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P06911

- LCN5_RAT

UniProt

P06911 - LCN5_RAT

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Protein

Epididymal-specific lipocalin-5

Gene

Lcn5

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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: Unplaced

Organism-specific databases

RGDi69320. Lcn5.

Subcellular locationi

Secreted
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 – 334
Beta strandi35 – 4410
Beta strandi59 – 668
Beta strandi69 – 7810
Beta strandi81 – 9111
Beta strandi97 – 1026
Beta strandi105 – 11410
Beta strandi116 – 12813
Beta strandi131 – 14111
Helixi147 – 15913
Helixi164 – 1663
Beta strandi167 – 1693
Helixi175 – 1828

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
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.
UniGeneiRn.10362.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59831 Genomic DNA. Translation: CAA42493.1 .
X59832 mRNA. Translation: CAA42494.1 .
M12790 mRNA. Translation: AAA41127.1 .
PIRi A43801. SQRTAD.
RefSeqi NP_077050.1. NM_024136.1.
UniGenei Rn.10362.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EPA X-ray 2.10 A/B 23-186 [» ]
1EPB X-ray 2.20 A/B 23-186 [» ]
ProteinModelPortali P06911.
SMRi P06911. Positions 23-186.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000058570.

Proteomic databases

PaxDbi P06911.
PRIDEi P06911.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29552.
KEGGi rno:29552.
UCSCi RGD:69320. rat.

Organism-specific databases

CTDi 13863.
RGDi 69320. Lcn5.

Phylogenomic databases

eggNOGi euNOG08191.
HOGENOMi HOG000113294.
HOVERGENi HBG096015.
InParanoidi P06911.
PhylomeDBi P06911.
TreeFami TF336103.

Miscellaneous databases

EvolutionaryTracei P06911.
NextBioi 609578.

Gene expression databases

Genevestigatori P06911.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR012674. Calycin.
IPR011038. Calycin-like.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view ]
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PRINTSi PR01254. PGNDSYNTHASE.
SUPFAMi SSF50814. SSF50814. 1 hit.
PROSITEi PS00213. LIPOCALIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 1, 2014
This is version 120 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