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P06911 (LCN5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epididymal-specific lipocalin-5
Alternative name(s):
Androgen-dependent epididymal 18.5 kDa protein
Epididymal retinoic acid-binding protein
Short name=E-RABP
Epididymal secretory protein I
Short name=ESP-I
Gene names
Name:Lcn5
Synonyms:Erabp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Associates with spermatozoa in the epididymal fluid but does not bind tightly to them. Binds both all-trans and 9-cis retinoic acid. May act as a retinoid carrier protein which is required for epididymal function and/or sperm maturation.

Subcellular location

Secreted. Note: Synthesized in the proximal part of the epididymis and secreted into the epididymal fluid.

Tissue specificity

Synthesized exclusively in the proximal part (caput epididymidis) of the epididymis. It makes up a substantial part of the total protein in the epididymal luminal fluid and binds to the sperm membrane.

Post-translational modification

There are two similar, immunologically cross-reacting forms of this protein, designated B and C, which probably result from different processing of the amino end.

The N-terminus of form C is probably blocked.

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentSecreted
   DomainSignal
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processlipid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Traceable author statement Ref.1. Source: RGD

   Molecular_functiontransporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.4
Chain20 – 188169Epididymal-specific lipocalin-5, C form
PRO_0000339294
Chain23 – 188166Epididymal-specific lipocalin-5, B form
PRO_0000017869

Amino acid modifications

Disulfide bond82 ↔ 176

Secondary structure

.......................... 188
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06911 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: 8248BBB4C2D95355

FASTA18820,670
        10         20         30         40         50         60 
MENIMPFALL GLCVGLAAGT EGAVVKDFDI SKFLGFWYEI AFASKMGTPG LAHKEEKMGA 

        70         80         90        100        110        120 
MVVELKENLL ALTTTYYSED HCVLEKVTAT EGDGPAKFQV TRLSGKKEVV VEATDYLTYA 

       130        140        150        160        170        180 
IIDITSLVAG AVHRTMKLYS RSLDDNGEAL YNFRKITSDH GFSETDLYIL KHDLTCVKVL 


QSAAESRP 

« Hide

References

[1]"An 18-kDa androgen-regulated protein that modifies galactosyltransferase activity is synthesized by the rat caput epididymidis, but has no structural similarity to rat milk alphalactalbumin."
Moore A., Hall L., Hamilton D.W.
Biol. Reprod. 43:497-506(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Epididymis.
[2]"Structure and expression of the rat epididymal secretory protein I gene. An androgen-regulated member of the lipocalin superfamily with a rare splice donor site."
Girotti M., Jones R., Emery D.C., Chia W., Hall L.
Biochem. J. 281:203-210(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
[3]"Molecular cloning of the cDNA for two major androgen-dependent secretory proteins of 18.5 kilodaltons synthesized by the rat epididymis."
Brooks D.E., Means A.R., Wright E.J., Singh S.P., Tiver K.K.
J. Biol. Chem. 261:4956-4961(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-188, PROTEIN SEQUENCE OF 23-40.
[4]"Purification and crystallization of a retinoic acid-binding protein from rat epididymis. Identity with the major androgen-dependent epididymal proteins."
Newcomer M.E., Ong D.E.
J. Biol. Chem. 265:12876-12879(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-47, CHARACTERIZATION.
[5]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 58-66, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
[6]"Structure of the epididymal retinoic acid binding protein at 2.1-A resolution."
Newcomer M.E.
Structure 1:7-18(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59831 Genomic DNA. Translation: CAA42493.1.
X59832 mRNA. Translation: CAA42494.1.
M12790 mRNA. Translation: AAA41127.1.
PIRSQRTAD. A43801.
RefSeqNP_077050.1. NM_024136.1.
UniGeneRn.10362.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EPAX-ray2.10A/B23-186[»]
1EPBX-ray2.20A/B23-186[»]
ProteinModelPortalP06911.
SMRP06911. Positions 23-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000058570.

Proteomic databases

PaxDbP06911.
PRIDEP06911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29552.
KEGGrno:29552.
UCSCRGD:69320. rat.

Organism-specific databases

CTD13863.
RGD69320. Lcn5.

Phylogenomic databases

eggNOGeuNOG08191.
HOGENOMHOG000113294.
HOVERGENHBG096015.
InParanoidP06911.
PhylomeDBP06911.
TreeFamTF336103.

Gene expression databases

GenevestigatorP06911.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR01254. PGNDSYNTHASE.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06911.
NextBio609578.

Entry information

Entry nameLCN5_RAT
AccessionPrimary (citable) accession number: P06911
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references