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P10745

- RET3_HUMAN

UniProt

P10745 - RET3_HUMAN

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Protein
Retinol-binding protein 3
Gene
RBP3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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. 2 Publications
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 Publication
Add
BLAST
Chaini18 – 12471230Retinol-binding protein 3
PRO_0000021523Add
BLAST

Amino acid modifications

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

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.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the peptidase S41A family.

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.

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. 2 Publications
VAR_069706
Natural varianti1194 – 11941T → M.1 Publication
VAR_069707

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti757 – 7571V → G in BAJ84061. 1 Publication
Sequence conflicti757 – 7571V → G in AAH39844. 1 Publication

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

EnsembliENST00000224600; ENSP00000224600; ENSG00000107618.
ENST00000584701; 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 ENST00000224600 ; ENSP00000224600 ; ENSG00000107618 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 131 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.

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

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