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P31025

- LCN1_HUMAN

UniProt

P31025 - LCN1_HUMAN

Protein

Lipocalin-1

Gene

LCN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    1. cysteine-type endopeptidase inhibitor activity Source: ProtInc

    GO - Biological processi

    1. negative regulation of endopeptidase activity Source: GOC
    2. proteolysis Source: ProtInc
    3. response to stimulus Source: UniProtKB-KW
    4. retina homeostasis Source: UniProt
    5. sensory perception of taste Source: UniProtKB-KW
    6. transport Source: UniProtKB-KW

    Keywords - Biological processi

    Sensory transduction, Taste, Transport

    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: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:6525. LCN1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30308.

    Protein family/group databases

    Allergomei3990. Hom s TL.

    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.
    GenevestigatoriP31025.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi110125. 5 interactions.
    IntActiP31025. 1 interaction.
    STRINGi9606.ENSP00000263598.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XKIX-ray1.80A23-176[»]
    3EYCX-ray2.60A/B/C/D23-176[»]
    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

    HOGENOMiHOG000231562.
    HOVERGENiHBG101411.
    InParanoidiP31025.
    OMAiSGRCQEV.
    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

    MKPLLLAVSL GLIAALQAHH LLASDEEIQD VSGTWYLKAM TVDREFPEMN    50
    LESVTPMTLT TLEGGNLEAK VTMLISGRCQ EVKAVLEKTD EPGKYTADGG 100
    KHVAYIIRSH VKDHYIFYCE GELHGKPVRG VKLVGRDPKN NLEALEDFEK 150
    AAGARGLSTE SILIPRQSET CSPGSD 176
    Length:176
    Mass (Da):19,250
    Last modified:July 1, 1993 - v1
    Checksum:i0DDBF124C8C78CB8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi401346.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6991.1.
    PIRi A44029. LCHUL.
    RefSeqi NP_001239546.1. NM_001252617.1.
    NP_001239547.1. NM_001252618.1.
    NP_001239548.1. NM_001252619.1.
    NP_002288.1. NM_002297.3.
    UniGenei Hs.530311.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XKI X-ray 1.80 A 23-176 [» ]
    3EYC X-ray 2.60 A/B/C/D 23-176 [» ]
    DisProti DP00647.
    ProteinModelPortali P31025.
    SMRi P31025. Positions 31-173.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110125. 5 interactions.
    IntActi P31025. 1 interaction.
    STRINGi 9606.ENSP00000263598.

    Protein family/group databases

    Allergomei 3990. Hom s TL.

    PTM databases

    PhosphoSitei P31025.

    Polymorphism databases

    DMDMi 401346.

    2D gel databases

    UCD-2DPAGE P31025.

    Proteomic databases

    MaxQBi P31025.
    PeptideAtlasi P31025.
    PRIDEi P31025.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263598 ; ENSP00000263598 ; ENSG00000160349 .
    ENST00000371781 ; ENSP00000360846 ; ENSG00000160349 .
    GeneIDi 3933.
    KEGGi hsa:3933.
    UCSCi uc004cfz.2. human.

    Organism-specific databases

    CTDi 3933.
    GeneCardsi GC09P138413.
    HGNCi HGNC:6525. LCN1.
    MIMi 151675. gene.
    neXtProti NX_P31025.
    PharmGKBi PA30308.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000231562.
    HOVERGENi HBG101411.
    InParanoidi P31025.
    OMAi SGRCQEV.
    OrthoDBi EOG7GXPD6.
    PhylomeDBi P31025.
    TreeFami TF338197.

    Miscellaneous databases

    ChiTaRSi LCN1. human.
    EvolutionaryTracei P31025.
    GeneWikii LCN1.
    GenomeRNAii 3933.
    NextBioi 15447.
    PROi P31025.
    SOURCEi Search...

    Gene expression databases

    Bgeei P31025.
    CleanExi HS_LCN1.
    Genevestigatori P31025.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR002450. von_Ebner_gland.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR01175. VNEBNERGLAND.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 142 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