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Protein

Epididymal-specific lipocalin-5

Gene

Lcn5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. transporter activity Source: InterPro

GO - Biological processi

  1. lipid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following 2 chains:
Gene namesi
Name:Lcn5
Synonyms:Erabp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69320. Lcn5.

Subcellular locationi

  1. Secreted

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

GO - Cellular componenti

  1. extracellular region Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 188169Epididymal-specific lipocalin-5, C formPRO_0000339294Add
BLAST
Chaini23 – 188166Epididymal-specific lipocalin-5, B formPRO_0000017869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi82 ↔ 176

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP06911.
PRIDEiP06911.

Expressioni

Tissue specificityi

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.

Gene expression databases

GenevestigatoriP06911.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000058570.

Structurei

Secondary structure

1
188
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 334Combined sources
Beta strandi35 – 4410Combined sources
Beta strandi59 – 668Combined sources
Beta strandi69 – 7810Combined sources
Beta strandi81 – 9111Combined sources
Beta strandi97 – 1026Combined sources
Beta strandi105 – 11410Combined sources
Beta strandi116 – 12813Combined sources
Beta strandi131 – 14111Combined sources
Helixi147 – 15913Combined sources
Helixi164 – 1663Combined sources
Beta strandi167 – 1693Combined sources
Helixi175 – 1828Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EPAX-ray2.10A/B23-186[»]
1EPBX-ray2.20A/B23-186[»]
ProteinModelPortaliP06911.
SMRiP06911. Positions 23-186.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06911.

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGieuNOG08191.
HOGENOMiHOG000113294.
HOVERGENiHBG096015.
InParanoidiP06911.
PhylomeDBiP06911.
TreeFamiTF336103.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01254. PGNDSYNTHASE.
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.

P06911-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENIMPFALL GLCVGLAAGT EGAVVKDFDI SKFLGFWYEI AFASKMGTPG
60 70 80 90 100
LAHKEEKMGA MVVELKENLL ALTTTYYSED HCVLEKVTAT EGDGPAKFQV
110 120 130 140 150
TRLSGKKEVV VEATDYLTYA IIDITSLVAG AVHRTMKLYS RSLDDNGEAL
160 170 180
YNFRKITSDH GFSETDLYIL KHDLTCVKVL QSAAESRP
Length:188
Mass (Da):20,670
Last modified:August 1, 1992 - v2
Checksum:i8248BBB4C2D95355
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59831 Genomic DNA. Translation: CAA42493.1.
X59832 mRNA. Translation: CAA42494.1.
M12790 mRNA. Translation: AAA41127.1.
PIRiA43801. SQRTAD.
RefSeqiNP_077050.1. NM_024136.1.
XP_008759802.1. XM_008761580.1.
UniGeneiRn.10362.

Genome annotation databases

GeneIDi29552.
KEGGirno:29552.
UCSCiRGD:69320. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59831 Genomic DNA. Translation: CAA42493.1.
X59832 mRNA. Translation: CAA42494.1.
M12790 mRNA. Translation: AAA41127.1.
PIRiA43801. SQRTAD.
RefSeqiNP_077050.1. NM_024136.1.
XP_008759802.1. XM_008761580.1.
UniGeneiRn.10362.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EPAX-ray2.10A/B23-186[»]
1EPBX-ray2.20A/B23-186[»]
ProteinModelPortaliP06911.
SMRiP06911. Positions 23-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000058570.

Proteomic databases

PaxDbiP06911.
PRIDEiP06911.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29552.
KEGGirno:29552.
UCSCiRGD:69320. rat.

Organism-specific databases

CTDi13863.
RGDi69320. Lcn5.

Phylogenomic databases

eggNOGieuNOG08191.
HOGENOMiHOG000113294.
HOVERGENiHBG096015.
InParanoidiP06911.
PhylomeDBiP06911.
TreeFamiTF336103.

Miscellaneous databases

EvolutionaryTraceiP06911.
NextBioi609578.
PROiP06911.

Gene expression databases

GenevestigatoriP06911.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01254. PGNDSYNTHASE.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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).

Entry informationi

Entry nameiLCN5_RAT
AccessioniPrimary (citable) accession number: P06911
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: August 1, 1992
Last modified: April 29, 2015
This is version 123 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

External Data

Dasty 3

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 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.