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Protein

Retinol-binding protein 5

Gene

RBP5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Intracellular transport of retinol.1 Publication

GO - Molecular functioni

  • retinal binding Source: UniProtKB-KW
  • retinoid binding Source: UniProtKB
  • retinol binding Source: UniProtKB-KW
  • transporter activity Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Names & Taxonomyi

Protein namesi
Recommended name:
Retinol-binding protein 5
Alternative name(s):
Cellular retinol-binding protein III
Short name:
CRBP-III
HRBPiso
Gene namesi
Name:RBP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:15847. RBP5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164742366.

Chemistry

DrugBankiDB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRBP5.
DMDMi14916691.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 135134Retinol-binding protein 5PRO_0000067400Add
BLAST

Proteomic databases

EPDiP82980.
PaxDbiP82980.
PRIDEiP82980.
TopDownProteomicsiP82980.

Expressioni

Tissue specificityi

Higher expression in adult kidney and liver and to a lesser extent in adult and fetal spleen, adult lymph nodes and appendix, and fetal liver and kidney. Strongly decreased in hepatocellular carcinoma tissues (at protein level).2 Publications

Gene expression databases

BgeeiP82980.
CleanExiHS_RBP5.
ExpressionAtlasiP82980. baseline and differential.
GenevisibleiP82980. HS.

Organism-specific databases

HPAiHPA038723.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNDBP1O952733EBI-3941274,EBI-748961

Protein-protein interaction databases

BioGridi123759. 4 interactions.
IntActiP82980. 3 interactions.
STRINGi9606.ENSP00000266560.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 159Combined sources
Helixi17 – 237Combined sources
Turni28 – 336Combined sources
Helixi34 – 363Combined sources
Beta strandi40 – 456Combined sources
Beta strandi47 – 559Combined sources
Beta strandi61 – 666Combined sources
Beta strandi71 – 744Combined sources
Turni76 – 794Combined sources
Beta strandi82 – 898Combined sources
Beta strandi91 – 10212Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi115 – 1228Combined sources
Beta strandi125 – 1339Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GGLX-ray2.31A/B2-134[»]
ProteinModelPortaliP82980.
SMRiP82980. Positions 2-134.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP82980.

Family & Domainsi

Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP82980.
OMAiKRNRGWR.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP82980.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031270. CRBP-III.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF74. PTHR11955:SF74. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P82980-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPNLTGYYR FVSQKNMEDY LQALNISLAV RKIALLLKPD KEIEHQGNHM
60 70 80 90 100
TVRTLSTFRN YTVQFDVGVE FEEDLRSVDG RKCQTIVTWE EEHLVCVQKG
110 120 130
EVPNRGWRHW LEGEMLYLEL TARDAVCEQV FRKVR
Length:135
Mass (Da):15,931
Last modified:January 23, 2007 - v3
Checksum:iB9D059DCCC0A88ED
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191D → N.
Corresponds to variant rs10963 [ dbSNP | Ensembl ].
VAR_049013
Natural varianti70 – 701E → Q.
Corresponds to variant rs7969705 [ dbSNP | Ensembl ].
VAR_034445
Natural varianti115 – 1151M → L.2 Publications
Corresponds to variant rs2290237 [ dbSNP | Ensembl ].
VAR_034446

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007436 mRNA. Translation: AAG09617.1.
AF212239 mRNA. Translation: AAK14925.1.
AK311977 mRNA. Translation: BAG34916.1.
AK223378 mRNA. Translation: BAD97098.1.
BC029355 mRNA. Translation: AAH29355.1.
CCDSiCCDS8574.1.
RefSeqiNP_113679.1. NM_031491.2.
XP_011519166.1. XM_011520864.1.
UniGeneiHs.246046.

Genome annotation databases

EnsembliENST00000266560; ENSP00000266560; ENSG00000139194.
GeneIDi83758.
KEGGihsa:83758.
UCSCiuc001qsq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007436 mRNA. Translation: AAG09617.1.
AF212239 mRNA. Translation: AAK14925.1.
AK311977 mRNA. Translation: BAG34916.1.
AK223378 mRNA. Translation: BAD97098.1.
BC029355 mRNA. Translation: AAH29355.1.
CCDSiCCDS8574.1.
RefSeqiNP_113679.1. NM_031491.2.
XP_011519166.1. XM_011520864.1.
UniGeneiHs.246046.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GGLX-ray2.31A/B2-134[»]
ProteinModelPortaliP82980.
SMRiP82980. Positions 2-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123759. 4 interactions.
IntActiP82980. 3 interactions.
STRINGi9606.ENSP00000266560.

Chemistry

DrugBankiDB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRBP5.
DMDMi14916691.

Proteomic databases

EPDiP82980.
PaxDbiP82980.
PRIDEiP82980.
TopDownProteomicsiP82980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266560; ENSP00000266560; ENSG00000139194.
GeneIDi83758.
KEGGihsa:83758.
UCSCiuc001qsq.4. human.

Organism-specific databases

CTDi83758.
GeneCardsiRBP5.
HGNCiHGNC:15847. RBP5.
HPAiHPA038723.
MIMi611866. gene.
neXtProtiNX_P82980.
PharmGKBiPA164742366.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP82980.
OMAiKRNRGWR.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP82980.
TreeFamiTF316894.

Miscellaneous databases

ChiTaRSiRBP5. human.
EvolutionaryTraceiP82980.
GenomeRNAii83758.
NextBioi72791.
PROiP82980.
SOURCEiSearch...

Gene expression databases

BgeeiP82980.
CleanExiHS_RBP5.
ExpressionAtlasiP82980. baseline and differential.
GenevisibleiP82980. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031270. CRBP-III.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF74. PTHR11955:SF74. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, retinoid binding and X-ray analysis of a human retinol-binding protein."
    Folli C., Calderone V., Ottonello S., Bolchi A., Zanotti G., Stoppini M., Berni R.
    Proc. Natl. Acad. Sci. U.S.A. 98:3710-3715(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, TISSUE SPECIFICITY.
  2. "A novel gene expressed in human liver non-tumor tissues."
    Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  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], VARIANT LEU-115.
    Tissue: Small intestine.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-115.
    Tissue: Spleen.
  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: Kidney.
  6. "Down-regulation of retinol binding protein 5 is associated with aggressive tumor features in hepatocellular carcinoma."
    Ho J.C.Y., Cheung S.T., Poon W.S., Lee Y.T., Ng I.O.L., Fan S.T.
    J. Cancer Res. Clin. Oncol. 133:929-936(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRET5_HUMAN
AccessioniPrimary (citable) accession number: P82980
Secondary accession number(s): Q53FB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.