ID IL7_HUMAN Reviewed; 177 AA. AC P13232; A0N0L3; Q5FBY5; Q5FBY9; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 11-NOV-2015, entry version 155. DE RecName: Full=Interleukin-7; DE Short=IL-7; DE Flags: Precursor; GN Name=IL7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2643102; DOI=10.1073/pnas.86.1.302; RA Goodwin R.G., Lupton S., Schmierer A., Hjerrild K.J., Jerzy R., RA Clevenger W., Gillis S., Cosman D., Namen A.E.; RT "Human interleukin 7: molecular cloning and growth factor activity on RT human and murine B-lineage cells."; RL Proc. Natl. Acad. Sci. U.S.A. 86:302-306(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2329282; RA Lupton S.D., Gimpel S., Jerzy R., Brunton L.L., Hjerrild K.A., RA Cosman D., Goodwin R.G.; RT "Characterization of the human and murine IL-7 genes."; RL J. Immunol. 144:3592-3601(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). RA Sameshima E., Tabata Y., Hayashi A., Iida K., Mitsuyama M., Kanai S., RA Furuya T.; RT "interleukin7 mRNA,nirs splice variant2."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., RA Nickerson D.A.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pancreas; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP DISULFIDE BONDS, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=9407080; DOI=10.1074/jbc.272.52.32995; RA Cosenza L., Sweeney E., Murphy J.R.; RT "Disulfide bond assignment in human interleukin-7 by matrix-assisted RT laser desorption/ionization mass spectroscopy and site-directed RT cysteine to serine mutational analysis."; RL J. Biol. Chem. 272:32995-33000(1997). RN [9] RP 3D-STRUCTURE MODELING. RX PubMed=8862549; DOI=10.1093/protein/9.6.493; RA Kroemer R.T., Doughty S.W., Robinson A.J., Richards W.G.; RT "Prediction of the three-dimensional structure of human interleukin-7 RT by homology modeling."; RL Protein Eng. 9:493-498(1996). RN [10] RP 3D-STRUCTURE MODELING. RX PubMed=10850801; DOI=10.1110/ps.9.5.916; RA Cosenza L., Rosenbach A., White J.V., Murphy J.R., Smith T.F.; RT "Comparative model building of interleukin-7 using interleukin-4 as a RT template: a structural hypothesis that displays atypical surface RT chemistry in helix D important for receptor activation."; RL Protein Sci. 9:916-926(2000). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 26-177 IN COMPLEX WITH IL7R, RP AND DISULFIDE BONDS. RX PubMed=19141282; DOI=10.1016/j.str.2008.10.019; RA McElroy C.A., Dohm J.A., Walsh S.T.; RT "Structural and biophysical studies of the human IL-7/IL-7Ralpha RT complex."; RL Structure 17:54-65(2009). CC -!- FUNCTION: Hematopoietic growth factor capable of stimulating the CC proliferation of lymphoid progenitors. It is important for CC proliferation during certain stages of B-cell maturation. CC -!- INTERACTION: CC P31785:IL2RG; NbExp=2; IntAct=EBI-80516, EBI-80475; CC P16871:IL7R; NbExp=3; IntAct=EBI-80516, EBI-80490; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P13232-1; Sequence=Displayed; CC Name=2; CC IsoId=P13232-2; Sequence=VSP_042926; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=P13232-3; Sequence=VSP_047579, VSP_047580; CC -!- SIMILARITY: Belongs to the IL-7/IL-9 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-7 entry; CC URL="https://en.wikipedia.org/wiki/Interleukin_7"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04156; AAA59156.1; -; mRNA. DR EMBL; M29053; AAC63047.1; -; Genomic_DNA. DR EMBL; M29048; AAC63047.1; JOINED; Genomic_DNA. DR EMBL; M29049; AAC63047.1; JOINED; Genomic_DNA. DR EMBL; M29050; AAC63047.1; JOINED; Genomic_DNA. DR EMBL; M29051; AAC63047.1; JOINED; Genomic_DNA. DR EMBL; M29052; AAC63047.1; JOINED; Genomic_DNA. DR EMBL; AB102879; BAD89408.1; -; mRNA. DR EMBL; AB102883; BAD89412.1; -; mRNA. DR EMBL; EF064721; ABK41904.1; -; Genomic_DNA. DR EMBL; AC083837; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC100854; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471068; EAW87060.1; -; Genomic_DNA. DR EMBL; CH471068; EAW87062.1; -; Genomic_DNA. DR EMBL; BC047698; AAH47698.1; -; mRNA. DR CCDS; CCDS56541.1; -. [P13232-2] DR CCDS; CCDS6224.1; -. [P13232-1] DR PIR; A43527; A32223. DR PIR; B32223; B32223. DR PIR; C32223; C32223. DR RefSeq; NP_000871.1; NM_000880.3. [P13232-1] DR RefSeq; NP_001186815.1; NM_001199886.1. [P13232-2] DR RefSeq; NP_001186816.1; NM_001199887.1. DR RefSeq; NP_001186817.1; NM_001199888.1. DR RefSeq; XP_011515823.1; XM_011517521.1. [P13232-1] DR UniGene; Hs.591873; -. DR PDB; 1IL7; Model; -; A=26-177. DR PDB; 3DI2; X-ray; 2.70 A; A/C=26-177. DR PDB; 3DI3; X-ray; 2.90 A; A=26-177. DR PDBsum; 1IL7; -. DR PDBsum; 3DI2; -. DR PDBsum; 3DI3; -. DR ProteinModelPortal; P13232; -. DR SMR; P13232; 32-172. DR BioGrid; 109788; 2. DR DIP; DIP-3044N; -. DR IntAct; P13232; 2. DR STRING; 9606.ENSP00000263851; -. DR BioMuta; IL7; -. DR DMDM; 124354; -. DR PaxDb; P13232; -. DR PRIDE; P13232; -. DR DNASU; 3574; -. DR Ensembl; ENST00000263851; ENSP00000263851; ENSG00000104432. [P13232-1] DR Ensembl; ENST00000520269; ENSP00000427750; ENSG00000104432. [P13232-2] DR GeneID; 3574; -. DR KEGG; hsa:3574; -. DR UCSC; uc003ybg.3; human. [P13232-1] DR UCSC; uc022awi.1; human. [P13232-2] DR CTD; 3574; -. DR GeneCards; IL7; -. DR HGNC; HGNC:6023; IL7. DR HPA; HPA019590; -. DR MIM; 146660; gene. DR neXtProt; NX_P13232; -. DR PharmGKB; PA29839; -. DR eggNOG; ENOG410IW6Q; Eukaryota. DR eggNOG; ENOG41114MI; LUCA. DR GeneTree; ENSGT00390000004451; -. DR HOGENOM; HOG000036891; -. DR HOVERGEN; HBG004609; -. DR InParanoid; P13232; -. DR KO; K05431; -. DR OMA; NNEPNFF; -. DR OrthoDB; EOG7S220M; -. DR PhylomeDB; P13232; -. DR TreeFam; TF338065; -. DR Reactome; R-HSA-1266695; Interleukin-7 signaling. DR SignaLink; P13232; -. DR ChiTaRS; IL7; human. DR EvolutionaryTrace; P13232; -. DR GeneWiki; Interleukin_7; -. DR GenomeRNAi; 3574; -. DR NextBio; 13968; -. DR PRO; PR:P13232; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; P13232; -. DR CleanEx; HS_IL7; -. DR ExpressionAtlas; P13232; baseline and differential. DR Genevisible; P13232; HS. 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:0008083; F:growth factor activity; ISS:UniProtKB. DR GO; GO:0005139; F:interleukin-7 receptor binding; TAS:ProtInc. DR GO; GO:0045453; P:bone resorption; ISS:UniProtKB. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl. DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0043086; P:negative regulation of catalytic activity; IEA:Ensembl. DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl. DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc. DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc. DR GO; GO:0046622; P:positive regulation of organ growth; IEA:Ensembl. DR GO; GO:0045582; P:positive regulation of T cell differentiation; ISS:UniProtKB. DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl. DR GO; GO:0002360; P:T cell lineage commitment; IBA:GO_Central. DR InterPro; IPR001181; IL-7. DR InterPro; IPR018049; IL-7/IL-9_CS. DR InterPro; IPR000226; IL-7/IL-9_fam. DR PANTHER; PTHR10526; PTHR10526; 1. DR Pfam; PF01415; IL7; 1. DR PIRSF; PIRSF001942; IL-7; 1. DR PRINTS; PR00435; INTERLEUKIN7. DR SMART; SM00127; IL7; 1. DR PROSITE; PS00255; INTERLEUKIN_7_9; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytokine; KW Disulfide bond; Glycoprotein; Growth factor; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 25 FT CHAIN 26 177 Interleukin-7. FT /FTId=PRO_0000015623. FT CARBOHYD 95 95 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 116 116 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 141 141 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 27 166 {ECO:0000269|PubMed:19141282, FT ECO:0000269|PubMed:9407080}. FT DISULFID 59 154 {ECO:0000269|PubMed:19141282, FT ECO:0000269|PubMed:9407080}. FT DISULFID 72 117 {ECO:0000269|PubMed:19141282, FT ECO:0000269|PubMed:9407080}. FT VAR_SEQ 1 51 Missing (in isoform 3). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_047579. FT VAR_SEQ 77 138 Missing (in isoform 3). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_047580. FT VAR_SEQ 77 120 Missing (in isoform 2). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_042926. FT HELIX 34 39 {ECO:0000244|PDB:3DI2}. FT HELIX 41 50 {ECO:0000244|PDB:3DI2}. FT STRAND 53 55 {ECO:0000244|PDB:3DI2}. FT TURN 57 59 {ECO:0000244|PDB:3DI3}. FT HELIX 65 69 {ECO:0000244|PDB:3DI2}. FT HELIX 77 89 {ECO:0000244|PDB:3DI2}. FT HELIX 99 115 {ECO:0000244|PDB:3DI2}. FT HELIX 153 171 {ECO:0000244|PDB:3DI2}. FT TURN 172 176 {ECO:0000244|PDB:3DI2}. SQ SEQUENCE 177 AA; 20187 MW; 8FC5243F9169617F CRC64; MFHVSFRYIF GLPPLILVLL PVASSDCDIE GKDGKQYESV LMVSIDQLLD SMKEIGSNCL NNEFNFFKRH ICDANKEGMF LFRAARKLRQ FLKMNSTGDF DLHLLKVSEG TTILLNCTGQ VKGRKPAALG EAQPTKSLEE NKSLKEQKKL NDLCFLKRLL QEIKTCWNKI LMGTKEH //