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P10745 (RET3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinol-binding protein 3
Alternative name(s):
Interphotoreceptor retinoid-binding protein
Short name=IRBP
Interstitial retinol-binding protein
Gene names
Name:RBP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

IRBP shuttles 11-cis and all trans retinoids between the retinol isomerase in the pigment epithelium and the visual pigments in the photoreceptor cells of the retina.

Subcellular location

Secretedextracellular spaceextracellular matrixinterphotoreceptor matrix. Note: Interphotoreceptor matrix that permeates the space between the retina and the contiguous layer of pigment epithelium cells.

Involvement in disease

Retinitis pigmentosa 66 (RP66) [MIM:615233]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16

Sequence similarities

Belongs to the peptidase S41A family.

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.

Sequence caution

The sequence AAC18875.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.12
Chain18 – 12471230Retinol-binding protein 3
PRO_0000021523

Regions

Repeat18 – 3203031
Repeat321 – 6303102
Repeat631 – 9313013
Repeat932 – 12302994
Region18 – 123012134 X approximate tandem repeats

Amino acid modifications

Glycosylation2051N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential

Natural variations

Natural variant181G → V. Ref.15
VAR_069669
Natural variant1221R → H. Ref.15
VAR_069670
Natural variant1551V → M. Ref.15
VAR_069671
Natural variant1631S → P. Ref.15
VAR_069672
Natural variant1961V → M. Ref.15
VAR_069673
Natural variant2671R → Q. Ref.15
VAR_069674
Natural variant2821V → M. Ref.15
VAR_069675
Natural variant3211T → I. Ref.15
VAR_069676
Natural variant3251A → T. Ref.15
VAR_069677
Natural variant3461R → H. Ref.15
VAR_069678
Natural variant3791A → T. Ref.15
VAR_069679
Natural variant4331S → L. Ref.15
VAR_069680
Natural variant4431R → S. Ref.15
VAR_069681
Natural variant5051H → L. Ref.15
VAR_069682
Natural variant5181Q → R. Ref.15
VAR_069683
Natural variant5231H → Q. Ref.15
VAR_069684
Natural variant5301R → H in a colorectal cancer sample; somatic mutation. Ref.14
VAR_035929
Natural variant5351R → C. Ref.15
VAR_069685
Natural variant5441R → H. Ref.15
VAR_069686
Natural variant5931V → A. Ref.15
VAR_069687
Natural variant5991I → V. Ref.15
VAR_069688
Natural variant6141D → N. Ref.15
VAR_069689
Natural variant6151A → V. Ref.15
VAR_069690
Natural variant6751T → I. Ref.15
VAR_069691
Natural variant6881A → V. Ref.15
VAR_069692
Natural variant6931V → M. Ref.15
VAR_069693
Natural variant7231P → L. Ref.15
VAR_069694
Natural variant7411G → S. Ref.15
VAR_069695
Natural variant7471R → C. Ref.15
VAR_069696
Natural variant7851N → K. Ref.15
VAR_069697
Natural variant8331R → C. Ref.15
VAR_069698
Natural variant8351G → S. Ref.15
VAR_069699
Natural variant8841V → M. Ref.15
Corresponds to variant rs11204213 [ dbSNP | Ensembl ].
VAR_051315
Natural variant9031T → R. Ref.15
VAR_069700
Natural variant9211S → R. Ref.15
VAR_069701
Natural variant9561E → K. Ref.15
VAR_069702
Natural variant9631T → I. Ref.15
VAR_069703
Natural variant10211S → Y. Ref.15
VAR_069704
Natural variant10591V → I. Ref.15
VAR_069705
Natural variant10801D → N in RP66; abolishes secretion; results in mis-folded insoluble complexes degraded via the ER-associated protein catabolic process. Ref.15 Ref.16
VAR_069706
Natural variant11941T → M. Ref.15
VAR_069707

Experimental info

Sequence conflict7571V → G in BAJ84061. Ref.5
Sequence conflict7571V → G in AAH39844. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P10745 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: 6C1841411E012E0F

FASTA1,247135,363
        10         20         30         40         50         60 
MMREWVLLMS VLLCGLAGPT HLFQPSLVLD MAKVLLDNYC FPENLLGMQE AIQQAIKSHE 

        70         80         90        100        110        120 
ILSISDPQTL ASVLTAGVQS SLNDPRLVIS YEPSTPEPPP QVPALTSLSE EELLAWLQRG 

       130        140        150        160        170        180 
LRHEVLEGNV GYLRVDSVPG QEVLSMMGEF LVAHVWGNLM GTSALVLDLR HCTGGQVSGI 

       190        200        210        220        230        240 
PYIISYLHPG NTILHVDTIY NRPSNTTTEI WTLPQVLGER YGADKDVVVL TSSQTRGVAE 

       250        260        270        280        290        300 
DIAHILKQMR RAIVVGERTG GGALDLRKLR IGESDFFFTV PVSRSLGPLG GGSQTWEGSG 

       310        320        330        340        350        360 
VLPCVGTPAE QALEKALAIL TLRSALPGVV HCLQEVLKDY YTLVDRVPTL LQHLASMDFS 

       370        380        390        400        410        420 
TVVSEEDLVT KLNAGLQAAS EDPRLLVRAI GPTETPSWPA PDAAAEDSPG VAPELPEDEA 

       430        440        450        460        470        480 
IRQALVDSVF QVSVLPGNVG YLRFDSFADA SVLGVLAPYV LRQVWEPLQD TEHLIMDLRH 

       490        500        510        520        530        540 
NPGGPSSAVP LLLSYFQGPE AGPVHLFTTY DRRTNITQEH FSHMELPGPR YSTQRGVYLL 

       550        560        570        580        590        600 
TSHRTATAAE EFAFLMQSLG WATLVGEITA GNLLHTRTVP LLDTPEGSLA LTVPVLTFID 

       610        620        630        640        650        660 
NHGEAWLGGG VVPDAIVLAE EALDKAQEVL EFHQSLGALV EGTGHLLEAH YARPEVVGQT 

       670        680        690        700        710        720 
SALLRAKLAQ GAYRTAVDLE SLASQLTADL QEVSGDHRLL VFHSPGELVV EEAPPPPPAV 

       730        740        750        760        770        780 
PSPEELTYLI EALFKTEVLP GQLGYLRFDA MAELETVKAV GPQLVRLVWQ QLVDTAALVI 

       790        800        810        820        830        840 
DLRYNPGSYS TAIPLLCSYF FEAEPRQHLY SVFDRATSKV TEVWTLPQVA GQRYGSHKDL 

       850        860        870        880        890        900 
YILMSHTSGS AAEAFAHTMQ DLQRATVIGE PTAGGALSVG IYQVGSSPLY ASMPTQMAMS 

       910        920        930        940        950        960 
ATTGKAWDLA GVEPDITVPM SEALSIAQDI VALRAKVPTV LQTAGKLVAD NYASAELGAK 

       970        980        990       1000       1010       1020 
MATKLSGLQS RYSRVTSEVA LAEILGADLQ MLSGDPHLKA AHIPENAKDR IPGIVPMQIP 

      1030       1040       1050       1060       1070       1080 
SPEVFEELIK FSFHTNVLED NIGYLRFDMF GDGELLTQVS RLLVEHIWKK IMHTDAMIID 

      1090       1100       1110       1120       1130       1140 
MRFNIGGPTS SIPILCSYFF DEGPPVLLDK IYSRPDDSVS ELWTHAQVVG ERYGSKKSMV 

      1150       1160       1170       1180       1190       1200 
ILTSSVTAGT AEEFTYIMKR LGRALVIGEV TSGGCQPPQT YHVDDTNLYL TIPTARSVGA 

      1210       1220       1230       1240 
SDGSSWEGVG VTPHVVVPAE EALARAKEML QHNQLRVKRS PGLQDHL 

« Hide

References

« Hide 'large scale' references
[1]"Human interstitial retinoid-binding protein. Gene structure and primary structure."
Liou G.I., Ma D.-P., Yang Y.-W., Geng L., Zhu C., Baehr W.
J. Biol. Chem. 264:8200-8206(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization and comparative structural features of the gene for human interstitial retinol-binding protein."
Fong S.-L., Fong W.B., Morris T.A., Kedzie K.M., Bridges C.D.B.
J. Biol. Chem. 265:3648-3653(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"Cloning of cDNAs encoding human interphotoreceptor retinoid-binding protein (IRBP) and comparison with bovine IRBP sequences."
Si J.S., Borst D.E., Redmond T.M., Nickerson J.M.
Gene 80:99-108(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Internal quadruplication in the structure of human interstitial retinol-binding protein deduced from its cloned cDNA."
Fong S.-L., Bridges C.D.B.
J. Biol. Chem. 263:15330-15334(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[5]"Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Retinoblastoma.
[6]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[9]"Human interstitial retinol-binding protein (IRBP): cloning, partial sequence, and chromosomal localization."
Liou G.I., Fong S.-L., Gosden J., van Tuinen P., Ledbetter D.H., Christie S., Rout D., Bhattacharya S., Cook R.G., Li Y., Wang C., Bridges C.D.B.
Somat. Cell Mol. Genet. 13:315-323(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-1247.
[10]"Hypomethylation of the interphotoreceptor retinoid-binding protein (IRBP) promotor and first exon is linked to expression of the gene."
Albini A., Toffenetti J., Zhen Z., Chader G.J., Noonan D.M.
Nucleic Acids Res. 18:5181-5187(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-382.
[11]"Mapping of transcription start sites of human retina expressed genes."
Roni V., Carpio R., Wissinger B.
BMC Genomics 8:42-42(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-10.
Tissue: Retina.
[12]"Interspecies conservation of structure of interphotoreceptor retinoid-binding protein. Similarities and differences as adjudged by peptide mapping and N-terminal sequencing."
Redmond T.M., Wiggert B., Robey F.A., Chader G.J.
Biochem. J. 240:19-26(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-42.
[13]"N-terminal sequence homologies in interstitial retinol-binding proteins from 10 vertebrate species."
Fong S.-L., Cook R.G., Alvarez R.A., Liou G.I., Landers R.A., Bridges C.D.B.
FEBS Lett. 205:309-312(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-39.
[14]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-530.
[15]"A homozygous missense mutation in the IRBP gene (RBP3) associated with autosomal recessive retinitis pigmentosa."
den Hollander A.I., McGee T.L., Ziviello C., Banfi S., Dryja T.P., Gonzalez-Fernandez F., Ghosh D., Berson E.L.
Invest. Ophthalmol. Vis. Sci. 50:1864-1872(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP66 ASN-1080, VARIANTS VAL-18; HIS-122; MET-155; PRO-163; MET-196; GLN-267; MET-282; ILE-321; THR-325; HIS-346; THR-379; LEU-433; SER-443; LEU-505; ARG-518; GLN-523; CYS-535; HIS-544; ALA-593; VAL-599; ASN-614; VAL-615; ILE-675; VAL-688; MET-693; LEU-723; SER-741; CYS-747; LYS-785; CYS-833; SER-835; MET-884; ARG-903; ARG-921; LYS-956; ILE-963; TYR-1021; ILE-1059 AND MET-1194.
[16]"Secretory defect and cytotoxicity: the potential disease mechanisms for the retinitis pigmentosa (RP)-associated interphotoreceptor retinoid-binding protein (IRBP)."
Li S., Yang Z., Hu J., Gordon W.C., Bazan N.G., Haas A.L., Bok D., Jin M.
J. Biol. Chem. 288:11395-11406(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT RP66 ASN-1080.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33875 expand/collapse EMBL AC list , M33864, M33865, M33866 Genomic DNA. Translation: AAA59453.1.
M22453 mRNA. Translation: AAA36126.1.
J05253 Genomic DNA. Translation: AAC18875.1. Different initiation.
AB593121 mRNA. Translation: BAJ84061.1.
AL731561 Genomic DNA. Translation: CAH74045.1.
CH471251 Genomic DNA. Translation: EAW50659.1.
BC039844 mRNA. Translation: AAH39844.1.
J03912 mRNA. Translation: AAA59188.1.
X53044 Genomic DNA. Translation: CAA37213.1.
DQ426897 mRNA. Translation: ABD90548.1.
PIRA33812.
RefSeqNP_002891.1. NM_002900.2.
UniGeneHs.591928.

3D structure databases

ProteinModelPortalP10745.
SMRP10745. Positions 24-326, 329-1230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111883. 1 interaction.
STRING9606.ENSP00000224600.

Chemistry

BindingDBP10745.
DrugBankDB00162. Vitamin A.

Protein family/group databases

MEROPSS41.950.

PTM databases

PhosphoSiteP10745.

Polymorphism databases

DMDM124894.

Proteomic databases

PaxDbP10745.
PRIDEP10745.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000224600; ENSP00000224600; ENSG00000107618.
ENST00000584701; ENSP00000463151; ENSG00000265203.
GeneID5949.
KEGGhsa:5949.
UCSCuc001jez.3. human.

Organism-specific databases

CTD5949.
GeneCardsGC10M048381.
HGNCHGNC:9921. RBP3.
MIM180290. gene.
615233. phenotype.
neXtProtNX_P10745.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA34288.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG76669.
HOGENOMHOG000139907.
HOVERGENHBG006175.
InParanoidP10745.
OMACSYFFDE.
OrthoDBEOG7MPRD1.
PhylomeDBP10745.
TreeFamTF332253.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000107618-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

BgeeP10745.
CleanExHS_RBP3.
GenevestigatorP10745.

Family and domain databases

InterProIPR005151. Tail-specific_protease.
[Graphical view]
PfamPF03572. Peptidase_S41. 4 hits.
[Graphical view]
SMARTSM00245. TSPc. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRBP3.
GenomeRNAi5949.
NextBio23178.
PROP10745.
SOURCESearch...

Entry information

Entry nameRET3_HUMAN
AccessionPrimary (citable) accession number: P10745
Secondary accession number(s): Q0QD34, Q5VSR0, Q8IXN0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM