RLBP1_HUMAN
ID RLBP1_HUMAN Reviewed; 317 AA.
AC P12271; B2R667;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Retinaldehyde-binding protein 1;
DE AltName: Full=Cellular retinaldehyde-binding protein;
GN Name=RLBP1; Synonyms=CRALBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3198595; DOI=10.1016/s0021-9258(18)37339-3;
RA Crabb J.W., Goldflam S., Harris S.E., Saari J.C.;
RT "Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein
RT from bovine and human retina and comparison of the protein structures.";
RL J. Biol. Chem. 263:18688-18692(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7929238; DOI=10.1016/s0021-9258(18)47265-1;
RA Intres R., Goldflam S., Cook J.R., Crabb J.W.;
RT "Molecular cloning and structural analysis of the human gene encoding
RT cellular retinaldehyde-binding protein.";
RL J. Biol. Chem. 269:25411-25418(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CHARACTERIZATION.
RX PubMed=9541407; DOI=10.1002/pro.5560070324;
RA Crabb J.W., Carlson A., Hen Y., Goldflam S., Intres R., West K.A.,
RA Hulmes J.D., Kapron J.T., Luck L.A., Horwitz J., Bok D.;
RT "Structural and functional characterization of recombinant human cellular
RT retinaldehyde-binding protein.";
RL Protein Sci. 7:746-757(1998).
RN [7]
RP INVOLVEMENT IN NFRCD.
RX PubMed=11868161; DOI=10.1086/339688;
RA Eichers E.R., Green J.S., Stockton D.W., Jackman C.S., Whelan J.,
RA McNamara J.A., Johnson G.J., Lupski J.R., Katsanis N.;
RT "Newfoundland rod-cone dystrophy, an early-onset retinal dystrophy, is
RT caused by splice-junction mutations in RLBP1.";
RL Am. J. Hum. Genet. 70:955-964(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 2-317 OF WILD-TYPE AND MUTANT
RP TRP-234 IN COMPLEX WITH 11-CIS-RETINAL, FUNCTION, TISSUE SPECIFICITY, AND
RP RETINAL-BINDING SITES.
RX PubMed=19846785; DOI=10.1073/pnas.0907454106;
RA He X., Lobsiger J., Stocker A.;
RT "Bothnia dystrophy is caused by domino-like rearrangements in cellular
RT retinaldehyde-binding protein mutant R234W.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18545-18550(2009).
RN [9]
RP VARIANT RPA GLN-151.
RX PubMed=9326942; DOI=10.1038/ng1097-198;
RA Maw M.A., Kennedy B., Knight A., Bridges R., Roth K.E., Mani E.J.,
RA Mukkadan J.K., Nancarrow D., Crabb J.W., Denton M.J.;
RT "Mutation of the gene encoding cellular retinaldehyde-binding protein in
RT autosomal recessive retinitis pigmentosa.";
RL Nat. Genet. 17:198-200(1997).
RN [10]
RP VARIANT BRD TRP-234.
RX PubMed=10102298;
RA Burstedt M.S., Sandgren O., Holmgren G., Forsman-Semb K.;
RT "Bothnia dystrophy caused by mutations in the cellular retinaldehyde-
RT binding protein gene (RLBP1) on chromosome 15q26.";
RL Invest. Ophthalmol. Vis. Sci. 40:995-1000(1999).
RN [11]
RP INVOLVEMENT IN RPA, AND VARIANT RPA LYS-226.
RX PubMed=10102299;
RA Morimura H., Berson E.L., Dryja T.P.;
RT "Recessive mutations in the RLBP1 gene encoding cellular retinaldehyde-
RT binding protein in a form of retinitis punctata albescens.";
RL Invest. Ophthalmol. Vis. Sci. 40:1000-1004(1999).
RN [12]
RP VARIANT RPA GLN-151.
RX PubMed=11453974; DOI=10.1034/j.1399-0004.2001.590607.x;
RA Katsanis N., Shroyer N.F., Lewis R.A., Cavender J.C., Al-Rajhi A.A.,
RA Jabak M., Lupski J.R.;
RT "Fundus albipunctatus and retinitis punctata albescens in a pedigree with
RT an R150Q mutation in RLBP1.";
RL Clin. Genet. 59:424-429(2001).
CC -!- FUNCTION: Soluble retinoid carrier essential the proper function of
CC both rod and cone photoreceptors. Participates in the regeneration of
CC active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-
CC trans products of the rhodopsin photocycle and in the de novo synthesis
CC of these retinoids from 11-trans metabolic precursors. The cycling of
CC retinoids between photoreceptor and adjacent pigment epithelium cells
CC is known as the 'visual cycle'. {ECO:0000269|PubMed:19846785}.
CC -!- SUBUNIT: Interacts with DEGS1; the interaction increases synthesis of
CC chromophore-precursors by DEGS1. {ECO:0000250|UniProtKB:E1C1U1}.
CC -!- INTERACTION:
CC P12271; Q9P2G9-2: KLHL8; NbExp=3; IntAct=EBI-11959637, EBI-11959635;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Retina and pineal gland. Not present in
CC photoreceptor cells but is expressed abundantly in the adjacent retinal
CC pigment epithelium (RPE) and in the Mueller glial cells of the retina.
CC {ECO:0000269|PubMed:19846785}.
CC -!- DISEASE: Bothnia retinal dystrophy (BRD) [MIM:607475]: A type of
CC retinitis punctata albescens. Affected individuals show night blindness
CC from early childhood with features consistent with retinitis punctata
CC albescens and macular degeneration. {ECO:0000269|PubMed:10102298}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Rod-cone dystrophy Newfoundland (NFRCD) [MIM:607476]: A rod-
CC cone dystrophy reminiscent of retinitis punctata albescens but with a
CC substantially lower age at onset and more-rapid and distinctive
CC progression. Rod-cone dystrophies results from initial loss of rod
CC photoreceptors, later followed by cone photoreceptors loss.
CC {ECO:0000269|PubMed:11868161}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Retinitis punctata albescens (RPA) [MIM:136880]: A form of
CC fleck retina disease characterized by aggregation of white flecks
CC posteriorly in the retina, causing night blindness and delayed dark
CC adaptation. It differs from fundus albipunctatus in being progressive
CC and evolving to generalized atrophy of the retina.
CC {ECO:0000269|PubMed:10102299, ECO:0000269|PubMed:11453974,
CC ECO:0000269|PubMed:9326942}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Mutations of the RLBP1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/cralbp.htm";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J04213; AAA60251.1; -; mRNA.
DR EMBL; L34219; AAA65123.1; -; Genomic_DNA.
DR EMBL; AK312457; BAG35364.1; -; mRNA.
DR EMBL; CH471101; EAX02038.1; -; Genomic_DNA.
DR EMBL; BC004199; AAH04199.1; -; mRNA.
DR CCDS; CCDS32324.1; -.
DR PIR; B31955; B31955.
DR RefSeq; NP_000317.1; NM_000326.4.
DR RefSeq; XP_011520172.1; XM_011521870.2.
DR PDB; 3HX3; X-ray; 1.69 A; A=2-317.
DR PDB; 3HY5; X-ray; 3.04 A; A=2-317.
DR PDB; 4CIZ; X-ray; 3.40 A; A=1-317.
DR PDB; 4CJ6; X-ray; 1.90 A; A=1-317.
DR PDBsum; 3HX3; -.
DR PDBsum; 3HY5; -.
DR PDBsum; 4CIZ; -.
DR PDBsum; 4CJ6; -.
DR AlphaFoldDB; P12271; -.
DR SMR; P12271; -.
DR BioGRID; 111949; 7.
DR IntAct; P12271; 1.
DR STRING; 9606.ENSP00000268125; -.
DR BindingDB; P12271; -.
DR DrugBank; DB00162; Vitamin A.
DR DrugCentral; P12271; -.
DR iPTMnet; P12271; -.
DR PhosphoSitePlus; P12271; -.
DR BioMuta; RLBP1; -.
DR DMDM; 117391; -.
DR jPOST; P12271; -.
DR MassIVE; P12271; -.
DR PaxDb; P12271; -.
DR PeptideAtlas; P12271; -.
DR PRIDE; P12271; -.
DR ProteomicsDB; 52841; -.
DR Antibodypedia; 15709; 272 antibodies from 27 providers.
DR DNASU; 6017; -.
DR Ensembl; ENST00000268125.10; ENSP00000268125.5; ENSG00000140522.12.
DR GeneID; 6017; -.
DR KEGG; hsa:6017; -.
DR MANE-Select; ENST00000268125.10; ENSP00000268125.5; NM_000326.5; NP_000317.1.
DR UCSC; uc002bnl.4; human.
DR CTD; 6017; -.
DR DisGeNET; 6017; -.
DR GeneCards; RLBP1; -.
DR GeneReviews; RLBP1; -.
DR HGNC; HGNC:10024; RLBP1.
DR HPA; ENSG00000140522; Tissue enriched (retina).
DR MalaCards; RLBP1; -.
DR MIM; 136880; phenotype.
DR MIM; 180090; gene.
DR MIM; 607475; phenotype.
DR MIM; 607476; phenotype.
DR neXtProt; NX_P12271; -.
DR OpenTargets; ENSG00000140522; -.
DR Orphanet; 85128; Bothnia retinal dystrophy.
DR Orphanet; 227796; Fundus albipunctatus.
DR Orphanet; 791; Retinitis pigmentosa.
DR Orphanet; 52427; Retinitis punctata albescens.
DR PharmGKB; PA34397; -.
DR VEuPathDB; HostDB:ENSG00000140522; -.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000160026; -.
DR HOGENOM; CLU_046597_4_0_1; -.
DR InParanoid; P12271; -.
DR OMA; GPVFGKC; -.
DR OrthoDB; 1133487at2759; -.
DR PhylomeDB; P12271; -.
DR BioCyc; MetaCyc:ENSG00000140522-MON; -.
DR PathwayCommons; P12271; -.
DR Reactome; R-HSA-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-HSA-2453864; Retinoid cycle disease events.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR SignaLink; P12271; -.
DR BioGRID-ORCS; 6017; 11 hits in 1068 CRISPR screens.
DR ChiTaRS; RLBP1; human.
DR EvolutionaryTrace; P12271; -.
DR GeneWiki; Retinaldehyde-binding_protein_1; -.
DR GenomeRNAi; 6017; -.
DR Pharos; P12271; Tbio.
DR PRO; PR:P12271; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P12271; protein.
DR Bgee; ENSG00000140522; Expressed in pigmented layer of retina and 93 other tissues.
DR ExpressionAtlas; P12271; baseline and differential.
DR Genevisible; P12271; HS.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005502; F:11-cis retinal binding; IEA:Ensembl.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IBA:GO_Central.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR GO; GO:0006776; P:vitamin A metabolic process; TAS:ProtInc.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR032941; RLBP1.
DR PANTHER; PTHR10174:SF200; PTHR10174:SF200; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Disease variant; Reference proteome;
KW Retinol-binding; Sensory transduction; Transport; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P10123"
FT CHAIN 2..317
FT /note="Retinaldehyde-binding protein 1"
FT /id="PRO_0000079330"
FT DOMAIN 136..297
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT BINDING 180
FT /ligand="11-cis-retinal"
FT /ligand_id="ChEBI:CHEBI:16066"
FT /evidence="ECO:0000269|PubMed:19846785"
FT BINDING 202
FT /ligand="11-cis-retinal"
FT /ligand_id="ChEBI:CHEBI:16066"
FT /evidence="ECO:0000269|PubMed:19846785"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P10123"
FT VARIANT 151
FT /note="R -> Q (in RPA; loss of ability to bind 11-cis-
FT retinaldehyde; dbSNP:rs137853290)"
FT /evidence="ECO:0000269|PubMed:11453974,
FT ECO:0000269|PubMed:9326942"
FT /id="VAR_005140"
FT VARIANT 226
FT /note="M -> K (in RPA; dbSNP:rs137853291)"
FT /evidence="ECO:0000269|PubMed:10102299"
FT /id="VAR_037317"
FT VARIANT 234
FT /note="R -> W (in BRD; dbSNP:rs28933990)"
FT /evidence="ECO:0000269|PubMed:10102298"
FT /id="VAR_015172"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3HY5"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3HY5"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:3HY5"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:3HY5"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:3HY5"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:3HY5"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:3HX3"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:3HX3"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:3HX3"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3HX3"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:3HX3"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:3HX3"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:3HX3"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:3HX3"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:3HX3"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3HX3"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:3HX3"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3HX3"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:3HX3"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:3HX3"
SQ SEQUENCE 317 AA; 36474 MW; 80A3B0AE65FDA6EB CRC64;
MSEGVGTFRM VPEEEQELRA QLEQLTTKDH GPVFGPCSQL PRHTLQKAKD ELNEREETRE
EAVRELQEMV QAQAASGEEL AVAVAERVQE KDSGFFLRFI RARKFNVGRA YELLRGYVNF
RLQYPELFDS LSPEAVRCTI EAGYPGVLSS RDKYGRVVML FNIENWQSQE ITFDEILQAY
CFILEKLLEN EETQINGFCI IENFKGFTMQ QAASLRTSDL RKMVDMLQDS FPARFKAIHF
IHQPWYFTTT YNVVKPFLKS KLLERVFVHG DDLSGFYQEI DENILPSDFG GTLPKYDGKA
VAEQLFGPQA QAENTAF
