P12271 (RLBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Retinaldehyde-binding protein 1

Alternative name(s):
Cellular retinaldehyde-binding protein

Gene names

Name:	RLBP1
Synonyms:	CRALBP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Sensory transduction Transport Vision
Cellular component	Cytoplasm
Disease	Disease mutation Retinitis pigmentosa
Ligand	Retinol-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to stimulus Inferred from electronic annotation. Source: UniProtKB-KW visual perception Traceable author statement Ref.9. Source: ProtInc vitamin A metabolic process Traceable author statement Ref.9. Source: ProtInc
Cellular_component	cell body Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	11-cis retinal binding Inferred from electronic annotation. Source: Compara retinol binding Inferred from electronic annotation. Source: UniProtKB-KW transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 317

316

Retinaldehyde-binding protein 1

PRO_0000079330

Regions

Domain

136 – 297

162

CRAL-TRIO

Sites

Binding site

180

1

11-cis-retinal

Binding site

202

1

11-cis-retinal

Amino acid modifications

Modified residue

2

1

N-acetylserine By similarity

Natural variations

Natural variant

151

1

R → Q in ARRP; loss of ability to bind 11-cis-retinaldehyde. Ref.9
Corresponds to variant rs28933989 [ dbSNP | Ensembl ].

VAR_005140

Natural variant

226

1

M → K in FA. Ref.11

VAR_037317

Natural variant

234

1

R → W in BRD. Ref.8 Ref.10
Corresponds to variant rs28933990 [ dbSNP | Ensembl ].

VAR_015172

Secondary structure

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317

Helix Strand Turn

Details...

Helix

27 – 29

3

Beta strand

33 – 35

3

Turn

41 – 43

3

Helix

44 – 49

6

Turn

50 – 52

3

Turn

55 – 57

3

Helix

58 – 74

17

Turn

75 – 77

3

Helix

79 – 87

9

Turn

88 – 90

3

Helix

93 – 102

10

Turn

103 – 105

3

Helix

107 – 123

17

Helix

125 – 127

3

Turn

128 – 130

3

Helix

133 – 141

9

Beta strand

144 – 147

4

Beta strand

157 – 162

6

Turn

168 – 170

3

Helix

173 – 187

15

Helix

191 – 196

6

Beta strand

198 – 203

6

Helix

209 – 214

6

Helix

217 – 228

12

Turn

232 – 234

3

Beta strand

235 – 242

8

Helix

247 – 254

8

Helix

255 – 257

3

Helix

260 – 263

4

Beta strand

266 – 270

5

Helix

274 – 279

6

Helix

282 – 284

3

Helix

287 – 289

3

Beta strand

291 – 293

3

Helix

299 – 305

7

Sequences

	Sequence		Length	Mass (Da)
	P12271 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 80A3B0AE65FDA6EB	FASTA	317	36,474
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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

GeneReviews

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.

IPI

IPI00218633.

PIR

B31955.

RefSeq

NP_000317.1. NM_000326.4.

UniGene

Hs.1933.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P12271.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000268125.

PTM databases

PhosphoSite

P12271.

Polymorphism databases

DMDM

117391.

Proteomic databases

PaxDb

P12271.

PRIDE

P12271.

Protocols and materials databases

DNASU

6017.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000268125; ENSP00000268125; ENSG00000140522.

GeneID

6017.

KEGG

hsa:6017.

UCSC

uc002bnl.3. human.

Organism-specific databases

CTD

6017.

GeneCards

GC15M089753.

HGNC

HGNC:10024. RLBP1.

MIM

136880. phenotype.
180090. gene.
268000. phenotype.
607475. phenotype.
607476. phenotype.

neXtProt

NX_P12271.

Orphanet

85128. Bothnia retinal dystrophy.
227796. Fundus albipunctatus.
791. Retinitis pigmentosa.
52427. Retinitis punctata albescens.

PharmGKB

PA34397.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG317741.

HOGENOM

HOG000059544.

HOVERGEN

HBG004720.

InParanoid

P12271.

OMA

GYVNFRL.

OrthoDB

EOG42FSJ0.

PhylomeDB

P12271.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000140522-MONOMER.

Gene expression databases

ArrayExpress

P12271.

Bgee

P12271.

CleanEx

HS_RLBP1.

Genevestigator

P12271.

GermOnline

ENSG00000140522. Homo sapiens.

Family and domain databases

Gene3D

3.40.525.10. 1 hit.

InterPro

IPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view]

Pfam

PF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]

PRINTS

PR00180. CRETINALDHBP.

SMART

SM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]

SUPFAM

SSF52087. CRAL_TRIO_C. 1 hit.
SSF46938. Sec14p_like_N. 1 hit.

PROSITE

PS50191. CRAL_TRIO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00162. Vitamin A.

EvolutionaryTrace

P12271.

GenomeRNAi

6017.

NextBio

23475.

SOURCE

Search...

Entry information

Entry name

RLBP1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.