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P12271

- RLBP1_HUMAN

UniProt

P12271 - RLBP1_HUMAN

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Protein

Retinaldehyde-binding protein 1

Gene

RLBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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'.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei180 – 180111-cis-retinal1 Publication
Binding sitei202 – 202111-cis-retinal1 Publication

GO - Molecular functioni

  1. 11-cis retinal binding Source: Ensembl
  2. retinol binding Source: UniProtKB-KW
  3. transporter activity Source: InterPro

GO - Biological processi

  1. phototransduction, visible light Source: Reactome
  2. retinoid metabolic process Source: Reactome
  3. visual perception Source: ProtInc
  4. vitamin A metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Transport, Vision

Keywords - Ligandi

Retinol-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000140522-MONOMER.
ReactomeiREACT_160083. The retinoid cycle in cones (daylight vision).
REACT_160130. Retinoid cycle disease events.
REACT_160156. The canonical retinoid cycle in rods (twilight vision).

Names & Taxonomyi

Protein namesi
Recommended name:
Retinaldehyde-binding protein 1
Alternative name(s):
Cellular retinaldehyde-binding protein
Gene namesi
Name:RLBP1
Synonyms:CRALBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:10024. RLBP1.

Subcellular locationi

GO - Cellular componenti

  1. cell body Source: Ensembl
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti151 – 1511R → Q in ARRP; loss of ability to bind 11-cis-retinaldehyde. 1 Publication
Corresponds to variant rs28933989 [ dbSNP | Ensembl ].
VAR_005140
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti234 – 2341R → W in BRD. 1 Publication
Corresponds to variant rs28933990 [ dbSNP | Ensembl ].
VAR_015172
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

MIMi136880. phenotype.
268000. phenotype.
607475. phenotype.
607476. phenotype.
Orphaneti85128. Bothnia retinal dystrophy.
227796. Fundus albipunctatus.
791. Retinitis pigmentosa.
52427. Retinitis punctata albescens.
PharmGKBiPA34397.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 317316Retinaldehyde-binding protein 1PRO_0000079330Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP12271.
PRIDEiP12271.

PTM databases

PhosphoSiteiP12271.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP12271.
CleanExiHS_RLBP1.
ExpressionAtlasiP12271. baseline.
GenevestigatoriP12271.

Interactioni

Protein-protein interaction databases

BioGridi111949. 2 interactions.
STRINGi9606.ENSP00000268125.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 293
Beta strandi33 – 353
Turni41 – 433
Helixi44 – 496
Turni50 – 523
Turni55 – 573
Helixi58 – 7417
Turni75 – 773
Helixi79 – 879
Turni88 – 903
Helixi93 – 10210
Turni103 – 1053
Helixi107 – 12317
Helixi125 – 1273
Turni128 – 1303
Helixi133 – 1419
Beta strandi144 – 1474
Beta strandi157 – 1626
Turni168 – 1703
Helixi173 – 18715
Helixi191 – 1966
Beta strandi198 – 2036
Helixi209 – 2146
Helixi217 – 22812
Turni232 – 2343
Beta strandi235 – 2428
Helixi247 – 2548
Helixi255 – 2573
Helixi260 – 2634
Beta strandi266 – 2705
Helixi274 – 2796
Helixi282 – 2843
Helixi287 – 2893
Beta strandi291 – 2933
Helixi299 – 3057

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP12271.
SMRiP12271. Positions 23-306.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12271.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini136 – 297162CRAL-TRIOPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG317741.
GeneTreeiENSGT00550000074253.
HOGENOMiHOG000059544.
HOVERGENiHBG004720.
InParanoidiP12271.
OMAiLFGPRAQ.
OrthoDBiEOG7H4DTZ.
PhylomeDBiP12271.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view]
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
PRINTSiPR00180. CRETINALDHBP.
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12271-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEGVGTFRM VPEEEQELRA QLEQLTTKDH GPVFGPCSQL PRHTLQKAKD
60 70 80 90 100
ELNEREETRE EAVRELQEMV QAQAASGEEL AVAVAERVQE KDSGFFLRFI
110 120 130 140 150
RARKFNVGRA YELLRGYVNF RLQYPELFDS LSPEAVRCTI EAGYPGVLSS
160 170 180 190 200
RDKYGRVVML FNIENWQSQE ITFDEILQAY CFILEKLLEN EETQINGFCI
210 220 230 240 250
IENFKGFTMQ QAASLRTSDL RKMVDMLQDS FPARFKAIHF IHQPWYFTTT
260 270 280 290 300
YNVVKPFLKS KLLERVFVHG DDLSGFYQEI DENILPSDFG GTLPKYDGKA
310
VAEQLFGPQA QAENTAF
Length:317
Mass (Da):36,474
Last modified:January 23, 2007 - v2
Checksum:i80A3B0AE65FDA6EB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti151 – 1511R → Q in ARRP; loss of ability to bind 11-cis-retinaldehyde. 1 Publication
Corresponds to variant rs28933989 [ dbSNP | Ensembl ].
VAR_005140
Natural varianti226 – 2261M → K in FA. 1 Publication
VAR_037317
Natural varianti234 – 2341R → W in BRD. 1 Publication
Corresponds to variant rs28933990 [ dbSNP | Ensembl ].
VAR_015172

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS32324.1.
PIRiB31955.
RefSeqiNP_000317.1. NM_000326.4.
UniGeneiHs.1933.

Genome annotation databases

EnsembliENST00000268125; ENSP00000268125; ENSG00000140522.
GeneIDi6017.
KEGGihsa:6017.
UCSCiuc002bnl.3. human.

Polymorphism databases

DMDMi117391.

Cross-referencesi

Web resourcesi

Mutations of the RLBP1 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS32324.1.
PIRi B31955.
RefSeqi NP_000317.1. NM_000326.4.
UniGenei Hs.1933.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XGG model - A 67-295 [» ]
1XGH model - A 67-295 [» ]
3HX3 X-ray 1.69 A 2-317 [» ]
3HY5 X-ray 3.04 A 2-317 [» ]
4CIZ X-ray 3.40 A 1-317 [» ]
4CJ6 X-ray 1.90 A 1-317 [» ]
ProteinModelPortali P12271.
SMRi P12271. Positions 23-306.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111949. 2 interactions.
STRINGi 9606.ENSP00000268125.

Chemistry

DrugBanki DB00162. Vitamin A.

PTM databases

PhosphoSitei P12271.

Polymorphism databases

DMDMi 117391.

Proteomic databases

PaxDbi P12271.
PRIDEi P12271.

Protocols and materials databases

DNASUi 6017.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268125 ; ENSP00000268125 ; ENSG00000140522 .
GeneIDi 6017.
KEGGi hsa:6017.
UCSCi uc002bnl.3. human.

Organism-specific databases

CTDi 6017.
GeneCardsi GC15M089753.
GeneReviewsi RLBP1.
HGNCi HGNC:10024. RLBP1.
MIMi 136880. phenotype.
180090. gene.
268000. phenotype.
607475. phenotype.
607476. phenotype.
neXtProti NX_P12271.
Orphaneti 85128. Bothnia retinal dystrophy.
227796. Fundus albipunctatus.
791. Retinitis pigmentosa.
52427. Retinitis punctata albescens.
PharmGKBi PA34397.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG317741.
GeneTreei ENSGT00550000074253.
HOGENOMi HOG000059544.
HOVERGENi HBG004720.
InParanoidi P12271.
OMAi LFGPRAQ.
OrthoDBi EOG7H4DTZ.
PhylomeDBi P12271.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000140522-MONOMER.
Reactomei REACT_160083. The retinoid cycle in cones (daylight vision).
REACT_160130. Retinoid cycle disease events.
REACT_160156. The canonical retinoid cycle in rods (twilight vision).

Miscellaneous databases

EvolutionaryTracei P12271.
GeneWikii Retinaldehyde-binding_protein_1.
GenomeRNAii 6017.
NextBioi 23475.
PROi P12271.
SOURCEi Search...

Gene expression databases

Bgeei P12271.
CleanExi HS_RLBP1.
ExpressionAtlasi P12271. baseline.
Genevestigatori P12271.

Family and domain databases

Gene3Di 3.40.525.10. 1 hit.
InterProi IPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view ]
Pfami PF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view ]
PRINTSi PR00180. CRETINALDHBP.
SMARTi SM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view ]
SUPFAMi SSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEi PS50191. CRAL_TRIO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiRLBP1_HUMAN
AccessioniPrimary (citable) accession number: P12271
Secondary accession number(s): B2R667
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 143 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3