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Protein

Epididymal-specific lipocalin-5

Gene

Lcn5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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 13-cis retinoic acid. May act as a retinoid carrier protein which is required for epididymal function and/or sperm maturation.2 Publications

GO - Molecular functioni

  • retinoid binding Source: MGI
  • small molecule binding Source: InterPro
  • transporter activity Source: InterPro

GO - Biological processi

  • retinoic acid metabolic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Epididymal-specific lipocalin-5
Alternative name(s):
Epididymal retinoic acid-binding protein
Short name:
E-RABP
Short name:
mE-RABP
Epididymal secretory protein 10
Short name:
MEP 10
Cleaved into the following 2 chains:
Gene namesi
Name:Lcn5Imported
Synonyms:Mep10Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1277241. Lcn5.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 192166Epididymal-specific lipocalin-5, major form1 PublicationPRO_0000339292Add
BLAST
Chaini30 – 192163Epididymal-specific lipocalin-5, minor form1 PublicationPRO_0000339293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi89 ↔ 183By similarity

Post-translational modificationi

2 different forms with differently processed N-termini exist.

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiA2AJB7.
PRIDEiA2AJB7.

Expressioni

Tissue specificityi

Epididymal fluid of the caudal and corpus regions (at protein level).1 Publication

Inductioni

Down-regulated to 11% of control levels 5 days after castration and is not detectable by 20 days (at protein level). Levels are partially restored by subsequent testosterone treatment.1 Publication

Gene expression databases

BgeeiA2AJB7.
GenevisibleiA2AJB7. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028306.

Structurei

3D structure databases

ProteinModelPortaliA2AJB7.
SMRiA2AJB7. Positions 30-190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J0UJ. Eukaryota.
ENOG411140G. LUCA.
GeneTreeiENSGT00440000034507.
HOGENOMiHOG000113294.
HOVERGENiHBG096015.
InParanoidiA2AJB7.
OMAiPVENNIR.
OrthoDBiEOG78H3VX.
PhylomeDBiA2AJB7.
TreeFamiTF336103.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00179. LIPOCALIN.
PR01254. PGNDSYNTHASE.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: A2AJB7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MCSVARHMES IMLFTLLGLC VGLAAGTEAA VVKDFDVNKF LGFWYEIALA
60 70 80 90 100
SKMGAYGLAH KEEKMGAMVV ELKENLLALT TTYYNEGHCV LEKVAATQVD
110 120 130 140 150
GSAKYKVTRI SGEKEVVVVA TDYMTYTVID ITSLVAGAVH RAMKLYSRSL
160 170 180 190
DNNGEALNNF QKIALKHGFS ETDIHILKHD LTCVNALQSG QI
Length:192
Mass (Da):21,013
Last modified:February 20, 2007 - v1
Checksum:iE91DA019DEF21F5B
GO
Isoform 21 Publication (identifier: A2AJB7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     181-192: LTCVNALQSGQI → YIEIKALPKPGS

Note: No experimental confirmation available.Curated
Show »
Length:192
Mass (Da):21,082
Checksum:iA5479B265E421F5C
GO
Isoform 31 Publication (identifier: A2AJB7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     181-192: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:180
Mass (Da):19,785
Checksum:i4C4FD80BA08429DF
GO
Isoform 41 Publication (identifier: A2AJB7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MCSVARHMESIMLFTLLGLCVGLAAGTEA → M

Show »
Length:164
Mass (Da):18,137
Checksum:i0D82734C4E603F5A
GO

Sequence cautioni

The sequence AAD09351.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929MCSVA…AGTEA → M in isoform 4. 1 PublicationVSP_052838Add
BLAST
Alternative sequencei181 – 19212LTCVN…QSGQI → YIEIKALPKPGS in isoform 2. 1 PublicationVSP_052839Add
BLAST
Alternative sequencei181 – 19212Missing in isoform 3. 1 PublicationVSP_052840Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68546 mRNA. Translation: AAC24316.1.
U68381 Genomic DNA. Translation: AAD09351.1. Different initiation.
AK136629 mRNA. Translation: BAE23077.1.
AK162355 mRNA. Translation: BAE36871.1.
AL732590 Genomic DNA. Translation: CAM25179.1.
AL732590 Genomic DNA. Translation: CAM25180.1.
AL732590 Genomic DNA. Translation: CAM25181.1.
CCDSiCCDS38078.1. [A2AJB7-3]
CCDS38079.1. [A2AJB7-1]
CCDS71003.1. [A2AJB7-2]
RefSeqiNP_001036095.1. NM_001042630.2. [A2AJB7-3]
NP_001263186.1. NM_001276257.1. [A2AJB7-2]
NP_031973.2. NM_007947.3. [A2AJB7-1]
UniGeneiMm.12867.

Genome annotation databases

EnsembliENSMUST00000028306; ENSMUSP00000028306; ENSMUSG00000026937. [A2AJB7-1]
ENSMUST00000100312; ENSMUSP00000097887; ENSMUSG00000026937. [A2AJB7-2]
ENSMUST00000100313; ENSMUSP00000097888; ENSMUSG00000026937. [A2AJB7-3]
GeneIDi13863.
KEGGimmu:13863.
UCSCiuc008itb.2. mouse. [A2AJB7-1]
uc033hlx.1. mouse. [A2AJB7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68546 mRNA. Translation: AAC24316.1.
U68381 Genomic DNA. Translation: AAD09351.1. Different initiation.
AK136629 mRNA. Translation: BAE23077.1.
AK162355 mRNA. Translation: BAE36871.1.
AL732590 Genomic DNA. Translation: CAM25179.1.
AL732590 Genomic DNA. Translation: CAM25180.1.
AL732590 Genomic DNA. Translation: CAM25181.1.
CCDSiCCDS38078.1. [A2AJB7-3]
CCDS38079.1. [A2AJB7-1]
CCDS71003.1. [A2AJB7-2]
RefSeqiNP_001036095.1. NM_001042630.2. [A2AJB7-3]
NP_001263186.1. NM_001276257.1. [A2AJB7-2]
NP_031973.2. NM_007947.3. [A2AJB7-1]
UniGeneiMm.12867.

3D structure databases

ProteinModelPortaliA2AJB7.
SMRiA2AJB7. Positions 30-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028306.

Proteomic databases

PaxDbiA2AJB7.
PRIDEiA2AJB7.

Protocols and materials databases

DNASUi13863.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028306; ENSMUSP00000028306; ENSMUSG00000026937. [A2AJB7-1]
ENSMUST00000100312; ENSMUSP00000097887; ENSMUSG00000026937. [A2AJB7-2]
ENSMUST00000100313; ENSMUSP00000097888; ENSMUSG00000026937. [A2AJB7-3]
GeneIDi13863.
KEGGimmu:13863.
UCSCiuc008itb.2. mouse. [A2AJB7-1]
uc033hlx.1. mouse. [A2AJB7-2]

Organism-specific databases

CTDi13863.
MGIiMGI:1277241. Lcn5.

Phylogenomic databases

eggNOGiENOG410J0UJ. Eukaryota.
ENOG411140G. LUCA.
GeneTreeiENSGT00440000034507.
HOGENOMiHOG000113294.
HOVERGENiHBG096015.
InParanoidiA2AJB7.
OMAiPVENNIR.
OrthoDBiEOG78H3VX.
PhylomeDBiA2AJB7.
TreeFamiTF336103.

Miscellaneous databases

NextBioi284750.
PROiA2AJB7.
SOURCEiSearch...

Gene expression databases

BgeeiA2AJB7.
GenevisibleiA2AJB7. MM.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00179. LIPOCALIN.
PR01254. PGNDSYNTHASE.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and hormonal regulation of a murine epididymal retinoic acid-binding protein messenger ribonucleic acid."
    Lareyre J.-J., Zheng W.-L., Zhao G.-Q., Kasper S., Newcomer M.E., Matusik R.J., Ong D.E., Orgebin-Crist M.-C.
    Endocrinology 139:2971-2981(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), INDUCTION.
    Strain: SWR/J1 Publication.
  2. "Genomic organization and chromosomal localization of the murine epididymal retinoic acid-binding protein (mE-RABP) gene."
    Lareyre J.-J., Mattei M.-G., Kasper S., Ong D.E., Matusik R.J., Orgebin-Crist M.-C.
    Mol. Reprod. Dev. 50:387-395(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
    Strain: 129Imported.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6JImported.
    Tissue: EpididymisImported.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "Isolation, immunolocalization, and sperm-association of three proteins of 18, 25, and 29 kilodaltons secreted by the mouse epididymis."
    Rankin T.L., Tsuruta K.J., Holland M.K., Griswold M.D., Orgebin-Crist M.-C.
    Biol. Reprod. 46:747-766(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-39, FUNCTION, SUBCELLULAR LOCATION.
    Strain: C57BL/6J1 Publication.
  6. "Secretion and transport of mouse epididymal proteins after injection of 35S-methionine."
    Vreeburg J.T.M., Holland M.K., Cornwall G.A., Orgebin-Crist M.-C.
    Biol. Reprod. 43:113-120(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "The 18-kDa mouse epididymal protein (MEP 10) binds retinoic acid."
    Rankin T.L., Ong D.E., Orgebin-Crist M.-C.
    Biol. Reprod. 46:767-771(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Profiling and imaging proteins in the mouse epididymis by imaging mass spectrometry."
    Chaurand P., Fouchecourt S., DaGue B.B., Xu B.J., Reyzer M.L., Orgebin-Crist M.-C., Caprioli R.M.
    Proteomics 3:2221-2239(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiLCN5_MOUSE
AccessioniPrimary (citable) accession number: A2AJB7
Secondary accession number(s): O88787
, Q3TS05, Q3UW42, Q9R2C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: February 20, 2007
Last modified: May 11, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.