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FYVE, RhoGEF and PH domain-containing protein 2

 FGD2_MOUSE              Reviewed;         655 AA.
Q8BY35; O88841; Q2L9D2; Q3U195; Q7TSE3; Q8VDH4;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-MAR-2018, entry version 124.
RecName: Full=FYVE, RhoGEF and PH domain-containing protein 2;
Name=Fgd2;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Spleen;
PubMed=10458911; DOI=10.1006/geno.1999.5903;
Pasteris N.G., Gorski J.L.;
"Isolation, characterization, and mapping of the mouse and human Fgd2
genes, faciogenital dysplasia (FGD1; Aarskog syndrome) gene
homologues.";
Genomics 60:57-66(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-287; ASN-288; GLN-454
AND TRP-455, AND DOMAIN DH; PH AND FYVE-TYPE ZINC-FINGER.
STRAIN=C57BL/10 X DBA/2; TISSUE=Spleen;
DOI=10.1074/jbc.M803957200;
Huber C., Martensson A., Bokoch G.M., Nemazee D., Gavin A.L.;
"FGD2, a CDC42-specific exchange factor expressed by antigen-
presenting cells, localizes to early endosomes and active membrane
ruffles.";
J. Biol. Chem. 283:34002-34012(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and 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;
Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
Nagaraja R.;
"Genomic sequence analysis in the mouse T-complex region.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Czech II; TISSUE=Mammary gland;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-39; SER-47;
THR-644 AND SER-654, AND 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: Activates CDC42, a member of the Ras-like family of
Rho- and Rac proteins, by exchanging bound GDP for free GTP.
Activates JNK1 via CDC42 but not RAC1. Binds to
phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-
trisphosphate, phosphatidylinositol 5-monophosphate,
phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-
monophosphate. {ECO:0000269|Ref.2}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.2}. Nucleus
{ECO:0000269|Ref.2}. Early endosome {ECO:0000269|Ref.2}. Early
endosome membrane {ECO:0000269|Ref.2}. Cell projection, ruffle
membrane {ECO:0000269|Ref.2}. Cytoplasm, cytoskeleton
{ECO:0000305|Ref.2}. Note=Recruitment to the endosome and ruffle
membrane requires the presence of phosphoinositides.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8BY35-1; Sequence=Displayed;
Name=2;
IsoId=Q8BY35-2; Sequence=VSP_013073;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Lymph node, spleen, B-lymphocytes and
macrophages (at protein level). Expressed at high levels in lymph
node, spleen, B-lymphocytes and bone marrow macrophages. Expressed
at lower levels in mature bone marrow dendritic cells. In both
immature and mature B-cells, expression is down-regulated by prior
B-cell receptor signaling. Expression remains high in resting B
and memory cells but declines upon differentiation into plasma
cells. {ECO:0000269|PubMed:10458911, ECO:0000269|Ref.2}.
-!- DOMAIN: The FYVE-type zinc-finger is necessary for early endosome
localization. Recruitment to endosomal membranes via this domain
requires the presence of phosphatidylinositol 3-phosphate or other
phosphatidylinositides. {ECO:0000269|Ref.2}.
-!- DOMAIN: The PH domain is necessary for localization to the ruffle
membrane. Recruitment to ruffle membrane occurs through binding of
phosphoinositides by the PH domain. This domain also contributes
to the lipid-binding properties of the protein.
{ECO:0000269|Ref.2}.
-!- DOMAIN: The DH domain is necessary for its ability to activate
JNK1 via CDC42. {ECO:0000269|Ref.2}.
-!- SEQUENCE CAUTION:
Sequence=AAC35430.1; Type=Frameshift; Positions=606; Evidence={ECO:0000305};
Sequence=AAP45200.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF017368; AAC35430.1; ALT_FRAME; mRNA.
EMBL; DQ344523; ABC70180.1; -; mRNA.
EMBL; AK042260; BAC31206.1; -; mRNA.
EMBL; AK156151; BAE33605.1; -; mRNA.
EMBL; AY301264; AAP45199.1; -; Genomic_DNA.
EMBL; AY301264; AAP45200.1; ALT_SEQ; Genomic_DNA.
EMBL; BC021845; AAH21845.1; -; mRNA.
CCDS; CCDS37537.1; -. [Q8BY35-1]
RefSeq; NP_001153010.1; NM_001159538.1.
RefSeq; NP_038738.2; NM_013710.4. [Q8BY35-1]
RefSeq; XP_006524363.1; XM_006524300.3. [Q8BY35-2]
RefSeq; XP_011244775.1; XM_011246473.2. [Q8BY35-2]
UniGene; Mm.279187; -.
ProteinModelPortal; Q8BY35; -.
SMR; Q8BY35; -.
BioGrid; 204940; 1.
STRING; 10090.ENSMUSP00000024810; -.
iPTMnet; Q8BY35; -.
PhosphoSitePlus; Q8BY35; -.
EPD; Q8BY35; -.
PaxDb; Q8BY35; -.
PeptideAtlas; Q8BY35; -.
PRIDE; Q8BY35; -.
Ensembl; ENSMUST00000024810; ENSMUSP00000024810; ENSMUSG00000024013. [Q8BY35-1]
GeneID; 26382; -.
KEGG; mmu:26382; -.
UCSC; uc008bsx.2; mouse. [Q8BY35-1]
CTD; 221472; -.
MGI; MGI:1347084; Fgd2.
eggNOG; KOG4424; Eukaryota.
eggNOG; ENOG410XRXV; LUCA.
GeneTree; ENSGT00890000139342; -.
HOGENOM; HOG000220866; -.
HOVERGEN; HBG007506; -.
InParanoid; Q8BY35; -.
KO; K05721; -.
OMA; DPMERYL; -.
OrthoDB; EOG091G03FU; -.
PhylomeDB; Q8BY35; -.
TreeFam; TF316247; -.
Reactome; R-MMU-193648; NRAGE signals death through JNK.
Reactome; R-MMU-194840; Rho GTPase cycle.
Reactome; R-MMU-416482; G alpha (12/13) signalling events.
PRO; PR:Q8BY35; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024013; -.
CleanEx; MM_FGD2; -.
ExpressionAtlas; Q8BY35; baseline and differential.
Genevisible; Q8BY35; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IDA:MGI.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0001726; C:ruffle; IDA:MGI.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:MGI.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IDA:MGI.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IGI:MGI.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
CDD; cd13386; PH1_FGD2; 1.
CDD; cd13236; PH2_FGD1-4; 1.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR035941; FGD1-4_PH2.
InterPro; IPR037797; FGD2_PH1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000306; Znf_FYVE.
InterPro; IPR017455; Znf_FYVE-rel.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF01363; FYVE; 1.
Pfam; PF00169; PH; 2.
Pfam; PF00621; RhoGEF; 1.
SMART; SM00064; FYVE; 1.
SMART; SM00233; PH; 2.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 2.
PROSITE; PS50178; ZF_FYVE; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Endosome;
Guanine-nucleotide releasing factor; Membrane; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
CHAIN 1 655 FYVE, RhoGEF and PH domain-containing
protein 2.
/FTId=PRO_0000080943.
DOMAIN 102 290 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 319 418 PH 1. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 544 641 PH 2. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
ZN_FING 458 518 FYVE-type. {ECO:0000255|PROSITE-
ProRule:PRU00091}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 644 644 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 654 654 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 194 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013073.
MUTAGEN 287 287 S->A: No effect on early endosome
localization and reduced JNK1 activation;
when associated with A-288.
{ECO:0000269|Ref.2}.
MUTAGEN 288 288 N->A: No effect on early endosome
localization and reduced JNK1 activation;
when associated with A-287.
{ECO:0000269|Ref.2}.
MUTAGEN 454 454 Q->K: Loss of early endosome
localization; when associated with T-455.
{ECO:0000269|Ref.2}.
MUTAGEN 455 455 W->T: Loss of early endosome
localization; when associated with K-454.
{ECO:0000269|Ref.2}.
CONFLICT 39 39 S -> I (in Ref. 1; ABC70180 and 2;
AAC35430). {ECO:0000305}.
CONFLICT 543 543 E -> D (in Ref. 1; ABC70180).
{ECO:0000305}.
CONFLICT 560 561 RS -> ST (in Ref. 3; BAE33605).
{ECO:0000305}.
SEQUENCE 655 AA; 74634 MW; F5272F107A29BDBE CRC64;
MERACEKQDS VCNLVAVFEN NRTPGEAPGS HSLEDQPHSP EHQLSLSPEP WEAPPVKEAL
KSEFRPVSRT YLSSLKNKLS SGAWRRSCQP GVSPGPETQE PEEKRVVREL LETEQAYVAR
LHLLDQVFFQ ELLREAGRSK AFPEDVVKLI FSNISSIYRF HAQFFLPELQ RRVDDWAATP
RIGDVIQKLA PFLKMYSEYV KNFERAAELL ATWMDKSQPF QEVVTRIQCS EASSSLTLQH
HMLEPVQRIP RYELLLKEYV QKLPAQAPDL EDAQRALDMI FSAAQHSNAA IAEMERLQGL
WDVYQRLGLE DDIVDPSNTL LREGPVLKIS FRRSDPMERY LVLFNNMLLY CVPRVLQVGA
QFQVRTRIDV AGMKVRELTD AEFPHSFLVS GKQRTLELQA RSRDEMVSWM QACQAAIDQV
EKRSETFKAA VQGPQGDTQE PKPQVEELGL RAPQWVRDKM VTMCMRCQEP FNALTRRRHH
CRACGYVVCA KCSDYRAELK YDSNRPNRVC LTCYTFLTGN VLPQGKEDKR RGILEKEASA
APEQSLVCSF LQLIGDKCSR SLPRSWCVIP RDDPLVLYVY AAPQDTKAHT SIPLLGYQVI
SGPQGDPRVF QLQQSGQQYT FKAESVELQG RWVTAIKRAA SGRTPEGPDE EDVSD


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