IL1FA_HUMAN
ID IL1FA_HUMAN Reviewed; 152 AA.
AC Q8WWZ1; Q53SR9; Q56AT8; Q7RTZ5; Q969H5; Q9BYX1;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Interleukin-1 family member 10;
DE Short=IL-1F10;
DE AltName: Full=Family of interleukin 1-theta;
DE Short=FIL1 theta;
DE AltName: Full=Interleukin-1 HY2;
DE Short=IL-1HY2;
DE AltName: Full=Interleukin-1 theta;
DE Short=IL-1 theta;
DE AltName: Full=Interleukin-38;
DE Short=IL-38;
GN Name=IL1F10 {ECO:0000312|MIM:615296}; Synonyms=FIL1T, IL1HY2, IL38;
GN ORFNames=FKSG75, UNQ6119/PRO20041;
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] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=11747621; DOI=10.1089/107999001753289505;
RA Bensen J.T., Dawson P.A., Mychaleckyj J.C., Bowden D.W.;
RT "Identification of a novel human cytokine gene in the interleukin gene
RT cluster on chromosome 2q12-14.";
RL J. Interferon Cytokine Res. 21:899-904(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Wang Y.-G., Li T., Gong L.;
RT "Identification and characterization of FKSG75, a novel member of the
RT interleukin-1 family.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS THR-44
RP AND ASP-51.
RC TISSUE=Fetal skin;
RX PubMed=11278614; DOI=10.1074/jbc.m010095200;
RA Lin H., Ho A.S., Haley-Vicente D., Zhang J., Bernal-Fussell J., Pace A.M.,
RA Hansen D., Schweighofer K., Mize N.K., Ford J.E.;
RT "Cloning and characterization of IL1HY2, a novel interleukin-1 family
RT member.";
RL J. Biol. Chem. 276:20597-20602(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11991722; DOI=10.1006/geno.2002.6751;
RA Nicklin M.J.H., Barton J.L., Nguyen M., Fitzgerald M.G., Duff W.G.,
RA Kornman K.;
RT "A sequence-based map of the nine genes of the human interleukin-1
RT cluster.";
RL Genomics 79:718-725(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-44 AND ASP-51.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-44 AND ASP-51.
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 [9]
RP FUNCTION.
RX PubMed=22315422; DOI=10.1073/pnas.1121534109;
RA van de Veerdonk F.L., Stoeckman A.K., Wu G., Boeckermann A.N., Azam T.,
RA Netea M.G., Joosten L.A., van der Meer J.W., Hao R., Kalabokis V.,
RA Dinarello C.A.;
RT "IL-38 binds to the IL-36 receptor and has biological effects on immune
RT cells similar to IL-36 receptor antagonist.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3001-3005(2012).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMED10.
RX PubMed=32272059; DOI=10.1016/j.cell.2020.03.031;
RA Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X.,
RA Zhang D., Lv X., Zheng L., Ge L.;
RT "A Translocation Pathway for Vesicle-Mediated Unconventional Protein
RT Secretion.";
RL Cell 181:637-652(2020).
RN [11]
RP VARIANTS THR-44 AND ASP-51.
RX PubMed=11991723; DOI=10.1006/geno.2002.6752;
RA Taylor S.L., Renshaw B.R., Garka K.E., Smith D.E., Sims J.E.;
RT "Genomic organization of the interleukin-1 locus.";
RL Genomics 79:726-733(2002).
CC -!- FUNCTION: Cytokine with immunomodulatory activity. Alone, does not
CC induce cytokine production, but reduces IL22 and IL17A production by T-
CC cells in response to heat-killed Candida albicans. Reduces IL36G-
CC induced production of IL8 by peripheral blood mononuclear cells.
CC Increases IL6 production by dendritic cells stimulated by bacterial
CC lipopolysaccharides (LPS). Ligand for IL-36R/IL1RL2.
CC {ECO:0000269|PubMed:22315422}.
CC -!- SUBUNIT: Interacts with cargo receptor TMED10; the interaction mediates
CC the translocation from the cytoplasm into the ERGIC (endoplasmic
CC reticulum-Golgi intermediate compartment) and thereby secretion.
CC {ECO:0000269|PubMed:32272059}.
CC -!- INTERACTION:
CC Q8WWZ1; P12268: IMPDH2; NbExp=3; IntAct=EBI-13318821, EBI-353389;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32272059}. Secreted
CC {ECO:0000269|PubMed:32272059}. Note=The secretion is dependent on
CC protein unfolding and facilitated by the cargo receptor TMED10; it
CC results in protein translocation from the cytoplasm into the ERGIC
CC (endoplasmic reticulum-Golgi intermediate compartment) followed by
CC vesicle entry and secretion. {ECO:0000269|PubMed:32272059}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WWZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WWZ1-2; Sequence=VSP_002658;
CC -!- TISSUE SPECIFICITY: Expressed in fetal skin, spleen and tonsil.
CC Expressed mostly in the basal epithelia of skin and in proliferating B-
CC cells of the tonsil.
CC -!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-1 entry;
CC URL="https://en.wikipedia.org/wiki/Interleukin_1";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il1f10/";
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DR EMBL; AY029413; AAK33010.1; -; mRNA.
DR EMBL; AY026753; AAK01948.1; -; mRNA.
DR EMBL; AF334755; AAK68048.1; -; mRNA.
DR EMBL; AF334756; AAK68049.1; -; Genomic_DNA.
DR EMBL; BN000002; CAD29878.1; -; Genomic_DNA.
DR EMBL; AY358846; AAQ89205.1; -; mRNA.
DR EMBL; AY972854; AAX59032.1; -; Genomic_DNA.
DR EMBL; AC016724; AAY14991.1; -; Genomic_DNA.
DR EMBL; BC103966; AAI03967.1; -; mRNA.
DR EMBL; BC103967; AAI03968.1; -; mRNA.
DR EMBL; BC103968; AAI03969.1; -; mRNA.
DR CCDS; CCDS2112.1; -. [Q8WWZ1-1]
DR RefSeq; NP_115945.4; NM_032556.5. [Q8WWZ1-1]
DR RefSeq; NP_775184.1; NM_173161.2. [Q8WWZ1-1]
DR PDB; 5BOW; X-ray; 1.31 A; A=3-152.
DR PDBsum; 5BOW; -.
DR AlphaFoldDB; Q8WWZ1; -.
DR SMR; Q8WWZ1; -.
DR BioGRID; 124164; 29.
DR IntAct; Q8WWZ1; 2.
DR STRING; 9606.ENSP00000376893; -.
DR iPTMnet; Q8WWZ1; -.
DR PhosphoSitePlus; Q8WWZ1; -.
DR BioMuta; IL1F10; -.
DR DMDM; 25008589; -.
DR MassIVE; Q8WWZ1; -.
DR PaxDb; Q8WWZ1; -.
DR PeptideAtlas; Q8WWZ1; -.
DR PRIDE; Q8WWZ1; -.
DR ProteomicsDB; 74961; -. [Q8WWZ1-1]
DR ProteomicsDB; 74962; -. [Q8WWZ1-2]
DR Antibodypedia; 47548; 195 antibodies from 27 providers.
DR DNASU; 84639; -.
DR Ensembl; ENST00000341010.6; ENSP00000341794.2; ENSG00000136697.13. [Q8WWZ1-1]
DR Ensembl; ENST00000393197.3; ENSP00000376893.2; ENSG00000136697.13. [Q8WWZ1-1]
DR GeneID; 84639; -.
DR KEGG; hsa:84639; -.
DR MANE-Select; ENST00000341010.6; ENSP00000341794.2; NM_173161.3; NP_775184.1.
DR UCSC; uc002tiu.4; human. [Q8WWZ1-1]
DR CTD; 84639; -.
DR DisGeNET; 84639; -.
DR GeneCards; IL1F10; -.
DR HGNC; HGNC:15552; IL1F10.
DR HPA; ENSG00000136697; Group enriched (lymphoid tissue, skin).
DR MIM; 615296; gene.
DR neXtProt; NX_Q8WWZ1; -.
DR OpenTargets; ENSG00000136697; -.
DR PharmGKB; PA38387; -.
DR VEuPathDB; HostDB:ENSG00000136697; -.
DR eggNOG; ENOG502SN3A; Eukaryota.
DR GeneTree; ENSGT00950000182943; -.
DR HOGENOM; CLU_095373_2_0_1; -.
DR InParanoid; Q8WWZ1; -.
DR OMA; QFYFEQS; -.
DR OrthoDB; 1410755at2759; -.
DR PhylomeDB; Q8WWZ1; -.
DR TreeFam; TF300203; -.
DR PathwayCommons; Q8WWZ1; -.
DR Reactome; R-HSA-9007892; Interleukin-38 signaling.
DR Reactome; R-HSA-9014826; Interleukin-36 pathway.
DR SignaLink; Q8WWZ1; -.
DR BioGRID-ORCS; 84639; 12 hits in 1054 CRISPR screens.
DR GeneWiki; IL1F10; -.
DR GenomeRNAi; 84639; -.
DR Pharos; Q8WWZ1; Tbio.
DR PRO; PR:Q8WWZ1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WWZ1; protein.
DR Bgee; ENSG00000136697; Expressed in skin of limb and 37 other tissues.
DR Genevisible; Q8WWZ1; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005149; F:interleukin-1 receptor binding; IEA:InterPro.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR027164; IL-1_F10.
DR InterPro; IPR000975; IL-1_fam.
DR InterPro; IPR003297; IL-1RA/IL-36.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR10078; PTHR10078; 1.
DR PANTHER; PTHR10078:SF29; PTHR10078:SF29; 1.
DR Pfam; PF00340; IL1; 1.
DR PRINTS; PR00264; INTERLEUKIN1.
DR PRINTS; PR01360; INTRLEUKIN1X.
DR SUPFAM; SSF50353; SSF50353; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytokine; Cytoplasm;
KW Reference proteome; Secreted.
FT CHAIN 1..152
FT /note="Interleukin-1 family member 10"
FT /id="PRO_0000153650"
FT VAR_SEQ 9..39
FT /note="YYIIKYADQKALYTRDGQLLVGDPVADNCCA -> MSSSFLPEPLPAKSLQH
FT GVPLSLDSSLSSLL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_002658"
FT VARIANT 44
FT /note="I -> T (in dbSNP:rs6761276)"
FT /evidence="ECO:0000269|PubMed:11278614,
FT ECO:0000269|PubMed:11991723, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.6"
FT /id="VAR_014262"
FT VARIANT 51
FT /note="A -> D (in dbSNP:rs6743376)"
FT /evidence="ECO:0000269|PubMed:11278614,
FT ECO:0000269|PubMed:11991723, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.6"
FT /id="VAR_014263"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:5BOW"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:5BOW"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:5BOW"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:5BOW"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:5BOW"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:5BOW"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:5BOW"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:5BOW"
SQ SEQUENCE 152 AA; 16943 MW; E0ABD2496551B34F CRC64;
MCSLPMARYY IIKYADQKAL YTRDGQLLVG DPVADNCCAE KICILPNRGL ARTKVPIFLG
IQGGSRCLAC VETEEGPSLQ LEDVNIEELY KGGEEATRFT FFQSSSGSAF RLEAAAWPGW
FLCGPAEPQQ PVQLTKESEP SARTKFYFEQ SW
