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Retinol-binding protein 4 (Plasma retinol-binding protein) (PRBP) (RBP) [Cleaved into: Plasma retinol-binding protein(1-182); Plasma retinol-binding protein(1-181); Plasma retinol-binding protein(1-179); Plasma retinol-binding protein(1-176)]

 RET4_HUMAN              Reviewed;         201 AA.
P02753; D3DR38; O43478; O43479; Q5VY24; Q8WWA3; Q9P178;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
29-MAR-2005, sequence version 3.
27-SEP-2017, entry version 202.
RecName: Full=Retinol-binding protein 4;
AltName: Full=Plasma retinol-binding protein;
Short=PRBP;
Short=RBP;
Contains:
RecName: Full=Plasma retinol-binding protein(1-182);
Contains:
RecName: Full=Plasma retinol-binding protein(1-181);
Contains:
RecName: Full=Plasma retinol-binding protein(1-179);
Contains:
RecName: Full=Plasma retinol-binding protein(1-176);
Flags: Precursor;
Name=RBP4; ORFNames=PRO2222;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6316270; DOI=10.1093/nar/11.22.7769;
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].
PubMed=15164054; DOI=10.1038/nature02462;
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 GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189.
PubMed=2998779;
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).
[6]
PROTEIN SEQUENCE OF 19-201, AND DISULFIDE BONDS.
PubMed=2444024; DOI=10.3109/03009738709178685;
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).
[7]
PROTEIN SEQUENCE OF 19-201.
PubMed=6942701; DOI=10.1111/j.1749-6632.1981.tb12739.x;
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).
[8]
PROTEIN SEQUENCE OF 19-183.
PubMed=573217; DOI=10.1016/0014-5793(79)81084-4;
Rask L., Anundi H., Peterson P.A.;
"The primary structure of the human retinol-binding protein.";
FEBS Lett. 104:55-58(1979).
[9]
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.
[10]
PARTIAL PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
PubMed=7666002;
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).
[11]
MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=12237133; DOI=10.1016/S0006-291X(02)02212-X;
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]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12716133; DOI=10.1021/pr025574c;
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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
INVOLVEMENT IN RDCCAS.
PubMed=23189188; DOI=10.1371/journal.pone.0050205;
Cukras C., Gaasterland T., Lee P., Gudiseva H.V., Chavali V.R.,
Pullakhandam R., Maranhao B., Edsall L., Soares S., Reddy G.B.,
Sieving P.A., Ayyagari R.;
"Exome analysis identified a novel mutation in the RBP4 gene in a
consanguineous pedigree with retinal dystrophy and developmental
abnormalities.";
PLoS ONE 7:E50205-E50205(2012).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
INVOLVEMENT IN MCOPCB10, VARIANTS MCOPCB10 THR-73 AND THR-75, AND
CHARACTERIZATION OF VARIANTS MCOPCB10 THR-73 AND THR-75.
PubMed=25910211; DOI=10.1016/j.cell.2015.03.006;
Chou C.M., Nelson C., Tarle S.A., Pribila J.T., Bardakjian T.,
Woods S., Schneider A., Glaser T.;
"Biochemical basis for dominant inheritance, variable penetrance, and
maternal effects in RBP4 congenital eye disease.";
Cell 161:634-646(2015).
[17]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
PubMed=6540172;
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).
[18]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=2217163; DOI=10.1002/prot.340080108;
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).
[19]
COMPARISON OF X-RAY STRUCTURES.
PubMed=1623143; DOI=10.1002/bip.360320425;
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).
[20]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH TTR.
PubMed=10052934; DOI=10.1021/bi982291i;
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).
[21]
VARIANTS RDCCAS ASN-59 AND ASP-93.
PubMed=9888420;
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).
[22]
CHARACTERIZATION OF VARIANTS RDCCAS ASN-59 AND ASP-93.
PubMed=10232633;
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).
-!- FUNCTION: Delivers retinol from the liver stores to the peripheral
tissues. In plasma, the RBP-retinol complex interacts with
transthyretin, this prevents its loss by filtration through the
kidney glomeruli. {ECO:0000250|UniProtKB:P04916}.
-!- INTERACTION:
O55245:TTR (xeno); NbExp=2; IntAct=EBI-2116134, EBI-7038226;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12237133}.
-!- MASS SPECTROMETRY: Mass=21063.46; Mass_error=1.88;
Method=Electrospray; Range=17-199;
Evidence={ECO:0000269|PubMed:7666002};
-!- MASS SPECTROMETRY: Mass=20534; Method=MALDI; Range=19-197;
Evidence={ECO:0000269|PubMed:12237133};
-!- MASS SPECTROMETRY: Mass=20162; Method=MALDI; Range=19-194;
Evidence={ECO:0000269|PubMed:12237133};
-!- DISEASE: Retinal dystrophy, iris coloboma, and comedogenic acne
syndrome (RDCCAS) [MIM:615147]: A disease characterized by retinal
degeneration, ocular colobomas involving both the anterior and
posterior segment, impaired night vision and loss of visual
acuity. Additional characteristic features include developmental
abnormalities and severe acne. {ECO:0000269|PubMed:10232633,
ECO:0000269|PubMed:23189188, ECO:0000269|PubMed:9888420}. Note=The
disease is caused by mutations affecting the gene represented in
this entry. Loss of functional RBP4 protein results in serum
retinol deficiency. Lack of normal levels of retinol impairs the
visual cycle leading to night blindness at early stages; prolonged
deficiency may lead to retinal degeneration. Additionally, retinol
deficiency may result in dry skin, increased susceptibility to
infection and acne (PubMed:23189188).
{ECO:0000269|PubMed:23189188}.
-!- DISEASE: Microphthalmia, isolated, with coloboma, 10 (MCOPCB10)
[MIM:616428]: A disorder of eye formation, ranging from small size
of a single eye to complete bilateral absence of ocular tissues.
Ocular abnormalities like opacities of the cornea and lens,
scaring of the retina and choroid, and other abnormalities may
also be present. Ocular colobomas are a set of malformations
resulting from abnormal morphogenesis of the optic cup and stalk,
and the fusion of the fetal fissure (optic fissure).
{ECO:0000269|PubMed:25910211}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF69622.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Mutations of the RBP4 gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/rlbp4mut.htm";
-!- WEB RESOURCE: Name=Wikipedia; Note=Retinol-binding protein 4
entry;
URL="https://en.wikipedia.org/wiki/Retinol_binding_protein_4";
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EMBL; X00129; CAA24959.1; -; mRNA.
EMBL; AL356214; CAH72328.1; -; Genomic_DNA.
EMBL; CH471066; EAW50065.1; -; Genomic_DNA.
EMBL; CH471066; EAW50066.1; -; Genomic_DNA.
EMBL; CH471066; EAW50067.1; -; Genomic_DNA.
EMBL; BC020633; AAH20633.1; -; mRNA.
EMBL; X02775; CAA26553.1; -; Genomic_DNA.
EMBL; X02824; CAB46489.1; -; Genomic_DNA.
EMBL; AF119868; AAF69622.1; ALT_INIT; mRNA.
EMBL; AF025334; AAC02945.1; -; Genomic_DNA.
EMBL; AF025335; AAC02946.1; -; Genomic_DNA.
CCDS; CCDS31249.1; -.
PIR; A93494; VAHU.
RefSeq; NP_001310446.1; NM_001323517.1.
RefSeq; NP_001310447.1; NM_001323518.1.
RefSeq; NP_006735.2; NM_006744.3.
UniGene; Hs.50223; -.
PDB; 1BRP; X-ray; 2.50 A; A=19-200.
PDB; 1BRQ; X-ray; 2.50 A; A=19-200.
PDB; 1JYD; X-ray; 1.70 A; A=19-200.
PDB; 1JYJ; X-ray; 2.00 A; A=19-200.
PDB; 1QAB; X-ray; 3.20 A; E/F=22-201.
PDB; 1RBP; X-ray; 2.00 A; A=19-200.
PDB; 1RLB; X-ray; 3.10 A; E/F=19-192.
PDB; 2WQ9; X-ray; 1.65 A; A=19-192.
PDB; 2WQA; X-ray; 2.85 A; E/F=19-194.
PDB; 2WR6; X-ray; 1.80 A; A=19-192.
PDB; 3BSZ; X-ray; 3.38 A; E/F=19-194.
PDB; 3FMZ; X-ray; 2.90 A; A/B=19-201.
PDB; 4O9S; X-ray; 2.30 A; A/B=19-201.
PDB; 4PSQ; X-ray; 2.40 A; A/B=19-201.
PDBsum; 1BRP; -.
PDBsum; 1BRQ; -.
PDBsum; 1JYD; -.
PDBsum; 1JYJ; -.
PDBsum; 1QAB; -.
PDBsum; 1RBP; -.
PDBsum; 1RLB; -.
PDBsum; 2WQ9; -.
PDBsum; 2WQA; -.
PDBsum; 2WR6; -.
PDBsum; 3BSZ; -.
PDBsum; 3FMZ; -.
PDBsum; 4O9S; -.
PDBsum; 4PSQ; -.
ProteinModelPortal; P02753; -.
SMR; P02753; -.
BioGrid; 111884; 13.
CORUM; P02753; -.
IntAct; P02753; 4.
STRING; 9606.ENSP00000360519; -.
BindingDB; P02753; -.
ChEMBL; CHEMBL3100; -.
DrugBank; DB06985; 2-[({4-[2-(trifluoromethyl)phenyl]piperidin-1-yl}carbonyl)amino]benzoic acid.
DrugBank; DB05076; Fenretinide.
DrugBank; DB03917; N-Ethyl Retinamide.
DrugBank; DB00162; Vitamin A.
GuidetoPHARMACOLOGY; 2549; -.
iPTMnet; P02753; -.
PhosphoSitePlus; P02753; -.
BioMuta; RBP4; -.
DMDM; 62298174; -.
SWISS-2DPAGE; P02753; -.
EPD; P02753; -.
MaxQB; P02753; -.
PaxDb; P02753; -.
PeptideAtlas; P02753; -.
PRIDE; P02753; -.
Ensembl; ENST00000371464; ENSP00000360519; ENSG00000138207.
Ensembl; ENST00000371467; ENSP00000360522; ENSG00000138207.
GeneID; 5950; -.
KEGG; hsa:5950; -.
UCSC; uc001kit.4; human.
CTD; 5950; -.
DisGeNET; 5950; -.
EuPathDB; HostDB:ENSG00000138207.12; -.
GeneCards; RBP4; -.
H-InvDB; HIX0009047; -.
HGNC; HGNC:9922; RBP4.
HPA; CAB004555; -.
HPA; HPA001641; -.
MalaCards; RBP4; -.
MIM; 180250; gene.
MIM; 615147; phenotype.
MIM; 616428; phenotype.
neXtProt; NX_P02753; -.
OpenTargets; ENSG00000138207; -.
Orphanet; 352718; Progressive retinal dystrophy due to retinol transport defect.
PharmGKB; PA34289; -.
eggNOG; ENOG410IJHC; Eukaryota.
eggNOG; ENOG4111K1Y; LUCA.
GeneTree; ENSGT00510000047107; -.
HOVERGEN; HBG004493; -.
InParanoid; P02753; -.
KO; K18271; -.
OMA; GHMSATA; -.
OrthoDB; EOG091G0KIM; -.
PhylomeDB; P02753; -.
TreeFam; TF331445; -.
BioCyc; MetaCyc:ENSG00000138207-MONOMER; -.
Reactome; R-HSA-2453864; Retinoid cycle disease events.
Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
Reactome; R-HSA-6809583; Retinoid metabolism disease events.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
ChiTaRS; RBP4; human.
EvolutionaryTrace; P02753; -.
GeneWiki; Retinol_binding_protein_4; -.
GenomeRNAi; 5950; -.
PRO; PR:P02753; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000138207; -.
CleanEx; HS_RBP4; -.
ExpressionAtlas; P02753; baseline and differential.
Genevisible; P02753; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
GO; GO:0019841; F:retinol binding; IDA:BHF-UCL.
GO; GO:0034632; F:retinol transporter activity; IC:BHF-UCL.
GO; GO:0048738; P:cardiac muscle tissue development; ISS:BHF-UCL.
GO; GO:0048562; P:embryonic organ morphogenesis; ISS:BHF-UCL.
GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; ISS:BHF-UCL.
GO; GO:0048706; P:embryonic skeletal system development; ISS:BHF-UCL.
GO; GO:0001654; P:eye development; IMP:BHF-UCL.
GO; GO:0048807; P:female genitalia morphogenesis; ISS:BHF-UCL.
GO; GO:0006094; P:gluconeogenesis; IMP:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IDA:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0060347; P:heart trabecula formation; ISS:BHF-UCL.
GO; GO:0030324; P:lung development; ISS:BHF-UCL.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IDA:BHF-UCL.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
GO; GO:0051024; P:positive regulation of immunoglobulin secretion; ISS:BHF-UCL.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0042572; P:retinol metabolic process; IMP:BHF-UCL.
GO; GO:0034633; P:retinol transport; IC:BHF-UCL.
GO; GO:0060157; P:urinary bladder development; ISS:BHF-UCL.
GO; GO:0060065; P:uterus development; ISS:BHF-UCL.
GO; GO:0060068; P:vagina development; ISS:BHF-UCL.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR002345; Lipocalin.
InterPro; IPR022271; Lipocalin_ApoD.
InterPro; IPR022272; Lipocalin_CS.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
InterPro; IPR002449; Retinol-bd/Purpurin.
PANTHER; PTHR11873; PTHR11873; 1.
Pfam; PF00061; Lipocalin; 1.
PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
PIRSF; PIRSF500204; RBP_purpurin; 1.
PRINTS; PR00179; LIPOCALIN.
PRINTS; PR01174; RETINOLBNDNG.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Methylation; Microphthalmia;
Reference proteome; Retinol-binding; Secreted; Sensory transduction;
Signal; Transport; Vision; Vitamin A.
SIGNAL 1 18 {ECO:0000269|PubMed:2444024,
ECO:0000269|PubMed:573217,
ECO:0000269|PubMed:6942701}.
CHAIN 19 201 Retinol-binding protein 4.
/FTId=PRO_0000017961.
CHAIN 19 200 Plasma retinol-binding protein(1-182).
/FTId=PRO_0000017962.
CHAIN 19 199 Plasma retinol-binding protein(1-181).
/FTId=PRO_0000017963.
CHAIN 19 197 Plasma retinol-binding protein(1-179).
/FTId=PRO_0000017964.
CHAIN 19 194 Plasma retinol-binding protein(1-176).
/FTId=PRO_0000017965.
BINDING 116 116 Substrate.
{ECO:0000250|UniProtKB:P27485}.
MOD_RES 139 139 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q00724}.
DISULFID 22 178 {ECO:0000269|PubMed:2444024}.
DISULFID 88 192 {ECO:0000269|PubMed:2444024}.
DISULFID 138 147 {ECO:0000269|PubMed:2444024}.
VARIANT 59 59 I -> N (in RDCCAS; dbSNP:rs121918584).
{ECO:0000269|PubMed:10232633,
ECO:0000269|PubMed:9888420}.
/FTId=VAR_009276.
VARIANT 73 73 A -> T (in MCOPCB10; dramatic reduction
in retinol binding; has greater affinity
for the STRA6 receptor;
dbSNP:rs794726862).
{ECO:0000269|PubMed:25910211}.
/FTId=VAR_073856.
VARIANT 75 75 A -> T (in MCOPCB10; dramatic reduction
in retinol binding; has greater affinity
for the STRA6 receptor;
dbSNP:rs794726861).
{ECO:0000269|PubMed:25910211}.
/FTId=VAR_073857.
VARIANT 93 93 G -> D (in RDCCAS; dbSNP:rs121918585).
{ECO:0000269|PubMed:10232633,
ECO:0000269|PubMed:9888420}.
/FTId=VAR_009277.
CONFLICT 8 8 L -> F (in Ref. 4; AAH20633).
{ECO:0000305}.
CONFLICT 13 17 LGSGR -> WAA (in Ref. 1; CAA24959 and 5;
CAA26553). {ECO:0000305}.
HELIX 24 26 {ECO:0000244|PDB:2WQ9}.
HELIX 35 38 {ECO:0000244|PDB:2WQ9}.
STRAND 40 48 {ECO:0000244|PDB:2WQ9}.
STRAND 51 53 {ECO:0000244|PDB:4O9S}.
STRAND 55 65 {ECO:0000244|PDB:2WQ9}.
STRAND 67 69 {ECO:0000244|PDB:1RLB}.
STRAND 71 80 {ECO:0000244|PDB:2WQ9}.
STRAND 82 84 {ECO:0000244|PDB:1JYD}.
STRAND 86 97 {ECO:0000244|PDB:2WQ9}.
STRAND 103 112 {ECO:0000244|PDB:2WQ9}.
STRAND 118 127 {ECO:0000244|PDB:2WQ9}.
STRAND 129 141 {ECO:0000244|PDB:2WQ9}.
STRAND 145 158 {ECO:0000244|PDB:2WQ9}.
HELIX 164 176 {ECO:0000244|PDB:2WQ9}.
TURN 180 182 {ECO:0000244|PDB:1BRP}.
SEQUENCE 201 AA; 23010 MW; 660C6DD8CC9B811A CRC64;
MKWVWALLLL AALGSGRAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP EGLFLQDNIV
AEFSVDETGQ MSATAKGRVR LLNNWDVCAD MVGTFTDTED PAKFKMKYWG VASFLQKGND
DHWIVDTDYD TYAVQYSCRL LNLDGTCADS YSFVFSRDPN GLPPEAQKIV RQRQEELCLA
RQYRLIVHNG YCDGRSERNL L


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