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Reviewed, UniProtKB/Swiss-Prot P27485 (RET4_PIG)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Retinol-binding protein 4
Alternative name(s):
    Plasma retinol-binding protein
      Short name=PRBP
      Short name=RBP
Gene names
Name: RBP4
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

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.

Subcellular location

Secreted.

Developmental stage

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. Ref.2

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

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Ontologies

Keywords
   Biological processTransport
   Cellular componentSecreted
   DomainSignal
   LigandRetinol-binding
Vitamin A
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processtransport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionretinal binding

Inferred from electronic annotation. Source: UniProtKB-KW

retinol binding

Inferred from electronic annotation. Source: UniProtKB-KW

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.2
Chain19 – 201183Retinol-binding protein 4
PRO_0000017968

Amino acid modifications

Disulfide bond22 ↔ 178
Disulfide bond88 ↔ 192
Disulfide bond138 ↔ 147

Experimental info

Sequence conflict1341V → A in AAA31113. Ref.1
Sequence conflict1851I → L in AAA31113. Ref.1

Secondary structure

1 ......................... 201
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P27485-1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: A20E39D3C9471DC8

FASTA20123,067
        10         20         30         40         50         60 
MEWVWALVLL AALGSAQAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP EGLFLQDNIV 

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

       130        140        150        160        170        180 
DHWIIDTDYD TYAVQYSCRL QNLDGTCADS YSFVFARDPH GFSPEVQKIV RQRQEELCLA 

       190        200 
RQYRIITHNG YCDGKSERNI L

« Hide

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References

[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: 1723146] [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: 2340335] [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: 9757135] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), SEQUENCE REVISION TO 134 AND 185.

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Cross-references

Sequence databases

M68860 mRNA. Translation: AAA31113.1.
PIRA39486.
RefSeqNP_999222.1.
UniGeneSsc.15695

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AQBX-ray1.65A19-201[»]
ModBaseSearch...

Genome annotation databases

GeneID397124.
KEGGssc:397124.

Phylogenomic databases

HOVERGENP27485.

Family and domain databases

InterProIPR012674. Calycin.
IPR002345. Lipocalin.
IPR000566. Lipocln_cytFABP.
IPR002449. Retinol_bd.
[Graphical view]
Gene3DG3DSA:2.40.128.20. Calycin. 1 hit.
PANTHERPTHR11873. Retinol_bd. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameRET4_PIG
AccessionPrimary (citable) accession number: P27485
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 15, 1998
Last modified: June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents