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P10745

- RET3_HUMAN

UniProt

P10745 - RET3_HUMAN

Protein

Retinol-binding protein 3

Gene

RBP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. retinal binding Source: UniProtKB-KW
    2. retinoid binding Source: ProtInc
    3. retinol binding Source: Ensembl
    4. serine-type peptidase activity Source: InterPro

    GO - Biological processi

    1. lipid metabolic process Source: ProtInc
    2. phototransduction, visible light Source: Reactome
    3. retinoid metabolic process Source: Reactome
    4. transport Source: UniProtKB-KW
    5. visual perception Source: ProtInc

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Vitamin A

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000107618-MONOMER.
    ReactomeiREACT_160083. The retinoid cycle in cones (daylight vision).
    REACT_160156. The canonical retinoid cycle in rods (twilight vision).

    Protein family/group databases

    MEROPSiS41.950.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinol-binding protein 3
    Alternative name(s):
    Interphotoreceptor retinoid-binding protein
    Short name:
    IRBP
    Interstitial retinol-binding protein
    Gene namesi
    Name:RBP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9921. RBP3.

    Subcellular locationi

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

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB
    3. interphotoreceptor matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1080 – 10801D → N in RP66; abolishes secretion; results in mis-folded insoluble complexes degraded via the ER-associated protein catabolic process. 1 Publication
    VAR_069706

    Keywords - Diseasei

    Disease mutation, Retinitis pigmentosa

    Organism-specific databases

    MIMi615233. phenotype.
    Orphaneti791. Retinitis pigmentosa.
    PharmGKBiPA34288.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 12471230Retinol-binding protein 3PRO_0000021523Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP10745.
    PRIDEiP10745.

    PTM databases

    PhosphoSiteiP10745.

    Expressioni

    Gene expression databases

    BgeeiP10745.
    CleanExiHS_RBP3.
    GenevestigatoriP10745.

    Interactioni

    Protein-protein interaction databases

    BioGridi111883. 1 interaction.
    STRINGi9606.ENSP00000224600.

    Structurei

    3D structure databases

    ProteinModelPortaliP10745.
    SMRiP10745. Positions 24-326, 329-1230.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati18 – 3203031Add
    BLAST
    Repeati321 – 6303102Add
    BLAST
    Repeati631 – 9313013Add
    BLAST
    Repeati932 – 12302994Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 123012134 X approximate tandem repeatsAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S41A family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG76669.
    HOGENOMiHOG000139907.
    HOVERGENiHBG006175.
    InParanoidiP10745.
    OMAiCSYFFDE.
    OrthoDBiEOG7MPRD1.
    PhylomeDBiP10745.
    TreeFamiTF332253.

    Family and domain databases

    Gene3Di3.90.226.10. 4 hits.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR005151. Tail-specific_protease.
    [Graphical view]
    PfamiPF03572. Peptidase_S41. 4 hits.
    [Graphical view]
    SMARTiSM00245. TSPc. 4 hits.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 4 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P10745-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMREWVLLMS VLLCGLAGPT HLFQPSLVLD MAKVLLDNYC FPENLLGMQE     50
    AIQQAIKSHE ILSISDPQTL ASVLTAGVQS SLNDPRLVIS YEPSTPEPPP 100
    QVPALTSLSE EELLAWLQRG LRHEVLEGNV GYLRVDSVPG QEVLSMMGEF 150
    LVAHVWGNLM GTSALVLDLR HCTGGQVSGI PYIISYLHPG NTILHVDTIY 200
    NRPSNTTTEI WTLPQVLGER YGADKDVVVL TSSQTRGVAE DIAHILKQMR 250
    RAIVVGERTG GGALDLRKLR IGESDFFFTV PVSRSLGPLG GGSQTWEGSG 300
    VLPCVGTPAE QALEKALAIL TLRSALPGVV HCLQEVLKDY YTLVDRVPTL 350
    LQHLASMDFS TVVSEEDLVT KLNAGLQAAS EDPRLLVRAI GPTETPSWPA 400
    PDAAAEDSPG VAPELPEDEA IRQALVDSVF QVSVLPGNVG YLRFDSFADA 450
    SVLGVLAPYV LRQVWEPLQD TEHLIMDLRH NPGGPSSAVP LLLSYFQGPE 500
    AGPVHLFTTY DRRTNITQEH FSHMELPGPR YSTQRGVYLL TSHRTATAAE 550
    EFAFLMQSLG WATLVGEITA GNLLHTRTVP LLDTPEGSLA LTVPVLTFID 600
    NHGEAWLGGG VVPDAIVLAE EALDKAQEVL EFHQSLGALV EGTGHLLEAH 650
    YARPEVVGQT SALLRAKLAQ GAYRTAVDLE SLASQLTADL QEVSGDHRLL 700
    VFHSPGELVV EEAPPPPPAV PSPEELTYLI EALFKTEVLP GQLGYLRFDA 750
    MAELETVKAV GPQLVRLVWQ QLVDTAALVI DLRYNPGSYS TAIPLLCSYF 800
    FEAEPRQHLY SVFDRATSKV TEVWTLPQVA GQRYGSHKDL YILMSHTSGS 850
    AAEAFAHTMQ DLQRATVIGE PTAGGALSVG IYQVGSSPLY ASMPTQMAMS 900
    ATTGKAWDLA GVEPDITVPM SEALSIAQDI VALRAKVPTV LQTAGKLVAD 950
    NYASAELGAK MATKLSGLQS RYSRVTSEVA LAEILGADLQ MLSGDPHLKA 1000
    AHIPENAKDR IPGIVPMQIP SPEVFEELIK FSFHTNVLED NIGYLRFDMF 1050
    GDGELLTQVS RLLVEHIWKK IMHTDAMIID MRFNIGGPTS SIPILCSYFF 1100
    DEGPPVLLDK IYSRPDDSVS ELWTHAQVVG ERYGSKKSMV ILTSSVTAGT 1150
    AEEFTYIMKR LGRALVIGEV TSGGCQPPQT YHVDDTNLYL TIPTARSVGA 1200
    SDGSSWEGVG VTPHVVVPAE EALARAKEML QHNQLRVKRS PGLQDHL 1247
    Length:1,247
    Mass (Da):135,363
    Last modified:November 1, 1991 - v2
    Checksum:i6C1841411E012E0F
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti757 – 7571V → G in BAJ84061. (PubMed:21697133)Curated
    Sequence conflicti757 – 7571V → G in AAH39844. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181G → V.1 Publication
    VAR_069669
    Natural varianti122 – 1221R → H.1 Publication
    VAR_069670
    Natural varianti155 – 1551V → M.1 Publication
    VAR_069671
    Natural varianti163 – 1631S → P.1 Publication
    VAR_069672
    Natural varianti196 – 1961V → M.1 Publication
    VAR_069673
    Natural varianti267 – 2671R → Q.1 Publication
    VAR_069674
    Natural varianti282 – 2821V → M.1 Publication
    VAR_069675
    Natural varianti321 – 3211T → I.1 Publication
    VAR_069676
    Natural varianti325 – 3251A → T.1 Publication
    VAR_069677
    Natural varianti346 – 3461R → H.1 Publication
    VAR_069678
    Natural varianti379 – 3791A → T.1 Publication
    VAR_069679
    Natural varianti433 – 4331S → L.1 Publication
    VAR_069680
    Natural varianti443 – 4431R → S.1 Publication
    VAR_069681
    Natural varianti505 – 5051H → L.1 Publication
    VAR_069682
    Natural varianti518 – 5181Q → R.1 Publication
    VAR_069683
    Natural varianti523 – 5231H → Q.1 Publication
    VAR_069684
    Natural varianti530 – 5301R → H in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035929
    Natural varianti535 – 5351R → C.1 Publication
    VAR_069685
    Natural varianti544 – 5441R → H.1 Publication
    VAR_069686
    Natural varianti593 – 5931V → A.1 Publication
    VAR_069687
    Natural varianti599 – 5991I → V.1 Publication
    VAR_069688
    Natural varianti614 – 6141D → N.1 Publication
    VAR_069689
    Natural varianti615 – 6151A → V.1 Publication
    VAR_069690
    Natural varianti675 – 6751T → I.1 Publication
    VAR_069691
    Natural varianti688 – 6881A → V.1 Publication
    VAR_069692
    Natural varianti693 – 6931V → M.1 Publication
    VAR_069693
    Natural varianti723 – 7231P → L.1 Publication
    VAR_069694
    Natural varianti741 – 7411G → S.1 Publication
    VAR_069695
    Natural varianti747 – 7471R → C.1 Publication
    VAR_069696
    Natural varianti785 – 7851N → K.1 Publication
    VAR_069697
    Natural varianti833 – 8331R → C.1 Publication
    VAR_069698
    Natural varianti835 – 8351G → S.1 Publication
    VAR_069699
    Natural varianti884 – 8841V → M.1 Publication
    Corresponds to variant rs11204213 [ dbSNP | Ensembl ].
    VAR_051315
    Natural varianti903 – 9031T → R.1 Publication
    VAR_069700
    Natural varianti921 – 9211S → R.1 Publication
    VAR_069701
    Natural varianti956 – 9561E → K.1 Publication
    VAR_069702
    Natural varianti963 – 9631T → I.1 Publication
    VAR_069703
    Natural varianti1021 – 10211S → Y.1 Publication
    VAR_069704
    Natural varianti1059 – 10591V → I.1 Publication
    VAR_069705
    Natural varianti1080 – 10801D → N in RP66; abolishes secretion; results in mis-folded insoluble complexes degraded via the ER-associated protein catabolic process. 1 Publication
    VAR_069706
    Natural varianti1194 – 11941T → M.1 Publication
    VAR_069707

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33875
    , 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.
    CCDSiCCDS7218.1.
    PIRiA33812.
    RefSeqiNP_002891.1. NM_002900.2.
    UniGeneiHs.591928.

    Genome annotation databases

    EnsembliENST00000584701; ENSP00000463151; ENSG00000265203.
    GeneIDi5949.
    KEGGihsa:5949.
    UCSCiuc001jez.3. human.

    Polymorphism databases

    DMDMi124894.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33875
    , 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 .
    CCDSi CCDS7218.1.
    PIRi A33812.
    RefSeqi NP_002891.1. NM_002900.2.
    UniGenei Hs.591928.

    3D structure databases

    ProteinModelPortali P10745.
    SMRi P10745. Positions 24-326, 329-1230.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111883. 1 interaction.
    STRINGi 9606.ENSP00000224600.

    Chemistry

    BindingDBi P10745.
    DrugBanki DB00162. Vitamin A.

    Protein family/group databases

    MEROPSi S41.950.

    PTM databases

    PhosphoSitei P10745.

    Polymorphism databases

    DMDMi 124894.

    Proteomic databases

    PaxDbi P10745.
    PRIDEi P10745.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000584701 ; ENSP00000463151 ; ENSG00000265203 .
    GeneIDi 5949.
    KEGGi hsa:5949.
    UCSCi uc001jez.3. human.

    Organism-specific databases

    CTDi 5949.
    GeneCardsi GC10M048381.
    GeneReviewsi RBP3.
    HGNCi HGNC:9921. RBP3.
    MIMi 180290. gene.
    615233. phenotype.
    neXtProti NX_P10745.
    Orphaneti 791. Retinitis pigmentosa.
    PharmGKBi PA34288.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG76669.
    HOGENOMi HOG000139907.
    HOVERGENi HBG006175.
    InParanoidi P10745.
    OMAi CSYFFDE.
    OrthoDBi EOG7MPRD1.
    PhylomeDBi P10745.
    TreeFami TF332253.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000107618-MONOMER.
    Reactomei REACT_160083. The retinoid cycle in cones (daylight vision).
    REACT_160156. The canonical retinoid cycle in rods (twilight vision).

    Miscellaneous databases

    GeneWikii RBP3.
    GenomeRNAii 5949.
    NextBioi 23178.
    PROi P10745.
    SOURCEi Search...

    Gene expression databases

    Bgeei P10745.
    CleanExi HS_RBP3.
    Genevestigatori P10745.

    Family and domain databases

    Gene3Di 3.90.226.10. 4 hits.
    InterProi IPR029045. ClpP/crotonase-like_dom.
    IPR005151. Tail-specific_protease.
    [Graphical view ]
    Pfami PF03572. Peptidase_S41. 4 hits.
    [Graphical view ]
    SMARTi SM00245. TSPc. 4 hits.
    [Graphical view ]
    SUPFAMi SSF52096. SSF52096. 4 hits.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiRET3_HUMAN
    AccessioniPrimary (citable) accession number: P10745
    Secondary accession number(s): Q0QD34, Q5VSR0, Q8IXN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Caution

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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3