IL19_HUMAN
ID IL19_HUMAN Reviewed; 177 AA.
AC Q9UHD0; B6VEV9; Q5VUT3; Q96QR4; Q9NUA0;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Interleukin-19;
DE Short=IL-19;
DE AltName: Full=Melanoma differentiation-associated protein-like protein;
DE AltName: Full=NG.1;
DE Flags: Precursor;
GN Name=IL19; Synonyms=ZMDA1;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-175.
RX PubMed=11196675; DOI=10.1038/sj.gene.6363714;
RA Gallagher G., Dickensheets H., Eskdale J., Izotova L.S.,
RA Mirochnitchenko O.V., Peat J.D., Vasquez N., Pestka S., Donnelly R.P.,
RA Kotenko S.V.;
RT "Cloning, expression and initial characterization of interleukin-19 (IL-
RT 19), a novel homolog of human interleukin-10 (IL-10).";
RL Genes Immun. 1:442-450(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-175.
RX PubMed=12370360; DOI=10.4049/jimmunol.169.8.4288;
RA Liao Y.-C., Liang W.G., Chen F.W., Hsu J.H., Yang J.J., Chang M.-S.;
RT "IL-19 induces production of IL-6 and TNF-alpha and results in cell
RT apoptosis through TNF-alpha.";
RL J. Immunol. 169:4288-4297(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=19906316; DOI=10.1186/1471-2164-10-518;
RA Wang P., Yu P., Gao P., Shi T., Ma D.;
RT "Discovery of novel human transcript variants by analysis of intronic
RT single-block EST with polyadenylation site.";
RL BMC Genomics 10:518-518(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-175.
RA Conklin D., Petersen J., Loften-Day C., Whitmore T., Muerer M., Sexson S.,
RA Smith D., Lok S., Pownder T., O'Hara P.;
RT "Homo sapiens homolog of melanoma differentiation associated gene.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-175.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP PROTEIN SEQUENCE OF 25-39.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 19-177, AND DISULFIDE BONDS.
RX PubMed=12403790; DOI=10.1074/jbc.m208602200;
RA Chang C., Magracheva E., Kozlov S., Fong S., Tobin G., Kotenko S.,
RA Wlodawer A., Zdanov A.;
RT "Crystal structure of interleukin-19 defines a new subfamily of helical
RT cytokines.";
RL J. Biol. Chem. 278:3308-3313(2003).
CC -!- FUNCTION: May play some important roles in inflammatory responses. Up-
CC regulates IL-6 and TNF-alpha and induces apoptosis (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC PRO_0000015379; Q6UXL0: IL20RB; NbExp=4; IntAct=EBI-14023330, EBI-14022792;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UHD0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHD0-2; Sequence=VSP_046253;
CC Name=3;
CC IsoId=Q9UHD0-3; Sequence=VSP_057193;
CC -!- SIMILARITY: Belongs to the IL-10 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il19/";
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DR EMBL; AF276915; AAG16755.1; -; Genomic_DNA.
DR EMBL; AY040367; AAK91776.1; -; mRNA.
DR EMBL; AF453946; AAN40906.1; -; mRNA.
DR EMBL; FJ380053; ACJ06540.1; -; mRNA.
DR EMBL; AF192498; AAF06663.1; -; mRNA.
DR EMBL; AF390905; AAK64498.1; -; Genomic_DNA.
DR EMBL; AL513315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049615; CAB72342.1; -; Genomic_DNA.
DR CCDS; CCDS1468.1; -. [Q9UHD0-1]
DR CCDS; CCDS1469.1; -. [Q9UHD0-1]
DR RefSeq; NP_037503.2; NM_013371.3. [Q9UHD0-1]
DR RefSeq; NP_715639.1; NM_153758.2. [Q9UHD0-1]
DR RefSeq; XP_011507752.1; XM_011509450.2. [Q9UHD0-3]
DR PDB; 1N1F; X-ray; 1.95 A; A=19-177.
DR PDBsum; 1N1F; -.
DR AlphaFoldDB; Q9UHD0; -.
DR SMR; Q9UHD0; -.
DR BioGRID; 118986; 2.
DR IntAct; Q9UHD0; 2.
DR STRING; 9606.ENSP00000343000; -.
DR GlyGen; Q9UHD0; 2 sites.
DR BioMuta; IL19; -.
DR DMDM; 146345440; -.
DR MassIVE; Q9UHD0; -.
DR PaxDb; Q9UHD0; -.
DR PeptideAtlas; Q9UHD0; -.
DR PRIDE; Q9UHD0; -.
DR ProteomicsDB; 84320; -. [Q9UHD0-1]
DR Antibodypedia; 34588; 399 antibodies from 31 providers.
DR DNASU; 29949; -.
DR Ensembl; ENST00000270218.10; ENSP00000270218.6; ENSG00000142224.18. [Q9UHD0-1]
DR Ensembl; ENST00000340758.7; ENSP00000343000.3; ENSG00000142224.18. [Q9UHD0-1]
DR Ensembl; ENST00000656872.2; ENSP00000499487.2; ENSG00000142224.18. [Q9UHD0-1]
DR Ensembl; ENST00000659997.3; ENSP00000499459.2; ENSG00000142224.18. [Q9UHD0-1]
DR GeneID; 29949; -.
DR KEGG; hsa:29949; -.
DR MANE-Select; ENST00000659997.3; ENSP00000499459.2; NM_153758.5; NP_715639.2.
DR UCSC; uc001heo.3; human. [Q9UHD0-1]
DR CTD; 29949; -.
DR DisGeNET; 29949; -.
DR GeneCards; IL19; -.
DR HGNC; HGNC:5990; IL19.
DR HPA; ENSG00000142224; Group enriched (cervix, salivary gland).
DR MIM; 605687; gene.
DR neXtProt; NX_Q9UHD0; -.
DR OpenTargets; ENSG00000142224; -.
DR PharmGKB; PA29806; -.
DR VEuPathDB; HostDB:ENSG00000142224; -.
DR eggNOG; ENOG502SRCR; Eukaryota.
DR GeneTree; ENSGT00950000183124; -.
DR HOGENOM; CLU_098690_0_0_1; -.
DR InParanoid; Q9UHD0; -.
DR OMA; LYMQKAL; -.
DR OrthoDB; 1267998at2759; -.
DR PhylomeDB; Q9UHD0; -.
DR TreeFam; TF333253; -.
DR PathwayCommons; Q9UHD0; -.
DR Reactome; R-HSA-8854691; Interleukin-20 family signaling.
DR SignaLink; Q9UHD0; -.
DR SIGNOR; Q9UHD0; -.
DR BioGRID-ORCS; 29949; 8 hits in 1071 CRISPR screens.
DR ChiTaRS; IL19; human.
DR EvolutionaryTrace; Q9UHD0; -.
DR GenomeRNAi; 29949; -.
DR Pharos; Q9UHD0; Tbio.
DR PRO; PR:Q9UHD0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UHD0; protein.
DR Bgee; ENSG00000142224; Expressed in nasal cavity epithelium and 78 other tissues.
DR Genevisible; Q9UHD0; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; TAS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR020443; IL-10/19/20/22/24/26_fam.
DR InterPro; IPR020423; IL-10_CS.
DR InterPro; IPR020421; IL-19.
DR Pfam; PF00726; IL10; 1.
DR PRINTS; PR01934; INTRLEUKIN19.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00520; INTERLEUKIN_10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytokine;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 25..177
FT /note="Interleukin-19"
FT /id="PRO_0000015379"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..121
FT /evidence="ECO:0000269|PubMed:12403790"
FT DISULFID 75..127
FT /evidence="ECO:0000269|PubMed:12403790"
FT DISULFID 76..129
FT /evidence="ECO:0000269|PubMed:12403790"
FT VAR_SEQ 1
FT /note="M -> MCTEGAFPHRSACSLPLTHVHTHIHVCVPVLWGSVPRGM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11196675"
FT /id="VSP_046253"
FT VAR_SEQ 122..177
FT /note="QEQRQCHCRQEATNATRVIHDNYDQLEVHAAAIKSLGELDVFLAWINKNHEV
FT MFSA -> VSHWVRIPASAPCLPKERPGSAGPHRPPDMVLGVKGNSLRTSTGRTVENLS
FT QWPLLPQGSLPADNSSDGLLLDNPPGVTNLCQHIP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19906316"
FT /id="VSP_057193"
FT VARIANT 175
FT /note="F -> S (in dbSNP:rs2243191)"
FT /evidence="ECO:0000269|PubMed:11196675,
FT ECO:0000269|PubMed:12370360, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5"
FT /id="VAR_013077"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:1N1F"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:1N1F"
FT HELIX 34..49
FT /evidence="ECO:0007829|PDB:1N1F"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1N1F"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1N1F"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:1N1F"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1N1F"
FT HELIX 98..121
FT /evidence="ECO:0007829|PDB:1N1F"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:1N1F"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:1N1F"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:1N1F"
SQ SEQUENCE 177 AA; 20452 MW; 7CCFB052177DE408 CRC64;
MKLQCVSLWL LGTILILCSV DNHGLRRCLI STDMHHIEES FQEIKRAIQA KDTFPNVTIL
STLETLQIIK PLDVCCVTKN LLAFYVDRVF KDHQEPNPKI LRKISSIANS FLYMQKTLRQ
CQEQRQCHCR QEATNATRVI HDNYDQLEVH AAAIKSLGEL DVFLAWINKN HEVMFSA
