ID D3ZS72_RAT Unreviewed; 1635 AA.
AC D3ZS72;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1 {ECO:0000313|Ensembl:ENSRNOP00000009517.8};
GN Name=Prex1 {ECO:0000313|Ensembl:ENSRNOP00000009517.8,
GN ECO:0000313|RGD:1306534};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000009517.8, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000009517.8, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000009517.8,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000009517.8}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000009517.8};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; D3ZS72; -.
DR IntAct; D3ZS72; 1.
DR STRING; 10116.ENSRNOP00000009517; -.
DR PhosphoSitePlus; D3ZS72; -.
DR PaxDb; 10116-ENSRNOP00000009517; -.
DR PeptideAtlas; D3ZS72; -.
DR Ensembl; ENSRNOT00000009517.8; ENSRNOP00000009517.8; ENSRNOG00000006952.8.
DR UCSC; RGD:1306534; rat.
DR AGR; RGD:1306534; -.
DR RGD; 1306534; Prex1.
DR VEuPathDB; HostDB:ENSRNOG00000006952; -.
DR eggNOG; KOG3519; Eukaryota.
DR GeneTree; ENSGT00940000159925; -.
DR HOGENOM; CLU_003935_0_0_1; -.
DR InParanoid; D3ZS72; -.
DR Reactome; R-RNO-193648; NRAGE signals death through JNK.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000006952; Expressed in spleen and 19 other cell types or tissues.
DR Genevisible; D3ZS72; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:RGD.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:RGD.
DR GO; GO:0023051; P:regulation of signaling; IBA:GO_Central.
DR GO; GO:0030217; P:T cell differentiation; ISO:RGD.
DR CDD; cd00136; PDZ; 2.
DR CDD; cd01224; PH_Collybistin_ASEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR22829; DEP DOMAIN PROTEIN; 1.
DR PANTHER; PTHR22829:SF6; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE-DEPENDENT RAC EXCHANGER 1 PROTEIN; 1.
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; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT DOMAIN 44..235
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 266..387
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 416..491
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 528..594
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 622..669
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1635 AA; 182968 MW; B089369064ABA023 CRC64;
MEAPGSGSGD GGGDPGGDGA HPDARGPSSG PCAAARDSER QLRLRLCVLN EILATERDYV
GTLRFLQSAF LQRIRQNVAD SVDKGLTEEN VKILFSNIED ILEVHKDFLA ALEYCLHPEP
QSQHELGNVF LKFKDKFCVY EEYCSNHEKA LRLLVELNKV PAARAFLLNC MLLGGRKTTD
IPLEGYLLSP IQRICKYPLL LKELSKRTPG KHPDHSAVQS ALQAMKTVCS NINETKRQME
KLEALEQLQS HIEGWEGSNL TDICTQLLLQ GTLLKISAGN IQERAFFLFD NLLVYCKRKS
RVTGSKKSTK RTKSINGSLY IFRGRINTEV MEVENVEDGT ADYHSNGYTV TNGWKIHNTA
KNKWFVCMAK TAEEKQKWLD ALIREREQRE SLKLGMERDA YVMIAEKGEK LYHMMMSKKV
NLIKDRRRKL STVPKCFLGN EFVAWLLEIG EISKTEEGVN LGQALLENGI IHHVSDKHQF
KNEQVMYRFR YDDGTYKARS ELEDIMSKVG RLLAACGAHP AGGPCSLDRD YHLKTYKSVV
PGSKLVDWLL AQGDCQTREE AVALGVGLCN NGFMHHVLEK SEFKDESQYF RFHADEEMEG
TSSKNKQLRN DFKLVENILA KRLLIPPQED DYGFDLEEKN KAVVVKSVQR GSLAEMAGLQ
AGRKIYSINE DLVFLRPFSE VETILNQSFC SRRPLRLLVA TKAKETIKIP DHPEALSFQI
RGTAPPCVFA VGRGSEAVAA GLCAGQCILK VNGNSVANDG ALEVLEHFQA FRSRREEALG
LYQWVYHSHE DAQQARASQG APDEDPQEDD SVLPLLSLGP QLSLHEDSAV VSLTLDNVHL
EHGVVYEYVS TAGAKCHVLE KIVEPRGCFR LAAKILEAFA EDDSLFVQNC GRLMAMGSAI
ITMSHYEFHN ICDTKLESIG QRIACYQEFA AQLKSRVSPP FKQAPLEDHP LCGLDFCPTN
CHINFMEVSY PKTTPSVGRS FSIRFGRKPS LIGLDPEQGH LNPMAYTQHC ITTMAAPSWK
CAPAVDGDSQ SQGLIDSIFV SASGALSQQE RGLSFLLKQE DREIQDAYLQ LFTKLDVALK
EMKQYVTQIN RLLSTITEPT SAAPCDPPLV EETSSSPPAS EESEVDRTDH GGIKKVCFKV
SEDEQEDSGH DTMSYRDSYS ECNSNRDSVL SYTSVRSNSS YLGSDETGSG DELPCDIRIP
SDKQDKLHGC LEHLFNQVDS IHALLKGPVM SRAFEETRHF PMEHSWQEFK QKEECTVRGR
NLIQISIQED PWNLPSSIRT LVDNIQRYVE DGKNQLLLAL LKCTDTELQL RRDAVFCQAL
VAAVCTFSEQ LLAALDYRYN NNGEYEESSR DASRKWLEQV AATGVLLHWQ SLLAPATVKE
ERTMLEDIWV TLSELDNVTF SFKQLDENSV ANTNVFYHIE GSRQALKVVF YLDGFHFSRL
PSRLEGGASL RLHTVLFTKA LENVEGPSPP GSQAAEDLQQ EINAQSLEKV QQYYRRLRAF
YLERSNLPTD ATTTAVKIDQ LIRPINALDE LYRLMKSFVH PKAGAGGSLG AGLVPVSSEL
CYRLGACQIT MCGTGMQRST LSVSLEQAAI LARSHGLLPK CVMQATDIMR KQGPRVEILA
KNLRIKDPMP QGAPR
//
