LCN1_HUMAN
ID LCN1_HUMAN Reviewed; 176 AA.
AC P31025; Q5T8A1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Lipocalin-1;
DE AltName: Full=Tear lipocalin;
DE Short=Tlc;
DE AltName: Full=Tear prealbumin;
DE Short=TP;
DE AltName: Full=von Ebner gland protein;
DE Short=VEG protein;
DE Flags: Precursor;
GN Name=LCN1; Synonyms=VEGP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tongue;
RX PubMed=7679926; DOI=10.1016/0167-4781(93)90279-m;
RA Blaeker M., Kock K., Ahlers C., Buck F., Schmale H.;
RT "Molecular cloning of human von Ebner's gland protein, a member of the
RT lipocalin superfamily highly expressed in lingual salivary glands.";
RL Biochim. Biophys. Acta 1172:131-137(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tear;
RX PubMed=1400345; DOI=10.1016/s0021-9258(19)88698-2;
RA Redl B., Holzfeind P., Lottspeich F.;
RT "cDNA cloning and sequencing reveals human tear prealbumin to be a member
RT of the lipophilic-ligand carrier protein superfamily.";
RL J. Biol. Chem. 267:20282-20287(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tear;
RX PubMed=8500570; DOI=10.1006/exer.1993.1075;
RA Lassagne H., Gachon A.-M.;
RT "Cloning of a human lacrimal lipocalin secreted in tears.";
RL Exp. Eye Res. 56:605-609(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8112601; DOI=10.1016/0378-1119(94)90752-8;
RA Holzfeind P., Redl B.;
RT "Structural organization of the gene encoding the human lipocalin tear
RT prealbumin and synthesis of the recombinant protein in Escherichia coli.";
RL Gene 139:177-183(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 19-38.
RC TISSUE=Nasal mucus;
RA Scalfari F., Castagna M., Fattori B., Andreini I., Maremmani C., Pelosi P.;
RT "Expression of a lipocalin in human nasal mucosa.";
RL Comp. Biochem. Physiol. 118B:819-824(1997).
RN [9]
RP PROTEIN SEQUENCE OF 19-35 AND 138-176, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Tear;
RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
RA Suarez T., Elortza F.;
RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed
RT by in silico and in vitro analyses for antimicrobial peptide
RT identification.";
RL J. Proteome Res. 14:2649-2658(2015).
RN [10]
RP INTERACTION WITH LMBR1L.
RC TISSUE=Pituitary;
RX PubMed=11287427; DOI=10.1074/jbc.m101762200;
RA Wojnar P., Lechner M., Merschak P., Redl B.;
RT "Molecular cloning of a novel lipocalin-1 interacting human cell membrane
RT receptor using phage display.";
RL J. Biol. Chem. 276:20206-20212(2001).
RN [11]
RP INTERACTION WITH LMBR1L, AND ENDOCYTOSIS.
RX PubMed=12591932; DOI=10.1074/jbc.m210922200;
RA Wojnar P., Lechner M., Redl B.;
RT "Antisense down-regulation of lipocalin-interacting membrane receptor
RT expression inhibits cellular internalization of lipocalin-1 in human NT2
RT cells.";
RL J. Biol. Chem. 278:16209-16215(2003).
RN [12]
RP SUBUNIT.
RX PubMed=17869594; DOI=10.1016/j.bbapap.2007.07.014;
RA Gasymov O.K., Abduragimov A.R., Merschak P., Redl B., Glasgow B.J.;
RT "Oligomeric state of lipocalin-1 (LCN1) by multiangle laser light
RT scattering and fluorescence anisotropy decay.";
RL Biochim. Biophys. Acta 1774:1307-1315(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-175.
RX PubMed=15489503; DOI=10.1074/jbc.m410466200;
RA Breustedt D.A., Korndorfer I.P., Redl B., Skerra A.;
RT "The 1.8-A crystal structure of human tear lipocalin reveals an extended
RT branched cavity with capacity for multiple ligands.";
RL J. Biol. Chem. 280:484-493(2005).
CC -!- FUNCTION: Could play a role in taste reception. Could be necessary for
CC the concentration and delivery of sapid molecules in the gustatory
CC system. Can bind various ligands, with chemical structures ranging from
CC lipids and retinoids to the macrocyclic antibiotic rifampicin and even
CC to microbial siderophores. Exhibits an extremely wide ligand pocket.
CC -!- SUBUNIT: Predominantly monomer (PubMed:17869594). May form homodimer
CC (PubMed:17869594). Interacts with LMBR1L; this interaction mediates the
CC endocytosis of LCN1 (PubMed:11287427, PubMed:12591932).
CC {ECO:0000269|PubMed:11287427, ECO:0000269|PubMed:12591932,
CC ECO:0000269|PubMed:17869594}.
CC -!- INTERACTION:
CC P31025; P09917: ALOX5; NbExp=3; IntAct=EBI-1052433, EBI-79934;
CC P31025; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-1052433, EBI-14240149;
CC P31025; Q6P9E2: RECK; NbExp=3; IntAct=EBI-1052433, EBI-10253121;
CC P31025; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-1052433, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mainly expressed in lachrymal and salivary glands.
CC Also expressed in the prostate.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; X62418; CAA44284.1; -; mRNA.
DR EMBL; M90424; AAA61845.1; -; mRNA.
DR EMBL; X67647; CAA47889.1; -; mRNA.
DR EMBL; L14927; AAA18633.1; -; Genomic_DNA.
DR EMBL; AL161452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88156.1; -; Genomic_DNA.
DR EMBL; BC065721; AAH65721.1; -; mRNA.
DR EMBL; BC074925; AAH74925.1; -; mRNA.
DR EMBL; BC074926; AAH74926.1; -; mRNA.
DR CCDS; CCDS6991.1; -.
DR PIR; A44029; LCHUL.
DR RefSeq; NP_001239546.1; NM_001252617.1.
DR RefSeq; NP_001239547.1; NM_001252618.1.
DR RefSeq; NP_001239548.1; NM_001252619.1.
DR RefSeq; NP_002288.1; NM_002297.3.
DR PDB; 1XKI; X-ray; 1.80 A; A=23-176.
DR PDB; 3EYC; X-ray; 2.60 A; A/B/C/D=23-176.
DR PDB; 4QAF; X-ray; 1.80 A; A/B=23-174.
DR PDB; 5T43; NMR; -; A=19-176.
DR PDBsum; 1XKI; -.
DR PDBsum; 3EYC; -.
DR PDBsum; 4QAF; -.
DR PDBsum; 5T43; -.
DR AlphaFoldDB; P31025; -.
DR SMR; P31025; -.
DR BioGRID; 110125; 119.
DR IntAct; P31025; 17.
DR MINT; P31025; -.
DR STRING; 9606.ENSP00000263598; -.
DR DrugBank; DB00755; Tretinoin.
DR SwissLipids; SLP:000001525; -.
DR Allergome; 3990; Hom s TL.
DR iPTMnet; P31025; -.
DR PhosphoSitePlus; P31025; -.
DR BioMuta; LCN1; -.
DR DMDM; 401346; -.
DR UCD-2DPAGE; P31025; -.
DR EPD; P31025; -.
DR jPOST; P31025; -.
DR MassIVE; P31025; -.
DR MaxQB; P31025; -.
DR PaxDb; P31025; -.
DR PeptideAtlas; P31025; -.
DR PRIDE; P31025; -.
DR ProteomicsDB; 54757; -.
DR TopDownProteomics; P31025; -.
DR Antibodypedia; 32051; 251 antibodies from 33 providers.
DR DNASU; 3933; -.
DR Ensembl; ENST00000263598.6; ENSP00000263598.2; ENSG00000160349.10.
DR Ensembl; ENST00000371781.4; ENSP00000360846.3; ENSG00000160349.10.
DR GeneID; 3933; -.
DR KEGG; hsa:3933; -.
DR MANE-Select; ENST00000371781.4; ENSP00000360846.3; NM_002297.4; NP_002288.1.
DR UCSC; uc004cfz.3; human.
DR CTD; 3933; -.
DR DisGeNET; 3933; -.
DR GeneCards; LCN1; -.
DR HGNC; HGNC:6525; LCN1.
DR HPA; ENSG00000160349; Group enriched (esophagus, seminal vesicle).
DR MIM; 151675; gene.
DR neXtProt; NX_P31025; -.
DR OpenTargets; ENSG00000160349; -.
DR PharmGKB; PA30308; -.
DR VEuPathDB; HostDB:ENSG00000160349; -.
DR eggNOG; ENOG502S22P; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR HOGENOM; CLU_125034_0_0_1; -.
DR InParanoid; P31025; -.
DR OMA; QAEACTP; -.
DR OrthoDB; 1450978at2759; -.
DR PhylomeDB; P31025; -.
DR TreeFam; TF338197; -.
DR PathwayCommons; P31025; -.
DR Reactome; R-HSA-804914; Transport of fatty acids.
DR SignaLink; P31025; -.
DR BioGRID-ORCS; 3933; 13 hits in 1034 CRISPR screens.
DR ChiTaRS; LCN1; human.
DR EvolutionaryTrace; P31025; -.
DR GeneWiki; LCN1; -.
DR GenomeRNAi; 3933; -.
DR Pharos; P31025; Tbio.
DR PRO; PR:P31025; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P31025; protein.
DR Bgee; ENSG00000160349; Expressed in lacrimal gland and 76 other tissues.
DR ExpressionAtlas; P31025; baseline and differential.
DR Genevisible; P31025; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031404; F:chloride ion binding; IDA:CAFA.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; TAS:ProtInc.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002450; von_Ebner_gland.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01175; VNEBNERGLAND.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Sensory transduction; Signal; Taste;
KW Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:25946035, ECO:0000269|Ref.8"
FT CHAIN 19..176
FT /note="Lipocalin-1"
FT /id="PRO_0000017974"
FT DISULFID 79..171
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5T43"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:1XKI"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5T43"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:4QAF"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:1XKI"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:5T43"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1XKI"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:4QAF"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1XKI"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1XKI"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1XKI"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1XKI"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4QAF"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1XKI"
FT STRAND 128..139
FT /evidence="ECO:0007829|PDB:1XKI"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:1XKI"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1XKI"
SQ SEQUENCE 176 AA; 19250 MW; 0DDBF124C8C78CB8 CRC64;
MKPLLLAVSL GLIAALQAHH LLASDEEIQD VSGTWYLKAM TVDREFPEMN LESVTPMTLT
TLEGGNLEAK VTMLISGRCQ EVKAVLEKTD EPGKYTADGG KHVAYIIRSH VKDHYIFYCE
GELHGKPVRG VKLVGRDPKN NLEALEDFEK AAGARGLSTE SILIPRQSET CSPGSD
