ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P02753


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name RET4_HUMAN
Primary accession number P02753
Secondary accession numbers O43478 O43479 Q5VY24 Q8WWA3 Q9P178
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on March 29, 2005 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 114)
Name and origin of the protein
Protein name Retinol-binding protein 4 [Precursor]
Synonyms Plasma retinol-binding protein
PRBP
RBP
Contains Plasma retinol-binding protein(1-182)
Plasma retinol-binding protein(1-181)
Plasma retinol-binding protein(1-179)
Plasma retinol-binding protein(1-176)
Gene name
Name: RBP4
ORFNames: PRO2222
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/11.22.7769; PubMed=6316270 [NCBI, ExPASy, EBI, Israel, Japan]
Colantuoni V., Romano V., Bensi G., Santoro C., Costanzo F., Raugei G., Cortese R.;
"Cloning and sequencing of a full length cDNA coding for human retinol-binding protein.";
Nucleic Acids Res. 11:7769-7776(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189.
PubMed=2998779 [NCBI, ExPASy, EBI, Israel, Japan]
D'Onofrio C., Colantuoni V., Cortese R.;
"Structure and cell-specific expression of a cloned human retinol binding protein gene: the 5'-flanking region contains hepatoma specific transcriptional signals.";
EMBO J. 4:1981-1989(1985).
[5]
PROTEIN SEQUENCE OF 19-201, AND DISULFIDE BONDS.
PubMed=2444024 [NCBI, ExPASy, EBI, Israel, Japan]
Rask L., Anundi H., Fohlman J., Peterson P.A.;
"The complete amino acid sequence of human serum retinol-binding protein.";
Ups. J. Med. Sci. 92:115-146(1987).
[6]
PROTEIN SEQUENCE OF 19-201.
PubMed=6942701 [NCBI, ExPASy, EBI, Israel, Japan]
Rask L., Anundi H., Boehme J., Eriksson U., Ronne H., Sege K., Peterson P.A.;
"Structural and functional studies of vitamin A-binding proteins.";
Ann. N. Y. Acad. Sci. 359:79-90(1981).
[7]
PROTEIN SEQUENCE OF 19-183.
DOI=10.1016/0014-5793(79)81084-4; PubMed=573217 [NCBI, ExPASy, EBI, Israel, Japan]
Rask L., Anundi H., Peterson P.A.;
"The primary structure of the human retinol-binding protein.";
FEBS Lett. 104:55-58(1979).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-201.
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.;
"Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[9]
PARTIAL PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
PubMed=7666002 [NCBI, ExPASy, EBI, Israel, Japan]
Jaconi S., Rose K., Hughes G.J., Saurat J.-H., Siegenthaler G.;
"Characterization of two post-translationally processed forms of human serum retinol-binding protein: altered ratios in chronic renal failure.";
J. Lipid Res. 36:1247-1253(1995).
[10]
MASS SPECTROMETRY.
DOI=10.1021/pr025574c; PubMed=12716133 [NCBI, ExPASy, EBI, Israel, Japan]
Kiernan U.A., Tubbs K.A., Nedelkov D., Niederkofler E.E., McConnell E., Nelson R.W.;
"Comparative urine protein phenotyping using mass spectrometric immunoassay.";
J. Proteome Res. 2:191-197(2003).
[11]
MASS SPECTROMETRY.
DOI=10.1016/S0006-291X(02)02212-X; PubMed=12237133 [NCBI, ExPASy, EBI, Israel, Japan]
Kiernan U.A., Tubbs K.A., Nedelkov D., Niederkofler E.E., Nelson R.W.;
"Comparative phenotypic analyses of human plasma and urinary retinol binding protein using mass spectrometric immunoassay.";
Biochem. Biophys. Res. Commun. 297:401-405(2002).
[12]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
PubMed=6540172 [NCBI, ExPASy, EBI, Israel, Japan]
Newcomer M.E., Jones T.A., Aqvist J., Sundelin J., Eriksson U., Rask L., Peterson P.A.;
"The three-dimensional structure of retinol-binding protein.";
EMBO J. 3:1451-1454(1984).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1002/prot.340080108; PubMed=2217163 [NCBI, ExPASy, EBI, Israel, Japan]
Cowan S.W., Newcomer M.E., Jones T.A.;
"Crystallographic refinement of human serum retinol binding protein at 2-A resolution.";
Proteins 8:44-61(1990).
[14]
COMPARISON OF X-RAY STRUCTURES.
PubMed=1623143 [NCBI, ExPASy, EBI, Israel, Japan]
Monaco H.L., Zanotti G.;
"Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity.";
Biopolymers 32:457-465(1992).
[15]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH TTR.
DOI=10.1021/bi982291i; PubMed=10052934 [NCBI, ExPASy, EBI, Israel, Japan]
Naylor H.M., Newcomer M.E.;
"The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP.";
Biochemistry 38:2647-2653(1999).
[16]
VARIANTS RBP DEFICIENCY ASN-59 AND ASP-93.
PubMed=9888420 [NCBI, ExPASy, EBI, Israel, Japan]
Seeliger M.W., Biesalski H.K., Wissinger B., Gollnick H., Gielen S., Frank J., Beck S.C., Zrenner E.;
"Phenotype in retinol deficiency due to a hereditary defect in retinol binding protein synthesis.";
Invest. Ophthalmol. Vis. Sci. 40:3-11(1999).
[17]
CHARACTERIZATION OF VARIANTS ASN-59 AND ASP-93.
PubMed=10232633 [NCBI, ExPASy, EBI, Israel, Japan]
Biesalski H.K., Frank J., Beck S.C., Heinrich F., Illek B., Reifen R., Gollnick H., Seeliger M.W., Wissinger B., Zrenner E.;
"Biochemical but not clinical vitamin A deficiency results from mutations in the gene for retinol binding protein.";
Am. J. Clin. Nutr. 69:931-936(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X00129; CAA24959.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356214; CAH72328.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020633; AAH20633.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X02775; CAA26553.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X02824; CAB46489.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF119868; AAF69622.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF025334; AAC02945.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF025335; AAC02946.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A93494; VAHU.
RefSeq NP_006735.2; -.
UniGene Hs.50223
3D structure databases
PDB
1BRP; X-ray; 2.50 A; A=19-200.[ExPASy / RCSB / EBI]
1BRQ; X-ray; 2.50 A; A=19-200.[ExPASy / RCSB / EBI]
1JYD; X-ray; 1.70 A; A=19-200.[ExPASy / RCSB / EBI]
1JYJ; X-ray; 2.00 A; A=19-200.[ExPASy / RCSB / EBI]
1QAB; X-ray; 3.20 A; E/F=22-201.[ExPASy / RCSB / EBI]
1RBP; X-ray; 2.00 A; A=19-200.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BRP; -.
1BRQ; -.
1JYD; -.
1JYJ; -.
1QAB; -.
1RBP; -.
ModBase P02753.
2D gel databases
SWISS-2DPAGE P02753; -.
Siena-2DPAGE P02753; -.
Organism-specific databases
H-InvDB HIX0009047; -.
HGNC HGNC:9922; RBP4.
GenAtlas RBP4.
HPA CAB004555; -.
HPA001641; -.
MIM 180250; gene+phenotype. [NCBI / EBI]
PharmGKB PA34289; -.
GeneCards P02753.
Gene expression databases
ArrayExpress P02753; -.
CleanEx HS_RBP4; -.
GermOnline ENSG00000138207; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0016918; Molecular function: retinal binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019841; Molecular function: retinol binding (inferred from electronic annotation from UniProtKB-KW).
GO:0034632; Molecular function: retinol transporter activity (inferred by curator from UniProtKB).
GO:0048738; Biological process: cardiac muscle development (inferred from sequence or structural similarity from UniProtKB).
GO:0048562; Biological process: embryonic organ morphogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0060059; Biological process: embryonic retina morphogenesis in camera-type eye (inferred from sequence or structural similarity from UniProtKB).
GO:0048706; Biological process: embryonic skeletal system development (inferred from sequence or structural similarity from UniProtKB).
GO:0048807; Biological process: female genitalia morphogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0006094; Biological process: gluconeogenesis (inferred from mutant phenotype from UniProtKB).
GO:0042593; Biological process: glucose homeostasis (inferred from direct assay from UniProtKB).
GO:0030324; Biological process: lung development (inferred from sequence or structural similarity from UniProtKB).
GO:0030277; Biological process: maintenance of gastrointestinal epithelium (inferred from direct assay from UniProtKB).
GO:0060044; Biological process: negative regulation of cardiac muscle cell proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0051024; Biological process: positive regulation of immunoglobulin secretion (inferred from sequence or structural similarity from UniProtKB).
GO:0032024; Biological process: positive regulation of insulin secretion (inferred from mutant phenotype from UniProtKB).
GO:0032526; Biological process: response to retinoic acid (inferred from direct assay from UniProtKB).
GO:0042572; Biological process: retinol metabolic process (inferred from mutant phenotype from UniProtKB).
GO:0034633; Biological process: retinol transport (inferred by curator from UniProtKB).
GO:0060157; Biological process: urinary bladder development (inferred from sequence or structural similarity from UniProtKB).
GO:0060065; Biological process: uterus development (inferred from sequence or structural similarity from UniProtKB).
GO:0060068; Biological process: vagina development (inferred from sequence or structural similarity from UniProtKB).
GO:0007601; Biological process: visual perception (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012674; Calycin.
IPR002345; Lipocalin.
IPR000566; Lipocln_cytFABP.
IPR002449; Retinol_bd.
Graphical view of domain structure.
Gene3D G3DSA:2.40.128.20; Calycin; 1.
PANTHER PTHR11873; Retinol_bd; 1.
Pfam PF00061; Lipocalin; 1.
Pfam graphical view of domain structure.
PRINTS PR00179; LIPOCALIN.
PR01174; RETINOLBNDNG.
PROSITE PS00213; LIPOCALIN; 1.
ProtoNet P02753.
Other
SWISS-3DIMAGE P02753.
Genome annotation databases
Ensembl ENSG00000138207; Homo sapiens. [Contig view]
GeneID 5950; -.
KEGG hsa:5950; -.
Phylogenomic databases
HOGENOM P02753; -.
HOVERGEN P02753; -.
Other
DrugBank DB00162; Vitamin A.
LinkHub P02753; -.
NextBio 23182; -.
SOURCE RBP4; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Disease mutation; Retinol-binding; Secreted; Sensory transduction; Signal; Transport; Vision; Vitamin A.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   201  183     Retinol-binding protein 4. PRO_0000017961
CHAIN   19   200  182     Plasma retinol-binding protein(1-182). PRO_0000017962
CHAIN   19   199  181     Plasma retinol-binding protein(1-181). PRO_0000017963
CHAIN   19   197  179     Plasma retinol-binding protein(1-179). PRO_0000017964
CHAIN   19   194  176     Plasma retinol-binding protein(1-176). PRO_0000017965
DISULFID   22   178         
DISULFID   88   192         
DISULFID   138   147         
VARIANT   59    59  1     I -> N (in RBP deficiency). VAR_009276 [3D]
VARIANT   93    93  1     G -> D (in RBP deficiency). VAR_009277 [3D]
CONFLICT   8     8        L -> F (in Ref. 3; AAH20633). 
CONFLICT   13    17        LGSGR -> WAA (in Ref. 1 and 4). 
HELIX   24    26  3      
HELIX   35    38  4      
STRAND   40    48  9      
STRAND   55    65  11      
STRAND   71    80  10      
STRAND   82    84  3      
STRAND   86    96  11      
STRAND   103   112  10      
STRAND   118   127  10      
STRAND   129   141  13      
STRAND   145   158  14      
HELIX   164   176  13      
Sequence information
Length: 201 AA [This is the length of the unprocessed precursor] Molecular weight: 23010 Da [This is the MW of the unprocessed precursor] CRC64: 660C6DD8CC9B811A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKWVWALLLL AALGSGRAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP EGLFLQDNIV 

        70         80         90        100        110        120 
AEFSVDETGQ MSATAKGRVR LLNNWDVCAD MVGTFTDTED PAKFKMKYWG VASFLQKGND 

       130        140        150        160        170        180 
DHWIVDTDYD TYAVQYSCRL LNLDGTCADS YSFVFSRDPN GLPPEAQKIV RQRQEELCLA 

       190        200 
RQYRLIVHNG YCDGRSERNL L 

P02753 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!