PREX2_MOUSE
ID PREX2_MOUSE Reviewed; 1598 AA.
AC Q3LAC4; E9QMG3; Q3UQI2; Q3UU18; Q9CXD5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein;
DE Short=P-Rex2;
DE Short=PtdIns(3,4,5)-dependent Rac exchanger 2;
DE AltName: Full=DEP domain-containing protein 2;
GN Name=Prex2; Synonyms=Depdc2;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=15304343; DOI=10.1016/j.febslet.2004.06.096;
RA Donald S., Hill K., Lecureuil C., Barnouin R., Krugmann S.,
RA John Coadwell W., Andrews S.R., Walker S.A., Hawkins P.T., Stephens L.R.,
RA Welch H.C.E.;
RT "P-Rex2, a new guanine-nucleotide exchange factor for Rac.";
RL FEBS Lett. 572:172-176(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-962 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 251-1598 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head, Lung, and Thymus;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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).
CC -!- FUNCTION: Functions as a RAC1 guanine nucleotide exchange factor (GEF),
CC activating Rac proteins by exchanging bound GDP for free GTP. Its
CC activity is synergistically activated by phosphatidylinositol 3,4,5-
CC trisphosphate and the beta gamma subunits of heterotrimeric G protein.
CC Mediates the activation of RAC1 in a PI3K-dependent manner. May be an
CC important mediator of Rac signaling, acting directly downstream of both
CC G protein-coupled receptors and phosphoinositide 3-kinase (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RAC1. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3LAC4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3LAC4-2; Sequence=VSP_025164, VSP_025165;
CC -!- DOMAIN: PH domain confers substrate specificity and recognition. Able
CC to discriminate between RAC1, RHOA, and CDC42 (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: DH domain alone was unable to confer substrate specificity and
CC recognition. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB31066.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE25059.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM109952; CAJ33348.1; -; mRNA.
DR EMBL; AC102481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC102529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC102631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC164600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK018093; BAB31066.1; ALT_SEQ; mRNA.
DR EMBL; AK138884; BAE23811.1; -; mRNA.
DR EMBL; AK142414; BAE25059.1; ALT_INIT; mRNA.
DR CCDS; CCDS48217.1; -. [Q3LAC4-1]
DR RefSeq; NP_083801.1; NM_029525.1. [Q3LAC4-1]
DR AlphaFoldDB; Q3LAC4; -.
DR SMR; Q3LAC4; -.
DR BioGRID; 224637; 10.
DR IntAct; Q3LAC4; 1.
DR MINT; Q3LAC4; -.
DR STRING; 10090.ENSMUSP00000027056; -.
DR iPTMnet; Q3LAC4; -.
DR PhosphoSitePlus; Q3LAC4; -.
DR MaxQB; Q3LAC4; -.
DR PaxDb; Q3LAC4; -.
DR PeptideAtlas; Q3LAC4; -.
DR PRIDE; Q3LAC4; -.
DR ProteomicsDB; 291652; -. [Q3LAC4-1]
DR ProteomicsDB; 291653; -. [Q3LAC4-2]
DR Antibodypedia; 2764; 70 antibodies from 15 providers.
DR DNASU; 109294; -.
DR Ensembl; ENSMUST00000027056; ENSMUSP00000027056; ENSMUSG00000048960. [Q3LAC4-1]
DR GeneID; 109294; -.
DR KEGG; mmu:109294; -.
DR UCSC; uc007ahs.2; mouse. [Q3LAC4-1]
DR UCSC; uc007aht.1; mouse. [Q3LAC4-2]
DR CTD; 80243; -.
DR MGI; MGI:1923385; Prex2.
DR VEuPathDB; HostDB:ENSMUSG00000048960; -.
DR eggNOG; KOG3519; Eukaryota.
DR eggNOG; KOG4428; Eukaryota.
DR GeneTree; ENSGT00940000155894; -.
DR HOGENOM; CLU_003935_0_0_1; -.
DR InParanoid; Q3LAC4; -.
DR OMA; VRQYNQK; -.
DR OrthoDB; 24217at2759; -.
DR PhylomeDB; Q3LAC4; -.
DR TreeFam; TF328639; -.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 109294; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Prex2; mouse.
DR PRO; PR:Q3LAC4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3LAC4; protein.
DR Bgee; ENSMUSG00000048960; Expressed in left lung lobe and 201 other tissues.
DR ExpressionAtlas; Q3LAC4; baseline and differential.
DR Genevisible; Q3LAC4; MM.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:MGI.
DR CDD; cd04439; DEP_1_P-Rex; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037367; Rex2_DEP_1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00049; DEP; 2.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50186; DEP; 2.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Guanine-nucleotide releasing factor;
KW Reference proteome; Repeat.
FT CHAIN 1..1598
FT /note="Phosphatidylinositol 3,4,5-trisphosphate-dependent
FT Rac exchanger 2 protein"
FT /id="PRO_0000286796"
FT DOMAIN 15..206
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 237..353
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 382..456
FT /note="DEP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 483..558
FT /note="DEP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 584..663
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 669..746
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1573..1598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 698..734
FT /note="TVAAAAGLHPGQCIIKVNGINVSKETHASVIAHVTAC -> ETFFAAASRSA
FT PAGPLALPCPTEGSPQSARNGPLSLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025164"
FT VAR_SEQ 735..1598
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025165"
FT CONFLICT 1166
FT /note="N -> T (in Ref. 1; CAJ33348)"
FT /evidence="ECO:0000305"
FT CONFLICT 1176..1178
FT /note="AFE -> PFD (in Ref. 1; CAJ33348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1598 AA; 181717 MW; AC9507BC9CC5EAD6 CRC64;
MSDESAREVD KQLRLRVCVL SELQKTERDY VGTLEFLVSA FLHRMNQCAA AKVDKNVTEE
TVKMLFSNIE EILIVHKEFL KVVEECLYPE PSAQQEVGAC FLHFKDKFRI YDEYCSNHEK
AQKLLLELNK IRTIRTFLLN CMLLGGRKNT DVPLEGYLVT PIQRICKYPL LLKELLKRTP
RRHSDYTAVM EALQAMKAVC SNINEAKRQM EKLEVLEEWQ AHIEGWEGSN ITDTCTEMLM
CGVLMKISSG NIQERVFFLF DNLLVYCKRK HRRLKNSKAS TDGYRYVFRG RINTEVMEVE
NVDDGTADFH SSGHIVVNGW KIHNTAKNKW FVCMAKSPEE KHEWFEAILK ERERRKGLKL
GMEQDTWVMI SEQGEKLYKM MCKQGNLIKD RKRKLTTFPK CFLGSEFVSW LLEIGEIHRP
EEGVHLGQAL LENGIIHHVT DKHQFKPEQM LYRFRYDDGT FYPRSEMQDV ISKGVRLYCR
LHSLFTPVVR DKDYHLRTYK SVVMANKLID WLIAQGDCRT REEAMIFAVG LCDNGFMHHV
LEKSEFKDEP LLFRFFADEE MEGSNMKHRL MKHDLKVVEN VIAKSLLIKS NEGSYGFGLE
DKNKVPIIKL VEKGSNAEMA GMEVGKKIFA INGDLVFLRP FPEVDCFLKS CLNSRKPLRV
LVSTKPRETV KIPDSADGLG FQIRGFGPSV VHAVGRGTVA AAAGLHPGQC IIKVNGINVS
KETHASVIAH VTACRKYKRP MKQDSIQWVY DSLESAQEDI QKSHSKPPGD GAGDAFECKV
EDVIDKFNTM AIIDGKKEHV SLTVDNVHLE YGVVYEYDST AGTKCNVVEK MVEPKGFFSL
TAKILEALAK SDEHFVQNCT SLNSLNEVIA TDLQSKFTSM CSERIEHVCH RISSYGRFSR
VLKNRAWPTF KQAKPKISPL HSSDFCPTNC HVNVMEVSYP KTSTSLGSAF GVQLDSRKHN
SHDKENKSVE PGKLSPMVYI QHTITTMAAP SGLSLGHKDG HGLQYLLKEE DLETQDIYHK
LLGKLQTALK EVEMSVCQID DLLSSITYSP KLERKTTECV TPMDSDNEKG ERNSKRVCFN
VAGDEQEDSG HDTVSNRDSY SDCNSNRNSI ASFTSICSSQ CSSYFHSDEM DSGDELPISV
RISHDKQDKI HTCLEQLFSQ IDSIINLLKG QAVIRAFEQT KYLTPGRGLQ EFQQEMEAKL
SCPRRLRLHL KQDPWNLPSS IQALAQSIRK HAEEVKCRIL LALLEYSDSE TQLRRDMVFC
QSLVATVCAF SEQLMAALNQ MFDNSKENEM ETCEASRRWL DQIANAGVLF HFQSLLSPNL
KDEQAMLEDT LVALFDLEKV SFFFKPSEED PLVANVPLTY QVEGSRQALK VYFYMDSYHF
EQLPQRLKNG GGFKIHPVLF SQALESMEGY CYRDNISVEE FQAQINTASL EKVKQYNQKL
RAFYLDKSNS PPNTTSKAAY IDKLMKPLNA LDELYRLITS FIRSKRIAAC VNTPCSASGV
GLLSVSSELC DRLGACHIIM CSSGVHRCTL SVTLEQTITL ARSHGLPPRY IMQAMDVMRK
QGARVQNTAK NLGVRDRTPQ SAPRLYKLCE PPPPVGEE
