P10745 (RET3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Retinol-binding protein 3

Alternative name(s):
Interphotoreceptor retinoid-binding protein
Short name=IRBP
Interstitial retinol-binding protein

Gene names

Name:

RBP3

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	1247 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	IRBP shuttles 11-cis and all trans retinoids between the retinol isomerase in the pigment epithelium and the visual pigments in the photoreceptor cells of the retina.
Subcellular location	Secreted › extracellular space › extracellular matrix › interphotoreceptor matrix. Note: Interphotoreceptor matrix that permeates the space between the retina and the contiguous layer of pigment epithelium cells.
Sequence similarities	Belongs to the peptidase S41A family.
Caution	It is uncertain whether Met-1 or Met-2 is the initiator.
Sequence caution	The sequence AAC18875.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transport
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Vitamin A
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lipid metabolic process Traceable author statement Ref.1. Source: ProtInc proteolysis Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW visual perception Traceable author statement Ref.1. Source: ProtInc
Cellular_component	interphotoreceptor matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	retinal binding Inferred from electronic annotation. Source: UniProtKB-KW retinoid binding Traceable author statement Ref.1. Source: ProtInc serine-type peptidase 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
	Signal peptide	1 – 17	17	Ref.9
	Chain	18 – 1247	1230	Retinol-binding protein 3		PRO_0000021523
Regions
	Repeat	18 – 320	303	1
	Repeat	321 – 630	310	2
	Repeat	631 – 931	301	3
	Repeat	932 – 1230	299	4
	Region	18 – 1230	1213	4 X approximate tandem repeats
Amino acid modifications
	Glycosylation	205	1	N-linked (GlcNAc...) Potential
	Glycosylation	515	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	530	1	R → H in a colorectal cancer sample; somatic mutation. Ref.11		VAR_035929
	Natural variant	884	1	V → M. Corresponds to variant rs11204213 [ dbSNP | Ensembl ].		VAR_051315

Sequences

	Sequence		Length	Mass (Da)
	P10745 [UniParc]. Last modified November 1, 1991. Version 2. Checksum: 6C1841411E012E0F	FASTA	1,247	135,363
	10 20 30 40 50 60 MMREWVLLMS VLLCGLAGPT HLFQPSLVLD MAKVLLDNYC FPENLLGMQE AIQQAIKSHE 70 80 90 100 110 120 ILSISDPQTL ASVLTAGVQS SLNDPRLVIS YEPSTPEPPP QVPALTSLSE EELLAWLQRG 130 140 150 160 170 180 LRHEVLEGNV GYLRVDSVPG QEVLSMMGEF LVAHVWGNLM GTSALVLDLR HCTGGQVSGI 190 200 210 220 230 240 PYIISYLHPG NTILHVDTIY NRPSNTTTEI WTLPQVLGER YGADKDVVVL TSSQTRGVAE 250 260 270 280 290 300 DIAHILKQMR RAIVVGERTG GGALDLRKLR IGESDFFFTV PVSRSLGPLG GGSQTWEGSG 310 320 330 340 350 360 VLPCVGTPAE QALEKALAIL TLRSALPGVV HCLQEVLKDY YTLVDRVPTL LQHLASMDFS 370 380 390 400 410 420 TVVSEEDLVT KLNAGLQAAS EDPRLLVRAI GPTETPSWPA PDAAAEDSPG VAPELPEDEA 430 440 450 460 470 480 IRQALVDSVF QVSVLPGNVG YLRFDSFADA SVLGVLAPYV LRQVWEPLQD TEHLIMDLRH 490 500 510 520 530 540 NPGGPSSAVP LLLSYFQGPE AGPVHLFTTY DRRTNITQEH FSHMELPGPR YSTQRGVYLL 550 560 570 580 590 600 TSHRTATAAE EFAFLMQSLG WATLVGEITA GNLLHTRTVP LLDTPEGSLA LTVPVLTFID 610 620 630 640 650 660 NHGEAWLGGG VVPDAIVLAE EALDKAQEVL EFHQSLGALV EGTGHLLEAH YARPEVVGQT 670 680 690 700 710 720 SALLRAKLAQ GAYRTAVDLE SLASQLTADL QEVSGDHRLL VFHSPGELVV EEAPPPPPAV 730 740 750 760 770 780 PSPEELTYLI EALFKTEVLP GQLGYLRFDA MAELETVKAV GPQLVRLVWQ QLVDTAALVI 790 800 810 820 830 840 DLRYNPGSYS TAIPLLCSYF FEAEPRQHLY SVFDRATSKV TEVWTLPQVA GQRYGSHKDL 850 860 870 880 890 900 YILMSHTSGS AAEAFAHTMQ DLQRATVIGE PTAGGALSVG IYQVGSSPLY ASMPTQMAMS 910 920 930 940 950 960 ATTGKAWDLA GVEPDITVPM SEALSIAQDI VALRAKVPTV LQTAGKLVAD NYASAELGAK 970 980 990 1000 1010 1020 MATKLSGLQS RYSRVTSEVA LAEILGADLQ MLSGDPHLKA AHIPENAKDR IPGIVPMQIP 1030 1040 1050 1060 1070 1080 SPEVFEELIK FSFHTNVLED NIGYLRFDMF GDGELLTQVS RLLVEHIWKK IMHTDAMIID 1090 1100 1110 1120 1130 1140 MRFNIGGPTS SIPILCSYFF DEGPPVLLDK IYSRPDDSVS ELWTHAQVVG ERYGSKKSMV 1150 1160 1170 1180 1190 1200 ILTSSVTAGT AEEFTYIMKR LGRALVIGEV TSGGCQPPQT YHVDDTNLYL TIPTARSVGA 1210 1220 1230 1240 SDGSSWEGVG VTPHVVVPAE EALARAKEML QHNQLRVKRS PGLQDHL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human interstitial retinoid-binding protein. Gene structure and primary structure." Liou G.I., Ma D.-P., Yang Y.-W., Geng L., Zhu C., Baehr W. J. Biol. Chem. 264:8200-8206(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Characterization and comparative structural features of the gene for human interstitial retinol-binding protein." Fong S.-L., Fong W.B., Morris T.A., Kedzie K.M., Bridges C.D.B. J. Biol. Chem. 265:3648-3653(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"Cloning of cDNAs encoding human interphotoreceptor retinoid-binding protein (IRBP) and comparison with bovine IRBP sequences." Si J.S., Borst D.E., Redmond T.M., Nickerson J.M. Gene 80:99-108(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Internal quadruplication in the structure of human interstitial retinol-binding protein deduced from its cloned cDNA." Fong S.-L., Bridges C.D.B. J. Biol. Chem. 263:15330-15334(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[5]	"The DNA sequence and comparative analysis of human chromosome 10." 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. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"Human interstitial retinol-binding protein (IRBP): cloning, partial sequence, and chromosomal localization." Liou G.I., Fong S.-L., Gosden J., van Tuinen P., Ledbetter D.H., Christie S., Rout D., Bhattacharya S., Cook R.G., Li Y., Wang C., Bridges C.D.B. Somat. Cell Mol. Genet. 13:315-323(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-1247.
[8]	"Hypomethylation of the interphotoreceptor retinoid-binding protein (IRBP) promotor and first exon is linked to expression of the gene." Albini A., Toffenetti J., Zhen Z., Chader G.J., Noonan D.M. Nucleic Acids Res. 18:5181-5187(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-382.
[9]	"Interspecies conservation of structure of interphotoreceptor retinoid-binding protein. Similarities and differences as adjudged by peptide mapping and N-terminal sequencing." Redmond T.M., Wiggert B., Robey F.A., Chader G.J. Biochem. J. 240:19-26(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-42.
[10]	"N-terminal sequence homologies in interstitial retinol-binding proteins from 10 vertebrate species." Fong S.-L., Cook R.G., Alvarez R.A., Liou G.I., Landers R.A., Bridges C.D.B. FEBS Lett. 205:309-312(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-39.
[11]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-530.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M33875 , M33864, M33865, M33866 Genomic DNA. Translation: AAA59453.1. M22453 mRNA. Translation: AAA36126.1. J05253 Genomic DNA. Translation: AAC18875.1. Different initiation. AL731561 Genomic DNA. Translation: CAH74045.1. CH471251 Genomic DNA. Translation: EAW50659.1. J03912 mRNA. Translation: AAA59188.1. X53044 Genomic DNA. Translation: CAA37213.1.
IPI	IPI00022337.
PIR	A33812.
RefSeq	NP_002891.1. NM_002900.2.
UniGene	Hs.591928.
3D structure databases
ProteinModelPortal	P10745.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000224600.
Protein family/group databases
MEROPS	S41.950.
PTM databases
PhosphoSite	P10745.
Polymorphism databases
DMDM	124894.
Proteomic databases
PaxDb	P10745.
PRIDE	P10745.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000224600; ENSP00000224600; ENSG00000107618. ENST00000584701; ENSP00000463151; ENSG00000265203.
GeneID	5949.
KEGG	hsa:5949.
UCSC	uc001jez.3. human.
Organism-specific databases
CTD	5949.
GeneCards	GC10M048381.
HGNC	HGNC:9921. RBP3.
MIM	180290. gene.
neXtProt	NX_P10745.
PharmGKB	PA34288.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG76669.
HOGENOM	HOG000139907.
HOVERGEN	HBG006175.
InParanoid	P10745.
OMA	CSYFFDE.
OrthoDB	EOG46T30P.
PhylomeDB	P10745.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000107618-MONOMER.
Gene expression databases
Bgee	P10745.
CleanEx	HS_RBP3.
Genevestigator	P10745.
GermOnline	ENSG00000107618. Homo sapiens.
Family and domain databases
InterPro	IPR024591. Interphotorcpt_retinol-bd_N. IPR005151. Interphotoreceptor_retinol-bd. [Graphical view]
Pfam	PF11918. DUF3436. 1 hit. PF03572. Peptidase_S41. 4 hits. [Graphical view]
SMART	SM00245. TSPc. 4 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P10745.
ChEMBL	CHEMBL2831.
DrugBank	DB00162. Vitamin A.
GenomeRNAi	5949.
NextBio	23178.
SOURCE	Search...

Entry information

Entry name

RET3_HUMAN

Accession

Primary (citable) accession number: P10745
Secondary accession number(s): Q5VSR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1991
Last modified:	May 1, 2013
This is version 117 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.