lymphocytes and immature dendritic cells to migrate. |journal=Blood |volume=105 |issue= 11 |pages= 4207-14 |year= 2005 |pmid= 15713799 |doi= 10.1182/blood-2004-07-2697 }}
* {{cite journal | vauthors = Fong SL, Fong WB, Morris TA, Kedzie KM, Bridges CD | title = Characterization and comparative structural features of the gene for human interstitial retinol-binding protein | journal = The Journal of Biological Chemistry | volume = 265 | issue = 7 | pages = 3648–53 | date = Mar 1990 | pmid = 2303470 | doi =  }}
}}
* {{cite journal | vauthors = Albini A, Toffenetti J, Zhu Z, Chader GJ, Noonan DM | title = Hypomethylation of the interphotoreceptor retinoid-binding protein (IRBP) promotor and first exon is linked to expression of the gene | journal = Nucleic Acids Research | volume = 18 | issue = 17 | pages = 5181–7 | date = Sep 1990 | pmid = 2402443 | pmc = 332140 | doi = 10.1093/nar/18.17.5181 }}
* {{cite journal | vauthors = Liou GI, Ma DP, Yang YW, Geng L, Zhu C, Baehr W | title = Human interstitial retinoid-binding protein. Gene structure and primary structure | journal = The Journal of Biological Chemistry | volume = 264 | issue = 14 | pages = 8200–6 | date = May 1989 | pmid = 2542268 | doi =  }}
* {{cite journal | vauthors = Si JS, Borst DE, Redmond TM, Nickerson JM | title = Cloning of cDNAs encoding human interphotoreceptor retinoid-binding protein (IRBP) and comparison with bovine IRBP sequences | journal = Gene | volume = 80 | issue = 1 | pages = 99–108 | date = Aug 1989 | pmid = 2792773 | doi = 10.1016/0378-1119(89)90254-0 }}
* {{cite journal | vauthors = Nakamura Y, Lathrop M, Bragg T, Leppert M, O'Connell P, Jones C, Lalouel JM, White R | title = An extended genetic linkage map of markers for human chromosome 10 | journal = Genomics | volume = 3 | issue = 4 | pages = 389–92 | date = Nov 1988 | pmid = 2907505 | doi = 10.1016/0888-7543(88)90133-4 }}
* {{cite journal | vauthors = Fong SL, Bridges CD | title = Internal quadruplication in the structure of human interstitial retinol-binding protein deduced from its cloned cDNA | journal = The Journal of Biological Chemistry | volume = 263 | issue = 30 | pages = 15330–4 | date = Oct 1988 | pmid = 3170584 | doi =  }}
* {{cite journal | vauthors = Liou GI, Fong SL, Gosden J, van Tuinen P, Ledbetter DH, Christie S, Rout D, Bhattacharya S, Cook RG, Li Y | title = Human interstitial retinol-binding protein (IRBP): cloning, partial sequence, and chromosomal localization | journal = Somatic Cell and Molecular Genetics | volume = 13 | issue = 4 | pages = 315–23 | date = Jul 1987 | pmid = 3455009 | doi = 10.1007/BF01534925 }}
* {{cite journal | vauthors = Fong SL, Cook RG, Alvarez RA, Liou GI, Landers RA, Bridges CD | title = N-terminal sequence homologies in interstitial retinol-binding proteins from 10 vertebrate species | journal = FEBS Letters | volume = 205 | issue = 2 | pages = 309–12 | date = Sep 1986 | pmid = 3743780 | doi = 10.1016/0014-5793(86)80918-8 }}
* {{cite journal | vauthors = Redmond TM, Wiggert B, Robey FA, Chader GJ | title = Interspecies conservation of structure of interphotoreceptor retinoid-binding protein. Similarities and differences as adjudged by peptide mapping and N-terminal sequencing | journal = The Biochemical Journal | volume = 240 | issue = 1 | pages = 19–26 | date = Nov 1986 | pmid = 3827838 | pmc = 1147370 | doi =  10.1042/bj2400019}}
* {{cite journal | vauthors = Chen Y, Houghton LA, Brenna JT, Noy N | title = Docosahexaenoic acid modulates the interactions of the interphotoreceptor retinoid-binding protein with 11-cis-retinal | journal = The Journal of Biological Chemistry | volume = 271 | issue = 34 | pages = 20507–15 | date = Aug 1996 | pmid = 8702792 | doi = 10.1074/jbc.271.34.20507 }}
* {{cite journal | vauthors = Shaw NS, Noy N | title = Interphotoreceptor retinoid-binding protein contains three retinoid binding sites | journal = Experimental Eye Research | volume = 72 | issue = 2 | pages = 183–90 | date = Feb 2001 | pmid = 11161734 | doi = 10.1006/exer.2000.0945 }}
* {{cite journal | vauthors = Foltz DR, Nye JS | title = Hyperphosphorylation and association with RBP of the intracellular domain of Notch1 | journal = Biochemical and Biophysical Research Communications | volume = 286 | issue = 3 | pages = 484–92 | date = Aug 2001 | pmid = 11511084 | doi = 10.1006/bbrc.2001.5421 }}
* {{cite journal | vauthors = Howard OM, Dong HF, Su SB, Caspi RR, Chen X, Plotz P, Oppenheim JJ | title = Autoantigens signal through chemokine receptors: uveitis antigens induce CXCR3- and CXCR5-expressing lymphocytes and immature dendritic cells to migrate | journal = Blood | volume = 105 | issue = 11 | pages = 4207–14 | date = Jun 2005 | pmid = 15713799 | pmc = 1895027 | doi = 10.1182/blood-2004-07-2697 }}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* [https://www.ncbi.nlm.nih.gov/books/NBK1417/  GeneReviews/NCBI/NIH/UW entry on Retinitis Pigmentosa Overview]
* {{cite web | url = http://www.orthomam.univ-montp2.fr/orthomam/data/cds/detailMarkers/ENSG00000107618_RBP3.xml | title = Overview of the coding DNA and protein sequence alignments of the RBP3 marker | authorlink = | date = | format = | work = OrthoMaM – a [[biological database]] of [[orthologous]] mammalian markers | publisher = | pages = | archiveurl = | archivedate = | quote =  The rbp3 evolutionary marker can be found, together with the corresponding gene [[phylogeny]] | accessdate = }}

Latest revision as of 14:04, 23 July 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Retinol-binding protein 3, interstitial (RBP3), also known as IRBP is a protein that in humans is encoded by the RBP3 gene.[1] RBP3 orthologs [2] have been identified in most eutherians except tenrecs and armadillos.

Function

The inter-photoreceptor retinoid-binding protein is a large glycoprotein known to bind retinoids and found primarily in the interphotoreceptor matrix of the retina between the retinal pigment epithelium and the photoreceptor cells. It is thought to transport retinoids between the retinal pigment epithelium and the photoreceptors, a critical role in the visual process.

Gene

The human IRBP gene is approximately 9.5 kbp in length and consists of four exons separated by three introns. The introns are 1.6-1.9 kbp long. The gene is transcribed by photoreceptor and retinoblastoma cells into an approximately 4.3-kilobase mRNA that is translated and processed into a glycosylated protein of 135,000 Da.

Structure

The amino acid sequence of human IRBP can be divided into four contiguous homology domains with 33-38% identity, suggesting a series of gene duplication events. In the gene, the boundaries of these domains are not defined by exon-intron junctions, as might have been expected. The first three homology domains and part of the fourth are all encoded by the first large exon, which is 3,180 base pairs long. The remainder of the fourth domain is encoded in the last three exons, which are 191, 143, and approximately 740 base pairs long, respectively.[1]

Application

The rbp3 gene is commonly used in animals as a nuclear DNA phylogenetic marker.[2] The exon 1 has first been used in a pioneer study to provide evidence for monophyly of Chiroptera.[3] Then, it has been used to infer the phylogeny of placental mammal orders,[4][5] and of the major clades of Rodentia,[6] Macroscelidea,[7] and Primates.[8] RBP3 is also useful at lower taxonomic levels, e.g., in muroid rodents[9] and Malagasy primates,[10] at the phylogeography level in Geomys and Apodemus rodents,[11][12] and even for carnivora species identification purposes.[13]

Note that the RBP3 intron 1 has also been used to investigate the platyrrhine primates phylogenetics.[14]

References

  1. ↑ 1.0 1.1 "Entrez Gene: RBP3 retinol binding protein 3, interstitial".
  2. ↑ 2.0 2.1 "OrthoMaM phylogenetic marker: RBP3 gene, exon 1".
  3. ↑ Stanhope MJ, Czelusniak J, Si JS, Nickerson J, Goodman M (Jun 1992). "A molecular perspective on mammalian evolution from the gene encoding interphotoreceptor retinoid binding protein, with convincing evidence for bat monophyly". Molecular Phylogenetics and Evolution. 1 (2): 148–60. doi:10.1016/1055-7903(92)90026-D. PMID 1342928.
  4. ↑ Stanhope MJ, Smith MR, Waddell VG, Porter CA, Shivji MS, Goodman M (Aug 1996). "Mammalian evolution and the interphotoreceptor retinoid binding protein (IRBP) gene: convincing evidence for several superordinal clades". Journal of Molecular Evolution. 43 (2): 83–92. doi:10.1007/BF02337352. PMID 8660440.
  5. ↑ Madsen O, Scally M, Douady CJ, Kao DJ, DeBry RW, Adkins R, Amrine HM, Stanhope MJ, de Jong WW, Springer MS (Feb 2001). "Parallel adaptive radiations in two major clades of placental mammals". Nature. 409 (6820): 610–4. doi:10.1038/35054544. PMID 11214318.
  6. ↑ Huchon D, Madsen O, Sibbald MJ, Ament K, Stanhope MJ, Catzeflis F, de Jong WW, Douzery EJ (Jul 2002). "Rodent phylogeny and a timescale for the evolution of Glires: evidence from an extensive taxon sampling using three nuclear genes". Molecular Biology and Evolution. 19 (7): 1053–65. doi:10.1093/oxfordjournals.molbev.a004164. PMID 12082125.
  7. ↑ Douady CJ, Catzeflis F, Raman J, Springer MS, Stanhope MJ (Jul 2003). "The Sahara as a vicariant agent, and the role of Miocene climatic events, in the diversification of the mammalian order Macroscelidea (elephant shrews)". Proceedings of the National Academy of Sciences of the United States of America. 100 (14): 8325–30. doi:10.1073/pnas.0832467100. PMC 166228. PMID 12821774.
  8. ↑ Poux C, Douzery EJ (May 2004). "Primate phylogeny, evolutionary rate variations, and divergence times: a contribution from the nuclear gene IRBP". American Journal of Physical Anthropology. 124 (1): 1–16. doi:10.1002/ajpa.10322. PMID 15085543.
  9. ↑ Jansa SA, Weksler M (Apr 2004). "Phylogeny of muroid rodents: relationships within and among major lineages as determined by IRBP gene sequences". Molecular Phylogenetics and Evolution. 31 (1): 256–76. doi:10.1016/j.ympev.2003.07.002. PMID 15019624.
  10. ↑ Horvath JE, Weisrock DW, Embry SL, Fiorentino I, Balhoff JP, Kappeler P, Wray GA, Willard HF, Yoder AD (Mar 2008). "Development and application of a phylogenomic toolkit: resolving the evolutionary history of Madagascar's lemurs". Genome Research. 18 (3): 489–99. doi:10.1101/gr.7265208. PMC 2259113. PMID 18245770.
  11. ↑ Genoways HH, Hamilton MJ, Bell DM, Chambers RR, Bradley RD (2008). "Hybrid zones, genetic isolation, and systematics of pocket gophers (genus Geomys) in Nebraska". J. Mammal. 89: 826–836. doi:10.1644/07-mamm-a-408.1.
  12. ↑ Tomozawa M, Suzuki H (Mar 2008). "A trend of central versus peripheral structuring in mitochondrial and nuclear gene sequences of the Japanese wood mouse, Apodemus speciosus". Zoological Science. 25 (3): 273–85. doi:10.2108/zsj.25.273. PMID 18393564.
  13. ↑ Oliveira R, Castro D, Godinho R, Luikart G, Alves PC (June 2009). "Species identification using a small nuclear gene: application to sympatric wild carnivores from South-western Europe". Conserv. Genet. 11 (3): 1023–1032. doi:10.1007/s10592-009-9947-4.
  14. ↑ Schneider H, Sampaio I, Harada ML, Barroso CM, Schneider MP, Czelusniak J, Goodman M (Jun 1996). "Molecular phylogeny of the New World monkeys (Platyrrhini, primates) based on two unlinked nuclear genes: IRBP intron 1 and epsilon-globin sequences". American Journal of Physical Anthropology. 100 (2): 153–79. doi:10.1002/(SICI)1096-8644(199606)100:2<153::AID-AJPA1>3.0.CO;2-Z. PMID 8771309.

Further reading

External links

Retrieved from "https://www.wikidoc.org/index.php?title=RBP3&oldid=1527353"