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Protein

Lipocalin-1

Gene

LCN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • cysteine-type endopeptidase inhibitor activity Source: ProtInc

GO - Biological processi

  • long-chain fatty acid transport Source: Reactome
  • negative regulation of endopeptidase activity Source: GOC
  • proteolysis Source: ProtInc
  • response to stimulus Source: UniProtKB-KW
  • retina homeostasis Source: UniProtKB
  • sensory perception of taste Source: UniProtKB-KW
  • transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Taste, Transport

Enzyme and pathway databases

ReactomeiREACT_23892. Transport of fatty acids.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:LCN1
Synonyms:VEGP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:6525. LCN1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30308.

Protein family/group databases

Allergomei3990. Hom s TL.

Polymorphism and mutation databases

BioMutaiLCN1.
DMDMi401346.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 176158Lipocalin-1PRO_0000017974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi79 ↔ 171

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP31025.
PeptideAtlasiP31025.
PRIDEiP31025.

2D gel databases

UCD-2DPAGEP31025.

PTM databases

PhosphoSiteiP31025.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP31025.
CleanExiHS_LCN1.
ExpressionAtlasiP31025. baseline.
GenevisibleiP31025. HS.

Interactioni

Subunit structurei

Homodimer (By similarity). Binds to LMBR1L which may mediate its endocytosis.By similarity

Protein-protein interaction databases

BioGridi110125. 7 interactions.
IntActiP31025. 2 interactions.
STRINGi9606.ENSP00000263598.

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 4210Combined sources
Beta strandi51 – 544Combined sources
Beta strandi57 – 615Combined sources
Beta strandi67 – 737Combined sources
Beta strandi80 – 889Combined sources
Beta strandi94 – 974Combined sources
Helixi98 – 1003Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi114 – 1218Combined sources
Beta strandi128 – 13912Combined sources
Helixi145 – 15410Combined sources
Beta strandi160 – 1634Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XKIX-ray1.80A23-176[»]
3EYCX-ray2.60A/B/C/D23-176[»]
4QAFX-ray1.80A/B23-174[»]
DisProtiDP00647.
ProteinModelPortaliP31025.
SMRiP31025. Positions 31-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31025.

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00440000033563.
HOGENOMiHOG000231562.
HOVERGENiHBG101411.
InParanoidiP31025.
OMAiLISGRCQ.
OrthoDBiEOG7GXPD6.
PhylomeDBiP31025.
TreeFamiTF338197.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002450. von_Ebner_gland.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01175. VNEBNERGLAND.
SUPFAMiSSF50814. SSF50814. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P31025-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPLLLAVSL GLIAALQAHH LLASDEEIQD VSGTWYLKAM TVDREFPEMN
60 70 80 90 100
LESVTPMTLT TLEGGNLEAK VTMLISGRCQ EVKAVLEKTD EPGKYTADGG
110 120 130 140 150
KHVAYIIRSH VKDHYIFYCE GELHGKPVRG VKLVGRDPKN NLEALEDFEK
160 170
AAGARGLSTE SILIPRQSET CSPGSD
Length:176
Mass (Da):19,250
Last modified:July 1, 1993 - v1
Checksum:i0DDBF124C8C78CB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6991.1.
PIRiA44029. LCHUL.
RefSeqiNP_001239546.1. NM_001252617.1.
NP_001239547.1. NM_001252618.1.
NP_001239548.1. NM_001252619.1.
NP_002288.1. NM_002297.3.
UniGeneiHs.530311.

Genome annotation databases

EnsembliENST00000263598; ENSP00000263598; ENSG00000160349.
ENST00000371781; ENSP00000360846; ENSG00000160349.
GeneIDi3933.
KEGGihsa:3933.
UCSCiuc004cfz.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6991.1.
PIRiA44029. LCHUL.
RefSeqiNP_001239546.1. NM_001252617.1.
NP_001239547.1. NM_001252618.1.
NP_001239548.1. NM_001252619.1.
NP_002288.1. NM_002297.3.
UniGeneiHs.530311.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XKIX-ray1.80A23-176[»]
3EYCX-ray2.60A/B/C/D23-176[»]
4QAFX-ray1.80A/B23-174[»]
DisProtiDP00647.
ProteinModelPortaliP31025.
SMRiP31025. Positions 31-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110125. 7 interactions.
IntActiP31025. 2 interactions.
STRINGi9606.ENSP00000263598.

Protein family/group databases

Allergomei3990. Hom s TL.

PTM databases

PhosphoSiteiP31025.

Polymorphism and mutation databases

BioMutaiLCN1.
DMDMi401346.

2D gel databases

UCD-2DPAGEP31025.

Proteomic databases

MaxQBiP31025.
PeptideAtlasiP31025.
PRIDEiP31025.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263598; ENSP00000263598; ENSG00000160349.
ENST00000371781; ENSP00000360846; ENSG00000160349.
GeneIDi3933.
KEGGihsa:3933.
UCSCiuc004cfz.2. human.

Organism-specific databases

CTDi3933.
GeneCardsiGC09P138413.
HGNCiHGNC:6525. LCN1.
MIMi151675. gene.
neXtProtiNX_P31025.
PharmGKBiPA30308.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00440000033563.
HOGENOMiHOG000231562.
HOVERGENiHBG101411.
InParanoidiP31025.
OMAiLISGRCQ.
OrthoDBiEOG7GXPD6.
PhylomeDBiP31025.
TreeFamiTF338197.

Enzyme and pathway databases

ReactomeiREACT_23892. Transport of fatty acids.

Miscellaneous databases

ChiTaRSiLCN1. human.
EvolutionaryTraceiP31025.
GeneWikiiLCN1.
GenomeRNAii3933.
NextBioi15447.
PROiP31025.
SOURCEiSearch...

Gene expression databases

BgeeiP31025.
CleanExiHS_LCN1.
ExpressionAtlasiP31025. baseline.
GenevisibleiP31025. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002450. von_Ebner_gland.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01175. VNEBNERGLAND.
SUPFAMiSSF50814. SSF50814. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiLCN1_HUMAN
AccessioniPrimary (citable) accession number: P31025
Secondary accession number(s): Q5T8A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 24, 2015
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.