ESIP1_MOUSE
ID ESIP1_MOUSE Reviewed; 314 AA.
AC Q8VDI1; Q80WK5; Q8VDW6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Epithelial-stromal interaction protein 1;
GN Name=Epsti1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RA Uwanogho D.A., Mellodew K., Molloy G., Galloway D., Starling B.B.,
RA Crossland N., Price J.;
RT "A novel program of gene expression driven by Notch, is associated with
RT commitment in neural stem cell lines.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Egg, Head, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY LPS AND IFNG, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29217193; DOI=10.1016/j.bbrc.2017.12.014;
RA Kim Y.H., Lee J.R., Hahn M.J.;
RT "Regulation of inflammatory gene expression in macrophages by epithelial-
RT stromal interaction 1 (Epsti1).";
RL Biochem. Biophys. Res. Commun. 496:778-783(2018).
CC -!- FUNCTION: Plays a role in M1 macrophage polarization and is required
CC for the proper regulation of gene expression during M1 versus M2
CC macrophage differentiation (PubMed:29217193). Might play a role in
CC RELA/p65 and STAT1 phosphorylation and nuclear localization upon
CC activation of macrophages (PubMed:29217193).
CC {ECO:0000269|PubMed:29217193}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Epsti1a;
CC IsoId=Q8VDI1-1; Sequence=Displayed;
CC Name=2; Synonyms=Epsti1b;
CC IsoId=Q8VDI1-2; Sequence=VSP_030203, VSP_030204;
CC -!- TISSUE SPECIFICITY: Expressed in the spleen, with expression in T
CC cells, B cells, natural killer cells and natural killer T cells and
CC high expression in monocytes and macrophages.
CC {ECO:0000269|PubMed:29217193}.
CC -!- INDUCTION: Up-regulated in macrophages upon induction by
CC lipopolysaccharides (LPS) and IFNG. {ECO:0000269|PubMed:29217193}.
CC -!- DISRUPTION PHENOTYPE: Down-regulation of M1 macrophage marker genes,
CC including Il12a, Il12b, Cxcl9, Cxcl10, Cxcl11, Hif1a and Il23a, and up-
CC regulation of M2 marker genes, including Arg1, Ym1, Msr1 and Ccl17, in
CC M1 macrophages. In bone marrow derived macrophages, impaired induction
CC of M1 macrophage marker gene expression and impaired phosphorylation
CC and nuclear localization of Rela/p65 and Stat1 after LPS and IFNG
CC stimulation and enhanced M2 macrophage marker gene expression after Il4
CC stimulation. Reduced number of MHC class II- and F4/80-expressing cells
CC within the population of M1 marker-expressing macrophages.
CC {ECO:0000269|PubMed:29217193}.
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DR EMBL; AY239223; AAP23934.1; -; mRNA.
DR EMBL; AY239224; AAP23935.1; -; mRNA.
DR EMBL; AK077223; BAC36694.1; -; mRNA.
DR EMBL; AK077376; BAC36775.1; -; mRNA.
DR EMBL; AK135710; BAE22621.1; -; mRNA.
DR EMBL; AK136055; BAE22799.1; -; mRNA.
DR EMBL; AC125130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020120; AAH20120.1; -; mRNA.
DR EMBL; BC021821; AAH21821.1; -; mRNA.
DR CCDS; CCDS56971.1; -. [Q8VDI1-1]
DR CCDS; CCDS88718.1; -. [Q8VDI1-2]
DR RefSeq; NP_083771.1; NM_029495.2.
DR RefSeq; NP_849147.1; NM_178825.4. [Q8VDI1-2]
DR AlphaFoldDB; Q8VDI1; -.
DR SMR; Q8VDI1; -.
DR STRING; 10090.ENSMUSP00000022591; -.
DR iPTMnet; Q8VDI1; -.
DR PhosphoSitePlus; Q8VDI1; -.
DR EPD; Q8VDI1; -.
DR jPOST; Q8VDI1; -.
DR MaxQB; Q8VDI1; -.
DR PaxDb; Q8VDI1; -.
DR PeptideAtlas; Q8VDI1; -.
DR PRIDE; Q8VDI1; -.
DR ProteomicsDB; 275540; -. [Q8VDI1-1]
DR ProteomicsDB; 275541; -. [Q8VDI1-2]
DR Antibodypedia; 3005; 216 antibodies from 26 providers.
DR DNASU; 108670; -.
DR Ensembl; ENSMUST00000227903; ENSMUSP00000154502; ENSMUSG00000022014. [Q8VDI1-2]
DR GeneID; 108670; -.
DR KEGG; mmu:108670; -.
DR UCSC; uc007usd.2; mouse. [Q8VDI1-2]
DR UCSC; uc007use.2; mouse. [Q8VDI1-1]
DR CTD; 94240; -.
DR MGI; MGI:1915168; Epsti1.
DR VEuPathDB; HostDB:ENSMUSG00000022014; -.
DR eggNOG; ENOG502RZCM; Eukaryota.
DR GeneTree; ENSGT00390000013820; -.
DR InParanoid; Q8VDI1; -.
DR OrthoDB; 1284389at2759; -.
DR TreeFam; TF335788; -.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 108670; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Epsti1; mouse.
DR PRO; PR:Q8VDI1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8VDI1; protein.
DR Bgee; ENSMUSG00000022014; Expressed in peripheral lymph node and 99 other tissues.
DR ExpressionAtlas; Q8VDI1; baseline and differential.
DR InterPro; IPR026185; EPSTI1.
DR PANTHER; PTHR22529; PTHR22529; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..314
FT /note="Epithelial-stromal interaction protein 1"
FT /id="PRO_0000314035"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 71..180
FT /evidence="ECO:0000255"
FT COMPBIAS 58..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 217..229
FT /note="KLPVLLRDPSWAG -> VSGNSRRLLSATF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030203"
FT VAR_SEQ 230..314
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030204"
FT CONFLICT 178
FT /note="T -> K (in Ref. 4; AAH20120)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="L -> F (in Ref. 4; AAH20120)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="L -> P (in Ref. 4; AAH20120)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="R -> K (in Ref. 4; AAH20120)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="E -> K (in Ref. 4; AAH20120)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="L -> I (in Ref. 1; AAP23935, 2; BAC36694/BAC36775/
FT BAE22621/BAE22799 and 4; AAH20120/AAH21821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 36098 MW; C11095623C6DA07D CRC64;
MYTRSKVVGP GLGTSSISRD HAGAGQRREL GLQQNRRQSL EVAAPEGPKM ERQGHADQGS
AGTYTLIAPN ESRRQKIQRI AEQELADLER WKQQNRAKPV YLVPQRLGGS QSEAEVRQKQ
QLQQMRSKYQ QKLKRDESIR IRKEAEEAKF QKMKAIQREK SNKLEEKKQL QEDIRRATFR
EHHQSKTAEL LSRLDTERRN RSACLIAPPA TQSSRWKLPV LLRDPSWAGS QAHRDSPQKE
DNPRLQKTRD GHQKNKLLET KGQHQEEERA QIHQAEHWRV NNAFLDRLQG KSQPGGLEQS
GGCCNMNSTD SWGL
