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DENN domain-containing protein 1B (Connecdenn 2)

 DEN1B_MOUSE             Reviewed;         766 AA.
Q3U1T9; B2RUR7; E9Q246; Q8CG96; Q9D5B9;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
16-MAR-2016, sequence version 3.
05-JUL-2017, entry version 94.
RecName: Full=DENN domain-containing protein 1B {ECO:0000312|MGI:MGI:2447812};
AltName: Full=Connecdenn 2 {ECO:0000250|UniProtKB:Q6P3S1};
Name=Dennd1b {ECO:0000312|MGI:MGI:2447812};
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
STRAIN=C57BL/6J; TISSUE=Testis;
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).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-500; SER-516; SER-517;
SER-530; SER-533; SER-632 AND SER-633, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
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).
[5]
FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INTERACTION WITH
CD3E AND RAB35, AND MUTAGENESIS OF GLY-246; LYS-482 AND
547-ASP--LEU-549.
PubMed=26774822; DOI=10.1016/j.cell.2015.11.052;
Yang C.W., Hojer C.D., Zhou M., Wu X., Wuster A., Lee W.P.,
Yaspan B.L., Chan A.C.;
"Regulation of T cell receptor signaling by DENND1B in TH2 cells and
allergic disease.";
Cell 164:141-155(2016).
-!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB35 that
acts as a regulator of T-cell receptor (TCR) internalization in
TH2 cells. Acts by promoting the exchange of GDP to GTP,
converting inactive GDP-bound RAB35 into its active GTP-bound
form. Plays a role in clathrin-mediated endocytosis. Controls
cytokine production in TH2 lymphocytes by controlling the rate of
TCR internalization and routing to endosomes: acts by mediating
clathrin-mediated endocytosis of TCR via its interaction with the
adapter protein complex 2 (AP-2) and GEF activity. Dysregulation
leads to impaired TCR down-modulation and recycling, affecting
cytokine production in TH2 cells. {ECO:0000269|PubMed:26774822}.
-!- SUBUNIT: Interacts with RAB35 (PubMed:26774822). Interacts with
clathrin heavy chain/CLTC (By similarity). Interacts with
components of the adapter protein complex 2 (AP-2) AP2A2 and AP2B1
(By similarity). Interacts with CD3E (PubMed:26774822).
{ECO:0000250|UniProtKB:Q6P3S1, ECO:0000269|PubMed:26774822}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q6P3S1}. Cytoplasmic vesicle, clathrin-
coated vesicle {ECO:0000250|UniProtKB:Q6P3S1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=5;
IsoId=Q3U1T9-1; Sequence=Displayed;
Name=2;
IsoId=Q3U1T9-2; Sequence=VSP_058173;
Name=3;
IsoId=Q3U1T9-3; Sequence=VSP_058174, VSP_058175;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q3U1T9-4; Sequence=VSP_058172;
Note=No experimental confirmation available.;
Name=1;
IsoId=Q3U1T9-5; Sequence=VSP_058174, VSP_058176;
-!- TISSUE SPECIFICITY: Expressed in a subset of dendritic cells
(DCs). {ECO:0000269|PubMed:26774822}.
-!- DOMAIN: The FXDXF motif mediates interaction the AP-2 complex.
{ECO:0000269|PubMed:26774822}.
-!- DOMAIN: The clathrin box motif mediates interaction with clathrin.
{ECO:0000269|PubMed:26774822}.
-!- PTM: Phosphorylated on serine and/or threonine, possibly
regulating the guanine nucleotide exchange factor (GEF) activity.
{ECO:0000250|UniProtKB:Q6P3S1}.
-!- DISRUPTION PHENOTYPE: Mice are developmentally normal and fertile
but accumulate more splenic and lymph node CD4(+) and CD8(+)
effector/memory T-cells with age. TH2 cells display increased TCR-
mediated responses, due to delayed surface TCR down-modulation and
recycling, and increased production of cytokines. Mice have
increased antigen-induced allergic responses.
{ECO:0000269|PubMed:26774822}.
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EMBL; AK015524; BAB29881.1; -; mRNA.
EMBL; AK155727; BAE33404.1; -; mRNA.
EMBL; AC138741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC117623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC042698; AAH42698.1; -; mRNA.
EMBL; BC141388; AAI41389.1; -; mRNA.
EMBL; BC141389; AAI41390.1; -; mRNA.
CCDS; CCDS35728.1; -. [Q3U1T9-2]
CCDS; CCDS48384.1; -. [Q3U1T9-1]
RefSeq; NP_001159973.1; NM_001166501.1. [Q3U1T9-1]
RefSeq; NP_851992.1; NM_181347.3. [Q3U1T9-2]
UniGene; Mm.337604; -.
UniGene; Mm.474921; -.
UniGene; Mm.475093; -.
ProteinModelPortal; Q3U1T9; -.
SMR; Q3U1T9; -.
STRING; 10090.ENSMUSP00000127580; -.
iPTMnet; Q3U1T9; -.
PhosphoSitePlus; Q3U1T9; -.
EPD; Q3U1T9; -.
MaxQB; Q3U1T9; -.
PaxDb; Q3U1T9; -.
PRIDE; Q3U1T9; -.
DNASU; 329260; -.
Ensembl; ENSMUST00000094505; ENSMUSP00000092082; ENSMUSG00000056268. [Q3U1T9-2]
Ensembl; ENSMUST00000168527; ENSMUSP00000127580; ENSMUSG00000056268. [Q3U1T9-1]
Ensembl; ENSMUST00000200533; ENSMUSP00000142738; ENSMUSG00000056268. [Q3U1T9-3]
GeneID; 329260; -.
KEGG; mmu:329260; -.
UCSC; uc007cvy.2; mouse. [Q3U1T9-3]
UCSC; uc007cvz.2; mouse. [Q3U1T9-2]
UCSC; uc007cwb.2; mouse.
UCSC; uc011wtc.1; mouse. [Q3U1T9-4]
CTD; 163486; -.
MGI; MGI:2447812; Dennd1b.
eggNOG; KOG3569; Eukaryota.
eggNOG; ENOG410XT3N; LUCA.
GeneTree; ENSGT00760000118819; -.
HOGENOM; HOG000060237; -.
HOVERGEN; HBG059209; -.
InParanoid; Q3U1T9; -.
KO; K20160; -.
OMA; FAKSHAR; -.
OrthoDB; EOG091G083L; -.
TreeFam; TF343037; -.
Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; Dennd1b; mouse.
PRO; PR:Q3U1T9; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000056268; -.
CleanEx; MM_DENND1B; -.
ExpressionAtlas; Q3U1T9; baseline and differential.
Genevisible; Q3U1T9; MM.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0017137; F:Rab GTPase binding; IPI:UniProtKB.
GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0035745; P:T-helper 2 cell cytokine production; IMP:UniProtKB.
InterPro; IPR005112; dDENN_dom.
InterPro; IPR001194; DENN_dom.
InterPro; IPR005113; uDENN_dom.
Pfam; PF03455; dDENN; 1.
Pfam; PF02141; DENN; 1.
Pfam; PF03456; uDENN; 1.
SMART; SM00801; dDENN; 1.
SMART; SM00799; DENN; 1.
SMART; SM00800; uDENN; 1.
PROSITE; PS50211; DENN; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Guanine-nucleotide releasing factor;
Phosphoprotein; Protein transport; Reference proteome; Transport.
CHAIN 1 766 DENN domain-containing protein 1B.
/FTId=PRO_0000304675.
DOMAIN 14 143 uDENN. {ECO:0000255|PROSITE-
ProRule:PRU00304}.
DOMAIN 160 296 cDENN. {ECO:0000255|PROSITE-
ProRule:PRU00304}.
DOMAIN 298 375 dDENN. {ECO:0000255|PROSITE-
ProRule:PRU00304}.
MOTIF 378 382 FXDXF motif.
{ECO:0000269|PubMed:26774822}.
MOTIF 547 556 Clathrin box.
{ECO:0000269|PubMed:26774822}.
MOD_RES 500 500 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 516 516 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 533 533 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 632 632 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 363 MDRRTRENPERTFDLVLKVKCHASENEDPEVLWKFPEDFGD
QEVLQSVPKFCFPFDVERVSQNQVGQHFTFVLTDMESKQRF
GFCRLTSGGRICLCILSYLPWFEVYYKLLNTLADYLAKELE
EDLNETLKSLYNHPVPKANTPVNLSVHSCFITPDITGLPTI
PESRNLTEYFVAVDVNNMLRLYASMLHERRIIITSSKLSTL
TACLHGSAALLYPMYWQHIYIPVLPPHLLDYCCAPMPYLIG
IHSSLIERVKNKSLEDVVVLNVDTNTLESPFNDLSSLPSDV
VSALKNKLKKQSTATGDGVARAFLRAQAALFGSYRDALRYK
PGEPITFCEESFVKHRSSVMKQFLETAVNLQLFKQ -> MV
LFISITCLYVFSSFSVRTSTCLIMFSCFSLRTCNSLAVFSC
ISLSDLLKSFLMSSTIIMRYAFKSRSRFSASLKLRAHLITM
FAWSFLHRILPM (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_058172.
VAR_SEQ 1 75 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_058173.
VAR_SEQ 149 149 V -> VNQELFIASEQVLKDDPSLIP (in isoform 1
and isoform 3).
/FTId=VSP_058174.
VAR_SEQ 205 766 LTACLHGSAALLYPMYWQHIYIPVLPPHLLDYCCAPMPYLI
GIHSSLIERVKNKSLEDVVVLNVDTNTLESPFNDLSSLPSD
VVSALKNKLKKQSTATGDGVARAFLRAQAALFGSYRDALRY
KPGEPITFCEESFVKHRSSVMKQFLETAVNLQLFKQFIDGR
LAKLNAGRGFSDIFEEEITSGGFCGGSPRSYQQWVYTVKKG
GALFNTAVTKATPAVRTAYKFAKSHARLGLKEVKSRLKHKD
NEEEYGTCSGLVQYTPVYTLHNEKGENREKHKLSQTHLKRP
HKSLDGTLYDDDDDDDDIERASKISSEDGEETRAYFYESDD
SVEAQVKAPYSGEMDLLGEILDTLSTHSSDQGKLAPAKSLD
FFRSMDDIDYKPTNKSNAPSENNLALLCASGDQGEWNLGQD
DSALHGRQLPPSPRKRVSSGGLTESLFILKEESREKPLCAD
SVSGPTVVGKPAPTSGLRSQPAAPEASQTERGRAEVKQTPG
QAPLQSEDLSVPGPGSRQSTFVPWEKAGKEDTKPSKDVGLL
QEVVSLCHMSCDFQQDLNISEESRSGNQT -> VSPSHLRL
(in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_058175.
VAR_SEQ 394 766 GSPRSYQQWVYTVKKGGALFNTAVTKATPAVRTAYKFAKSH
ARLGLKEVKSRLKHKDNEEEYGTCSGLVQYTPVYTLHNEKG
ENREKHKLSQTHLKRPHKSLDGTLYDDDDDDDDIERASKIS
SEDGEETRAYFYESDDSVEAQVKAPYSGEMDLLGEILDTLS
THSSDQGKLAPAKSLDFFRSMDDIDYKPTNKSNAPSENNLA
LLCASGDQGEWNLGQDDSALHGRQLPPSPRKRVSSGGLTES
LFILKEESREKPLCADSVSGPTVVGKPAPTSGLRSQPAAPE
ASQTERGRAEVKQTPGQAPLQSEDLSVPGPGSRQSTFVPWE
KAGKEDTKPSKDVGLLQEVVSLCHMSCDFQQDLNISEESRS
GNQT -> GKDSLESNYLDI (in isoform 1).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_058176.
MUTAGEN 246 246 G->D: Abolishes guanine nucleotide
exchange factor (GEF) activity and
impaired TCR down-modulation and
recycling in TH2 cells.
{ECO:0000269|PubMed:26774822}.
MUTAGEN 482 482 K->A: Impaired interaction with the AP-2
complex and impaired TCR down-modulation
and recycling in TH2 cells; when
associated with 547-A--A-549.
{ECO:0000269|PubMed:26774822}.
MUTAGEN 547 549 DLL->AAA: Impaired interaction with the
AP-2 complex and impaired TCR down-
modulation and recycling in TH2 cells;
when associated with A-482.
{ECO:0000269|PubMed:26774822}.
SEQUENCE 766 AA; 85526 MW; 1CF3B3EEC8E5FB7F CRC64;
MDRRTRENPE RTFDLVLKVK CHASENEDPE VLWKFPEDFG DQEVLQSVPK FCFPFDVERV
SQNQVGQHFT FVLTDMESKQ RFGFCRLTSG GRICLCILSY LPWFEVYYKL LNTLADYLAK
ELEEDLNETL KSLYNHPVPK ANTPVNLSVH SCFITPDITG LPTIPESRNL TEYFVAVDVN
NMLRLYASML HERRIIITSS KLSTLTACLH GSAALLYPMY WQHIYIPVLP PHLLDYCCAP
MPYLIGIHSS LIERVKNKSL EDVVVLNVDT NTLESPFNDL SSLPSDVVSA LKNKLKKQST
ATGDGVARAF LRAQAALFGS YRDALRYKPG EPITFCEESF VKHRSSVMKQ FLETAVNLQL
FKQFIDGRLA KLNAGRGFSD IFEEEITSGG FCGGSPRSYQ QWVYTVKKGG ALFNTAVTKA
TPAVRTAYKF AKSHARLGLK EVKSRLKHKD NEEEYGTCSG LVQYTPVYTL HNEKGENREK
HKLSQTHLKR PHKSLDGTLY DDDDDDDDIE RASKISSEDG EETRAYFYES DDSVEAQVKA
PYSGEMDLLG EILDTLSTHS SDQGKLAPAK SLDFFRSMDD IDYKPTNKSN APSENNLALL
CASGDQGEWN LGQDDSALHG RQLPPSPRKR VSSGGLTESL FILKEESREK PLCADSVSGP
TVVGKPAPTS GLRSQPAAPE ASQTERGRAE VKQTPGQAPL QSEDLSVPGP GSRQSTFVPW
EKAGKEDTKP SKDVGLLQEV VSLCHMSCDF QQDLNISEES RSGNQT


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