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Differentially expressed in FDCP 6 (DEF-6) (IRF4-binding protein) (SWAP-70-like adapter of T-cells)

 DEFI6_MOUSE             Reviewed;         630 AA.
Q8C2K1; A1KXF9; B2KF17; Q0VBU6; Q3V3M7; Q80XA9; Q9CRJ2;
10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-MAR-2018, entry version 117.
RecName: Full=Differentially expressed in FDCP 6;
Short=DEF-6;
AltName: Full=IRF4-binding protein;
AltName: Full=SWAP-70-like adapter of T-cells;
Name=Def6; Synonyms=Ibp, Slat;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
LOCATION, INDUCTION, INTERACTION WITH ZAP70, AND TISSUE SPECIFICITY.
STRAIN=B10.A;
PubMed=12648457; DOI=10.1016/S1074-7613(03)00054-2;
Tanaka Y., Bi K., Kitamura R., Hong S., Altman Y., Matsumoto A.,
Tabata H., Lebedeva S., Bushway P.J., Altman A.;
"SWAP-70-like adapter of T cells, an adapter protein that regulates
early TCR-initiated signaling in Th2 lineage cells.";
Immunity 18:403-414(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=12651066; DOI=10.1016/S0198-8859(03)00024-7;
Gupta S., Lee A.E., Hu C., Fanzo J.C., Goldberg I., Cattoretti G.,
Pernis A.B.;
"Molecular cloning of IBP, a SWAP-70 homologous GEF, which is highly
expressed in the immune system.";
Hum. Immunol. 64:389-401(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, AND DISEASE.
PubMed=12923183; DOI=10.1074/jbc.M308960200;
Gupta S., Fanzo J.C., Hu C., Cox D., Jang S.Y., Lee A.E.,
Greenberg S., Pernis A.B.;
"T cell receptor engagement leads to the recruitment of IBP, a novel
guanine nucleotide exchange factor, to the immunological synapse.";
J. Biol. Chem. 278:43541-43549(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent
guanine nucleotide exchange factor (GEF) which plays a role in the
activation of Rho GTPases RAC1, RhoA and CDC42. Can regulate cell
morphology in cooperation with activated RAC1. Plays a role in Th2
(T helper cells) development and/or activation, perhaps by
interfering with ZAP70 signaling. Required for optimal T-cell
effector function, lymphocyte homeostasis and the prevention of
systemic autoimmunity (By similarity). {ECO:0000250,
ECO:0000269|PubMed:12648457, ECO:0000269|PubMed:12923183}.
-!- SUBUNIT: Interacts with IRF4, activated RAC1 and F-actin. Both the
phosphorylated and non-phosphorylated forms bind
phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) (By
similarity). Interacts with ZAP70. {ECO:0000250,
ECO:0000269|PubMed:12648457}.
-!- INTERACTION:
Q61738-6:Itga7; NbExp=3; IntAct=EBI-2121188, EBI-1786329;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12648457}.
Cell membrane {ECO:0000269|PubMed:12648457}. Nucleus
{ECO:0000250|UniProtKB:Q9H4E7}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q9H4E7}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:Q9H4E7}. Cell projection, filopodium
{ECO:0000250|UniProtKB:Q9H4E7}. Note=Recruited to the plasma
membrane upon binding phosphatidylinositol 3,4,5-trisphosphate.
Binds to actin filaments. {ECO:0000250|UniProtKB:Q9H4E7}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8C2K1-1; Sequence=Displayed;
Name=2;
IsoId=Q8C2K1-2; Sequence=VSP_026671;
-!- TISSUE SPECIFICITY: Thymus. {ECO:0000269|PubMed:12648457}.
-!- INDUCTION: Up-regulated in differentiating Th2 cells and down-
regulated in Th1 cells. {ECO:0000269|PubMed:12648457}.
-!- DOMAIN: The PH domain is essential for phosphatidylinositol 3,4,5-
trisphosphate binding.
-!- PTM: Tyrosine-phosphorylated by tyrosine-protein kinase LCK in
response to T-cell activation. {ECO:0000250}.
-!- DISEASE: Note=Defects in Def6 results in spontaneous development
of a lupus-like syndrome in aging female mice. It is characterized
by the accumulation of effector/memory T-cells and IgG B-cells,
profound hypergammaglobulinemia, autoantibody production, and
glomerulonephritis. {ECO:0000269|PubMed:12923183}.
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EMBL; AY278770; AAQ19048.1; -; mRNA.
EMBL; AF329497; AAO67354.1; -; mRNA.
EMBL; AY241695; AAO91768.1; -; mRNA.
EMBL; AK010356; BAB26876.1; -; mRNA.
EMBL; AK038050; BAE20528.1; -; mRNA.
EMBL; AK088460; BAC40366.1; -; mRNA.
EMBL; CT009658; CAQ51695.1; -; Genomic_DNA.
EMBL; BC120500; AAI20501.1; -; mRNA.
EMBL; BC131953; AAI31954.1; -; mRNA.
CCDS; CCDS28574.1; -. [Q8C2K1-1]
RefSeq; NP_081461.2; NM_027185.3.
UniGene; Mm.204731; -.
ProteinModelPortal; Q8C2K1; -.
IntAct; Q8C2K1; 2.
STRING; 10090.ENSMUSP00000002327; -.
iPTMnet; Q8C2K1; -.
PhosphoSitePlus; Q8C2K1; -.
EPD; Q8C2K1; -.
PaxDb; Q8C2K1; -.
PeptideAtlas; Q8C2K1; -.
PRIDE; Q8C2K1; -.
GeneID; 23853; -.
KEGG; mmu:23853; -.
UCSC; uc008bqi.2; mouse. [Q8C2K1-1]
UCSC; uc012aoe.1; mouse. [Q8C2K1-2]
CTD; 50619; -.
MGI; MGI:1346328; Def6.
eggNOG; ENOG410IG09; Eukaryota.
eggNOG; ENOG410Z316; LUCA.
HOVERGEN; HBG053201; -.
InParanoid; Q8C2K1; -.
PhylomeDB; Q8C2K1; -.
TreeFam; TF333160; -.
PRO; PR:Q8C2K1; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_DEF6; -.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF47473; SSF47473; 2.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 630 Differentially expressed in FDCP 6.
/FTId=PRO_0000294523.
DOMAIN 216 312 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
COMPBIAS 57 60 Poly-Asp.
COMPBIAS 331 497 Glu-rich.
MOD_RES 210 210 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9H4E7}.
MOD_RES 225 225 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9H4E7}.
MOD_RES 590 590 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4E7}.
VAR_SEQ 33 405 Missing (in isoform 2).
{ECO:0000303|PubMed:12648457}.
/FTId=VSP_026671.
CONFLICT 48 48 P -> T (in Ref. 3; BAE20528).
{ECO:0000305}.
CONFLICT 134 134 P -> Q (in Ref. 3; BAE20528).
{ECO:0000305}.
CONFLICT 161 161 E -> K (in Ref. 2; AAO91768, 3; BAE20528
and 4; AAI20501/AAI31954). {ECO:0000305}.
CONFLICT 279 279 C -> S (in Ref. 2; AAO91768).
{ECO:0000305}.
SEQUENCE 630 AA; 73454 MW; 309E060522DD91E0 CRC64;
MALRKELLKS IWYAFTALDV EKSGKVSKSQ LKVLSHNLYT VLNIPHDPVA LEEHFRDDDD
GPVSSQGYMP YLNKYILDKV EEGAFVKEHF DELCWTLTAK KNYRADGIGS SPLSNQDAFR
LWCLFNFLSE DKYPLIMVPD EVEYLLKKLL GSLSLEMGLG ELEELLAQDA QSAQTAVGLS
VWQFLELFNS GRCLRGVGRD SLSMAIQEVY QELIQDVLKQ GYLWKRGHLR RNWAERWFQL
QPSSLCYFGS EECKEKRGTI PLDAHCCVEV LPDREGKRCM FCVKTASRTY EMSASDTRQR
QEWTAAIQTA IRLQAEGKTS LHKDLKQKRR EQREQRERRR AAKEEELLRL QQLQEEKERK
LQELELLQEA QRQAERLLQE EEERRRSQHK ELQQALEGQL REAEQARASM QAEMELKKEE
AARQRQRIAE LEEMQERLQE ALQLEVKARR DEEAVRLAQT RLLEEEEEKL KQLMHLKEEQ
ERYIERAQQE KQELQQEMAL QSRSLQHAQQ QLEEVRQNRQ RADEDVEAAQ RKLRQASTNV
KHWNVQMNRL MHPIEPGDKR PTTSSSFTGF QPPPLARRDS SLKRLTRWGS QGNRTLSVNS
SEQKSLNGGD ETPILALASQ EEKLDPAPGN


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