PREX1_MOUSE
ID PREX1_MOUSE Reviewed; 1650 AA.
AC Q69ZK0; A2A5U1; Q6PFD4; Q8BN08;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein;
DE Short=P-Rex1;
DE Short=PtdIns(3,4,5)-dependent Rac exchanger 1;
GN Name=Prex1; Synonyms=Kiaa1415;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1144-1650 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Fetal brain;
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 FUNCTION, AND INTERACTION WITH RAC1 AND RAC2.
RX PubMed=16243036; DOI=10.1016/j.cub.2005.09.014;
RA Dong X., Mo Z., Bokoch G., Guo C., Li Z., Wu D.;
RT "P-Rex1 is a primary Rac2 guanine nucleotide exchange factor in mouse
RT neutrophils.";
RL Curr. Biol. 15:1874-1879(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991; SER-1186 AND SER-1191,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 INTERACTION WITH AUTS2.
RX PubMed=25533347; DOI=10.1016/j.celrep.2014.11.045;
RA Hori K., Nagai T., Shan W., Sakamoto A., Taya S., Hashimoto R., Hayashi T.,
RA Abe M., Yamazaki M., Nakao K., Nishioka T., Sakimura K., Yamada K.,
RA Kaibuchi K., Hoshino M.;
RT "Cytoskeletal regulation by AUTS2 in neuronal migration and
RT neuritogenesis.";
RL Cell Rep. 9:2166-2179(2014).
CC -!- FUNCTION: Functions as a RAC guanine nucleotide exchange factor (GEF),
CC which activates the Rac proteins by exchanging bound GDP for free GTP.
CC Its activity is synergistically activated by phosphatidylinositol
CC 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G
CC protein. May function downstream of heterotrimeric G proteins in
CC neutrophils (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16243036}.
CC -!- SUBUNIT: Interacts preferentially with RAC2 (PubMed:16243036).
CC Interacts with RAC1 (PubMed:16243036). Interacts with AUTS2
CC (PubMed:25533347). {ECO:0000269|PubMed:16243036,
CC ECO:0000269|PubMed:25533347}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Mainly
CC cytosolic. Some amount is apparently associated to the plasma membrane
CC (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q69ZK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZK0-2; Sequence=VSP_026436;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173168; BAD32446.1; ALT_INIT; mRNA.
DR EMBL; AL591884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK090301; BAC41161.1; -; mRNA.
DR EMBL; BC057617; AAH57617.1; -; mRNA.
DR CCDS; CCDS38334.1; -. [Q69ZK0-1]
DR RefSeq; NP_808450.2; NM_177782.3. [Q69ZK0-1]
DR AlphaFoldDB; Q69ZK0; -.
DR SMR; Q69ZK0; -.
DR BioGRID; 234934; 6.
DR IntAct; Q69ZK0; 3.
DR STRING; 10090.ENSMUSP00000037180; -.
DR iPTMnet; Q69ZK0; -.
DR PhosphoSitePlus; Q69ZK0; -.
DR EPD; Q69ZK0; -.
DR jPOST; Q69ZK0; -.
DR MaxQB; Q69ZK0; -.
DR PaxDb; Q69ZK0; -.
DR PeptideAtlas; Q69ZK0; -.
DR PRIDE; Q69ZK0; -.
DR ProteomicsDB; 291650; -. [Q69ZK0-1]
DR ProteomicsDB; 291651; -. [Q69ZK0-2]
DR Antibodypedia; 1100; 247 antibodies from 35 providers.
DR Ensembl; ENSMUST00000036719; ENSMUSP00000037180; ENSMUSG00000039621. [Q69ZK0-1]
DR Ensembl; ENSMUST00000109246; ENSMUSP00000104869; ENSMUSG00000039621. [Q69ZK0-2]
DR GeneID; 277360; -.
DR KEGG; mmu:277360; -.
DR UCSC; uc008nym.1; mouse. [Q69ZK0-2]
DR UCSC; uc008nyn.1; mouse. [Q69ZK0-1]
DR CTD; 57580; -.
DR MGI; MGI:3040696; Prex1.
DR VEuPathDB; HostDB:ENSMUSG00000039621; -.
DR eggNOG; KOG3519; Eukaryota.
DR GeneTree; ENSGT00940000159925; -.
DR HOGENOM; CLU_003935_0_0_1; -.
DR InParanoid; Q69ZK0; -.
DR OMA; TMPHYEF; -.
DR OrthoDB; 24217at2759; -.
DR PhylomeDB; Q69ZK0; -.
DR TreeFam; TF328639; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 277360; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Prex1; mouse.
DR PRO; PR:Q69ZK0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q69ZK0; protein.
DR Bgee; ENSMUSG00000039621; Expressed in granulocyte and 229 other tissues.
DR ExpressionAtlas; Q69ZK0; baseline and differential.
DR Genevisible; Q69ZK0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0030593; P:neutrophil chemotaxis; IGI:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IGI:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IGI:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IGI:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IGI:MGI.
DR GO; GO:0030217; P:T cell differentiation; IGI:MGI.
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; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 2.
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; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1650
FT /note="Phosphatidylinositol 3,4,5-trisphosphate-dependent
FT Rac exchanger 1 protein"
FT /id="PRO_0000292674"
FT DOMAIN 44..235
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 266..387
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 416..491
FT /note="DEP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 518..592
FT /note="DEP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 620..698
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCU6"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..1188
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026436"
FT CONFLICT 1575
FT /note="G -> V (in Ref. 4; AAH57617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1650 AA; 184935 MW; EB1C0140126209FC CRC64;
MEAPGSGGGD GGGDPGGDGA HPDARGPVSG PCAAARDSER QLRLRLCVLN EILGTERDYV
GTLRFLQSAF LQRIRQNVAD SVEKGLTEEN VKVLFSNIED ILEVHKDFLA ALEYCLHPEP
QSQHELGNVF LKFKDKFCVY EEYCSNHEKA LRLLVELNKV PAVRAFLLSC MLLGGRKTTD
IPLEGYLLSP IQRICKYPLL LKELAKRTPG KHPDHTAVQS ALQAMKTVCS NINETKRQME
KLEALEQLQS HIEGWEGSNL TDICTELLLQ GNLLKISAGN IQERAFFLFD NLLVYCKRKS
RVTGSKKSTK RTKSINGSLY IFRGRINTEV MEVENVEDGT ADYHSNGYTV TNGWKIHNTA
KNKWFVCMAK TAEEKQKWLD ALIREREQRE SLKLGMERDA YVMIAEKGEK LYHMMMSKKV
NLIKDRRRKL STVPKCFLGN EFVAWLLEIG EISKTEEGVN LGQALLENGI IHHVSDKHQF
KNEQVMYRFR YDDGTYKARS ELEDIMSKGV RLYCRLHSLY APVIKDRDYH LKTYKSVVPG
SKLVDWLLAQ GDCQTREEAV ALGVGLCNNG FMHHVLEKSE FKDESQYFRF HADEEMEGTS
SKNKQLRNDF KLVENILAKR LLIPPQEDDY GFDLEEKNKA VVVKSVQRGS LAEMAGLQAG
RKIYSINEDL VFLRPFSEVE TILNQFFCSR RPLRLLVATK AKETIKVPDH PEALSFQIRG
TAPPCVFAVG RGSEAVAAGL CAGQCILKVN GTSVANDGAL EVLEHFQAFR NHREEALGLY
QWVYHSHEDA QLARASQGAP DEDPQEDDQP DSALPLLSLG PQLSLHEDSA VVSLTLDNVH
LEHGVVYEYM STAGAKCHVL EKIVEPRGCF RLAAKILEAF AVDDSIFVQN CGRLMAMSSA
IVTMSHYEFH NICDTKLESI GQRIACYQEF AAQLKSRVSP PFKQASLEPH PLCGLDFCPT
NCHVNLMEVS YPKTTPSVGR SFSIRFGRKP SLIGLDPEQG LNPMAYTQHC ITTMAAPSWK
CSPAVDEDSQ GQGLNDSSYG SASGAPSQQD RGLSFLLKQE DREIQDAYLQ LFTKLDVALK
EMKQYVTQIN RLLSTITEPT SAAPAPCDPS LVEETSSSPP VSEESEVDRT DHSGIKKVCF
KVSEDEQEDS GHDTMSYRDS YSECNSNRDS VLSYTSVRSN SSYLGSDEMG SGDELPCDMR
IPSDKQDKLH GCLEHLFNQV DSIHALLKGP VMSRAFEETR HFPMKHSWQE FKQKEECTVR
GRNLIQISIQ EDPWNLPSSI RTLVDNIQQY VEDGKNQLLL ALLKCTDTEL QLRRDAVFCQ
ALVAAVCTFS EQLLAALDYR YNNNGEYEES SRDASRKWLE QVAATGVLLH WQSLLAPASV
KEERTMLEDI WVTLSELDNV TFSFKQLDEN SVANTNVFYH IEGSRQALKV VFYLDGFHFS
RLPSRLEGGA SLRLHTVLFT KALESVEGPP PPGNQAAEEL QQEINAQSLE KVQQYYRKLR
AFYLERSNLP TDAGATAVKI DQLIRPINAL DELYRLMKTF VHPKAGAAGS LGAGLIPVSS
ELCYRLGACQ ITMCGTGMQR STLSVSLEQA AILARSHGLL PKCVMQATDI MRKQGPRVEI
LAKNLRIKDP MPQGAPRLYQ LCQPPVDGDL
