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P31025 (LCN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Lipocalin-1
Alternative name(s):
Tear lipocalin
Short name=Tlc
Tear prealbumin
Short name=TP
Von Ebner gland protein
Short name=VEG protein
Gene names
Name:LCN1
Synonyms:VEGP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Could play a role in taste reception. Could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. Exhibits an extremely wide ligand pocket.

Subunit structure

Homodimer By similarity. Binds to LMBR1L which may mediate its endocytosis. Ref.9 Ref.10

Subcellular location

Secreted.

Tissue specificity

Mainly expressed in lachrymal and salivary glands. Also expressed in the prostate.

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.8
Chain19 – 176158Lipocalin-1
PRO_0000017974

Amino acid modifications

Disulfide bond79 ↔ 171

Secondary structure

........................ 176
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31025 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 0DDBF124C8C78CB8

FASTA17619,250
        10         20         30         40         50         60 
MKPLLLAVSL GLIAALQAHH LLASDEEIQD VSGTWYLKAM TVDREFPEMN LESVTPMTLT 

        70         80         90        100        110        120 
TLEGGNLEAK VTMLISGRCQ EVKAVLEKTD EPGKYTADGG KHVAYIIRSH VKDHYIFYCE 

       130        140        150        160        170 
GELHGKPVRG VKLVGRDPKN NLEALEDFEK AAGARGLSTE SILIPRQSET CSPGSD 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of human von Ebner's gland protein, a member of the lipocalin superfamily highly expressed in lingual salivary glands."
Blaeker M., Kock K., Ahlers C., Buck F., Schmale H.
Biochim. Biophys. Acta 1172:131-137(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Tongue.
[2]"cDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein superfamily."
Redl B., Holzfeind P., Lottspeich F.
J. Biol. Chem. 267:20282-20287(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Tear.
[3]"Cloning of a human lacrimal lipocalin secreted in tears."
Lassagne H., Gachon A.-M.
Exp. Eye Res. 56:605-609(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Tear.
[4]"Structural organization of the gene encoding the human lipocalin tear prealbumin and synthesis of the recombinant protein in Escherichia coli."
Holzfeind P., Redl B.
Gene 139:177-183(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Expression of a lipocalin in human nasal mucosa."
Scalfari F., Castagna M., Fattori B., Andreini I., Maremmani C., Pelosi P.
Comp. Biochem. Physiol. 118B:819-824(1997)
Cited for: PROTEIN SEQUENCE OF 19-38.
Tissue: Nasal mucus.
[9]"Molecular cloning of a novel lipocalin-1 interacting human cell membrane receptor using phage display."
Wojnar P., Lechner M., Merschak P., Redl B.
J. Biol. Chem. 276:20206-20212(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LMBR1L.
Tissue: Pituitary.
[10]"Antisense down-regulation of lipocalin-interacting membrane receptor expression inhibits cellular internalization of lipocalin-1 in human NT2 cells."
Wojnar P., Lechner M., Redl B.
J. Biol. Chem. 278:16209-16215(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LMBR1L, ENDOCYTOSIS.
[11]"The 1.8-A crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands."
Breustedt D.A., Korndorfer I.P., Redl B., Skerra A.
J. Biol. Chem. 280:484-493(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-175.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62418 mRNA. Translation: CAA44284.1.
M90424 mRNA. Translation: AAA61845.1.
X67647 mRNA. Translation: CAA47889.1.
L14927 Genomic DNA. Translation: AAA18633.1.
AL161452 Genomic DNA. Translation: CAI14045.1.
CH471090 Genomic DNA. Translation: EAW88156.1.
BC065721 mRNA. Translation: AAH65721.1.
BC074925 mRNA. Translation: AAH74925.1.
BC074926 mRNA. Translation: AAH74926.1.
PIRLCHUL. A44029.
RefSeqNP_001239546.1. NM_001252617.1.
NP_001239547.1. NM_001252618.1.
NP_001239548.1. NM_001252619.1.
NP_002288.1. NM_002297.3.
UniGeneHs.530311.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XKIX-ray1.80A23-175[»]
3EYCX-ray2.60A/B/C/D23-175[»]
DisProtDP00647.
ProteinModelPortalP31025.
SMRP31025. Positions 31-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110125. 4 interactions.
IntActP31025. 1 interaction.
STRING9606.ENSP00000263598.

Protein family/group databases

Allergome3990. Hom s TL.

PTM databases

PhosphoSiteP31025.

Polymorphism databases

DMDM401346.

2D gel databases

UCD-2DPAGEP31025.

Proteomic databases

PeptideAtlasP31025.
PRIDEP31025.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263598; ENSP00000263598; ENSG00000160349.
ENST00000371781; ENSP00000360846; ENSG00000160349.
GeneID3933.
KEGGhsa:3933.
UCSCuc004cfz.2. human.

Organism-specific databases

CTD3933.
GeneCardsGC09P138413.
HGNCHGNC:6525. LCN1.
MIM151675. gene.
neXtProtNX_P31025.
PharmGKBPA30308.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000231562.
HOVERGENHBG101411.
InParanoidP31025.
OMALISGRCQ.
OrthoDBEOG7GXPD6.
PhylomeDBP31025.
TreeFamTF338197.

Gene expression databases

BgeeP31025.
CleanExHS_LCN1.
GenevestigatorP31025.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002450. von_Ebner_gland.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR01175. VNEBNERGLAND.
SUPFAMSSF50814. SSF50814. 1 hit.
ProtoNetSearch...

Other

ChiTaRSLCN1. human.
EvolutionaryTraceP31025.
GeneWikiLCN1.
GenomeRNAi3933.
NextBio15447.
PROP31025.
SOURCESearch...

Entry information

Entry nameLCN1_HUMAN
AccessionPrimary (citable) accession number: P31025
Secondary accession number(s): Q5T8A1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM