P06911 (LCN5_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Epididymal-specific lipocalin-5, B form
2. Epididymal-specific lipocalin-5, C form

Gene names

Name:	Lcn5
Synonyms:	Erabp

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	188 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Transport
Cellular component	Secreted
Domain	Signal
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lipid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Traceable author statement Ref.1. Source: RGD
Molecular_function	transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.4

Chain

20 – 188

169

Epididymal-specific lipocalin-5, C form

PRO_0000339294

Chain

23 – 188

166

Epididymal-specific lipocalin-5, B form

PRO_0000017869

Amino acid modifications

Disulfide bond

82 ↔ 176

Secondary structure

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188

Helix Strand Turn

Details...

Helix

30 – 33

4

Beta strand

35 – 44

10

Beta strand

59 – 66

8

Beta strand

69 – 78

10

Beta strand

81 – 91

11

Beta strand

97 – 102

6

Beta strand

105 – 114

10

Beta strand

116 – 128

13

Beta strand

131 – 141

11

Helix

147 – 159

13

Helix

164 – 166

3

Beta strand

167 – 169

3

Helix

175 – 182

8

Sequences

	Sequence		Length	Mass (Da)
	P06911 [UniParc]. Last modified August 1, 1992. Version 2. Checksum: 8248BBB4C2D95355	FASTA	188	20,670
	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

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, 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.

IPI

IPI00779451.

PIR

SQRTAD. A43801.

RefSeq

NP_077050.1. NM_024136.1.

UniGene

Rn.10362.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P06911.

SMR

P06911. Positions 23-186.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000058570.

Proteomic databases

PaxDb

P06911.

PRIDE

P06911.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

29552.

KEGG

rno:29552.

UCSC

RGD:69320. rat.

Organism-specific databases

CTD

13863.

RGD

69320. Lcn5.

Phylogenomic databases

eggNOG

euNOG08191.

HOGENOM

HOG000113294.

HOVERGEN

HBG096015.

InParanoid

P06911.

OrthoDB

EOG46Q6TW.

Gene expression databases

Genevestigator

P06911.

GermOnline

ENSRNOG00000017184. Rattus norvegicus.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR01254. PGNDSYNTHASE.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00213. LIPOCALIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06911.

NextBio

609578.

Entry information

Entry name

LCN5_RAT

Accession

Primary (citable) accession number: P06911

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program