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Protein

Retinol-binding protein 4

Gene

RBP4

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Names & Taxonomyi

Protein namesi
Recommended name:
Retinol-binding protein 4
Alternative name(s):
Plasma retinol-binding protein
Short name:
PRBP
Short name:
RBP
Gene namesi
Name:RBP4
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 201183Retinol-binding protein 4PRO_0000017968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 178
Disulfide bondi88 ↔ 192
Disulfide bondi138 ↔ 147

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP27485.
PeptideAtlasiP27485.

Expressioni

Developmental stagei

Produced between days 10 and 15 of pregnancy and at day 15 found in both the peri-implantation conceptus (trophectoderm and yolk sac) and the endometrial surface and glandular epithelium. Found in allantoic fluid at day 30 of gestation.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011168.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Helixi35 – 384Combined sources
Beta strandi40 – 489Combined sources
Beta strandi51 – 533Combined sources
Beta strandi55 – 6511Combined sources
Beta strandi71 – 8010Combined sources
Beta strandi86 – 9712Combined sources
Beta strandi103 – 11210Combined sources
Beta strandi118 – 12710Combined sources
Beta strandi129 – 14113Combined sources
Beta strandi145 – 15814Combined sources
Helixi164 – 17613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQBX-ray1.65A19-201[»]
ProteinModelPortaliP27485.
SMRiP27485. Positions 19-193.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27485.

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJHC. Eukaryota.
ENOG4111K1Y. LUCA.
HOGENOMiHOG000293156.
HOVERGENiHBG004493.
InParanoidiP27485.
KOiK18271.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002449. Retinol-bd/Purpurin.
[Graphical view]
PANTHERiPTHR11873. PTHR11873. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFiPIRSF036893. Lipocalin_ApoD. 1 hit.
PIRSF500204. RBP_purpurin. 1 hit.
PRINTSiPR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P27485-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEWVWALVLL AALGSAQAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP
60 70 80 90 100
EGLFLQDNIV AEFSVDENGH MSATAKGRVR LLNNWDVCAD MVGTFTDTED
110 120 130 140 150
PAKFKMKYWG VASFLQKGND DHWIIDTDYD TYAVQYSCRL QNLDGTCADS
160 170 180 190 200
YSFVFARDPH GFSPEVQKIV RQRQEELCLA RQYRIITHNG YCDGKSERNI

L
Length:201
Mass (Da):23,067
Last modified:July 15, 1998 - v2
Checksum:iA20E39D3C9471DC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341V → A in AAA31113 (PubMed:1723146).Curated
Sequence conflicti185 – 1851I → L in AAA31113 (PubMed:1723146).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68860 mRNA. Translation: AAA31113.1.
PIRiA39486.
RefSeqiNP_999222.1. NM_214057.1.
UniGeneiSsc.15695.

Genome annotation databases

GeneIDi397124.
KEGGissc:397124.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68860 mRNA. Translation: AAA31113.1.
PIRiA39486.
RefSeqiNP_999222.1. NM_214057.1.
UniGeneiSsc.15695.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQBX-ray1.65A19-201[»]
ProteinModelPortaliP27485.
SMRiP27485. Positions 19-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011168.

Proteomic databases

PaxDbiP27485.
PeptideAtlasiP27485.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397124.
KEGGissc:397124.

Organism-specific databases

CTDi5950.

Phylogenomic databases

eggNOGiENOG410IJHC. Eukaryota.
ENOG4111K1Y. LUCA.
HOGENOMiHOG000293156.
HOVERGENiHBG004493.
InParanoidiP27485.
KOiK18271.

Miscellaneous databases

EvolutionaryTraceiP27485.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002449. Retinol-bd/Purpurin.
[Graphical view]
PANTHERiPTHR11873. PTHR11873. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFiPIRSF036893. Lipocalin_ApoD. 1 hit.
PIRSF500204. RBP_purpurin. 1 hit.
PRINTSiPR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The retinol-binding protein of the expanding pig blastocyst: molecular cloning and expression in trophectoderm and embryonic disc."
    Trout W.E., McDonnell J.J., Kramer K.K., Baumbach G.A., Roberts R.M.
    Mol. Endocrinol. 5:1533-1540(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Retinol-binding protein: a major secretory product of the pig conceptus."
    Harney J.P., Mirando M.A., Smith L.C., Bazer F.W.
    Biol. Reprod. 42:523-532(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-51, DEVELOPMENTAL STAGE.
  3. "Structure of pig plasma retinol-binding protein at 1.65-A resolution."
    Zanotti G., Panzalorto M., Marcato A., Malpeli G., Folli C., Berni R.
    Acta Crystallogr. D 54:1049-1052(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), SEQUENCE REVISION TO 134 AND 185.

Entry informationi

Entry nameiRET4_PIG
AccessioniPrimary (citable) accession number: P27485
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 15, 1998
Last modified: July 6, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.