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P12271 (RLBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinaldehyde-binding protein 1
Alternative name(s):
Cellular retinaldehyde-binding protein
Gene names
Name:RLBP1
Synonyms:CRALBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Soluble retinoid carrier essential the proper function of both rod and cone photoreceptors. Participates in the regeneration of active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-trans products of the rhodopsin photocycle and in the de novo synthesis of these retinoids from 11-trans metabolic precursors. The cycling of retinoids between photoreceptor and adjacent pigment epithelium cells is known as the 'visual cycle'. Ref.8

Subcellular location

Cytoplasm.

Tissue specificity

Retina and pineal gland. Not present in photoreceptor cells but is expressed abundantly in the adjacent retinal pigment epithelium (RPE) and in the Mueller glial cells of the retina. Ref.8

Involvement in disease

Retinitis pigmentosa autosomal recessive (ARRP) [MIM:268000]: 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.9

Bothnia retinal dystrophy (BRD) [MIM:607475]: A type of retinitis punctata albescens. Affected individuals show night blindness from early childhood with features consistent with retinitis punctata albescens and macular degeneration.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Rod-cone dystrophy Newfoundland (NFRCD) [MIM:607476]: A rod-cone dystrophy reminiscent of retinitis punctata albescens but with a substantially lower age at onset and more-rapid and distinctive progression. Rod-cone dystrophies results from initial loss of rod photoreceptors, later followed by cone photoreceptors loss.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Retinitis punctata albescens (RPA) [MIM:136880]: Rare form of stationary night blindness characterized by a delay in the regeneration of cone and rod photopigments.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Contains 1 CRAL-TRIO domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 317316Retinaldehyde-binding protein 1
PRO_0000079330

Regions

Domain136 – 297162CRAL-TRIO

Sites

Binding site180111-cis-retinal
Binding site202111-cis-retinal

Amino acid modifications

Modified residue21N-acetylserine By similarity

Natural variations

Natural variant1511R → Q in ARRP; loss of ability to bind 11-cis-retinaldehyde. Ref.9
Corresponds to variant rs28933989 [ dbSNP | Ensembl ].
VAR_005140
Natural variant2261M → K in FA. Ref.11
VAR_037317
Natural variant2341R → W in BRD. Ref.8 Ref.10
Corresponds to variant rs28933990 [ dbSNP | Ensembl ].
VAR_015172

Secondary structure

.............................................................. 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12271 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 80A3B0AE65FDA6EB

FASTA31736,474
        10         20         30         40         50         60 
MSEGVGTFRM VPEEEQELRA QLEQLTTKDH GPVFGPCSQL PRHTLQKAKD ELNEREETRE 

        70         80         90        100        110        120 
EAVRELQEMV QAQAASGEEL AVAVAERVQE KDSGFFLRFI RARKFNVGRA YELLRGYVNF 

       130        140        150        160        170        180 
RLQYPELFDS LSPEAVRCTI EAGYPGVLSS RDKYGRVVML FNIENWQSQE ITFDEILQAY 

       190        200        210        220        230        240 
CFILEKLLEN EETQINGFCI IENFKGFTMQ QAASLRTSDL RKMVDMLQDS FPARFKAIHF 

       250        260        270        280        290        300 
IHQPWYFTTT YNVVKPFLKS KLLERVFVHG DDLSGFYQEI DENILPSDFG GTLPKYDGKA 

       310 
VAEQLFGPQA QAENTAF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein from bovine and human retina and comparison of the protein structures."
Crabb J.W., Goldflam S., Harris S.E., Saari J.C.
J. Biol. Chem. 263:18688-18692(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and structural analysis of the human gene encoding cellular retinaldehyde-binding protein."
Intres R., Goldflam S., Cook J.R., Crabb J.W.
J. Biol. Chem. 269:25411-25418(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Caudate nucleus.
[4]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].
[5]"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: Uterus.
[6]"Structural and functional characterization of recombinant human cellular retinaldehyde-binding protein."
Crabb J.W., Carlson A., Hen Y., Goldflam S., Intres R., West K.A., Hulmes J.D., Kapron J.T., Luck L.A., Horwitz J., Bok D.
Protein Sci. 7:746-757(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Newfoundland rod-cone dystrophy, an early-onset retinal dystrophy, is caused by splice-junction mutations in RLBP1."
Eichers E.R., Green J.S., Stockton D.W., Jackman C.S., Whelan J., McNamara J.A., Johnson G.J., Lupski J.R., Katsanis N.
Am. J. Hum. Genet. 70:955-964(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN NFRCD.
[8]"Bothnia dystrophy is caused by domino-like rearrangements in cellular retinaldehyde-binding protein mutant R234W."
He X., Lobsiger J., Stocker A.
Proc. Natl. Acad. Sci. U.S.A. 106:18545-18550(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 2-317 OF WILD-TYPE AND MUTANT TRP-234 IN COMPLEX WITH 11-CIS-RETINAL, FUNCTION, TISSUE SPECIFICITY, RETINAL-BINDING SITES.
[9]"Mutation of the gene encoding cellular retinaldehyde-binding protein in autosomal recessive retinitis pigmentosa."
Maw M.A., Kennedy B., Knight A., Bridges R., Roth K.E., Mani E.J., Mukkadan J.K., Nancarrow D., Crabb J.W., Denton M.J.
Nat. Genet. 17:198-200(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARRP GLN-151.
[10]"Bothnia dystrophy caused by mutations in the cellular retinaldehyde-binding protein gene (RLBP1) on chromosome 15q26."
Burstedt M.S., Sandgren O., Holmgren G., Forsman-Semb K.
Invest. Ophthalmol. Vis. Sci. 40:995-1000(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BRD TRP-234.
[11]"Recessive mutations in the RLBP1 gene encoding cellular retinaldehyde-binding protein in a form of retinitis punctata albescens."
Morimura H., Berson E.L., Dryja T.P.
Invest. Ophthalmol. Vis. Sci. 40:1000-1004(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA LYS-226.
+Additional computationally mapped references.

Web resources

Mutations of the RLBP1 gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04213 mRNA. Translation: AAA60251.1.
L34219 Genomic DNA. Translation: AAA65123.1.
AK312457 mRNA. Translation: BAG35364.1.
CH471101 Genomic DNA. Translation: EAX02038.1.
BC004199 mRNA. Translation: AAH04199.1.
CCDSCCDS32324.1.
PIRB31955.
RefSeqNP_000317.1. NM_000326.4.
UniGeneHs.1933.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XGGmodel-A67-295[»]
1XGHmodel-A67-295[»]
3HX3X-ray1.69A2-317[»]
3HY5X-ray3.04A2-317[»]
4CIZX-ray3.40A1-317[»]
4CJ6X-ray1.90A1-317[»]
ProteinModelPortalP12271.
SMRP12271. Positions 23-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111949. 2 interactions.
STRING9606.ENSP00000268125.

Chemistry

DrugBankDB00162. Vitamin A.

PTM databases

PhosphoSiteP12271.

Polymorphism databases

DMDM117391.

Proteomic databases

PaxDbP12271.
PRIDEP12271.

Protocols and materials databases

DNASU6017.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268125; ENSP00000268125; ENSG00000140522.
GeneID6017.
KEGGhsa:6017.
UCSCuc002bnl.3. human.

Organism-specific databases

CTD6017.
GeneCardsGC15M089753.
GeneReviewsRLBP1.
HGNCHGNC:10024. RLBP1.
MIM136880. phenotype.
180090. gene.
268000. phenotype.
607475. phenotype.
607476. phenotype.
neXtProtNX_P12271.
Orphanet85128. Bothnia retinal dystrophy.
227796. Fundus albipunctatus.
791. Retinitis pigmentosa.
52427. Retinitis punctata albescens.
PharmGKBPA34397.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG317741.
HOGENOMHOG000059544.
HOVERGENHBG004720.
InParanoidP12271.
OMALFGPRAQ.
OrthoDBEOG7H4DTZ.
PhylomeDBP12271.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000140522-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP12271.
BgeeP12271.
CleanExHS_RLBP1.
GenevestigatorP12271.

Family and domain databases

Gene3D3.40.525.10. 1 hit.
InterProIPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view]
PfamPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
PRINTSPR00180. CRETINALDHBP.
SMARTSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEPS50191. CRAL_TRIO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12271.
GeneWikiRetinaldehyde-binding_protein_1.
GenomeRNAi6017.
NextBio23475.
PROP12271.
SOURCESearch...

Entry information

Entry nameRLBP1_HUMAN
AccessionPrimary (citable) accession number: P12271
Secondary accession number(s): B2R667
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 140 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 15

Human chromosome 15: entries, gene names and cross-references to MIM