ID   Q6PDM6_MOUSE            Unreviewed;      1166 AA.
AC   Q6PDM6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 161.
DE   RecName: Full=Guanine nucleotide exchange factor DBS {ECO:0000256|ARBA:ARBA00068285};
DE   AltName: Full=DBL's big sister {ECO:0000256|ARBA:ARBA00079556};
DE   AltName: Full=MCF2-transforming sequence-like protein {ECO:0000256|ARBA:ARBA00082859};
GN   Name=Mcf2l {ECO:0000313|EMBL:AAH58622.1, ECO:0000313|MGI:MGI:103263};
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 {ECO:0000313|EMBL:AAH58622.1};
RN   [1] {ECO:0000313|EMBL:AAH58622.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH58622.1};
RC   TISSUE=Brain {ECO:0000313|EMBL:AAH58622.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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).
CC   -!- FUNCTION: Guanine nucleotide exchange factor that catalyzes guanine
CC       nucleotide exchange on RHOA and CDC42, and thereby contributes to the
CC       regulation of RHOA and CDC42 signaling pathways. Seems to lack activity
CC       with RAC1. Becomes activated and highly tumorigenic by truncation of
CC       the N-terminus. {ECO:0000256|ARBA:ARBA00057838}.
CC   -!- SUBUNIT: Interacts with GTP-bound RAC1. Interacts with CDC42. Interacts
CC       with RHOA. Interacts with CCPG1, which results in specific inhibition
CC       of its exchange activity toward RHOA, but does not affect its activity
CC       on CDC42. {ECO:0000256|ARBA:ARBA00062285}.
CC   -!- INTERACTION:
CC       Q6PDM6; P61586: RHOA; Xeno; NbExp=3; IntAct=EBI-602149, EBI-446668;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the MCF2 family.
CC       {ECO:0000256|ARBA:ARBA00049987}.
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DR   EMBL; BC058622; AAH58622.1; -; mRNA.
DR   RefSeq; NP_001152957.1; NM_001159485.2.
DR   RefSeq; NP_001152958.1; NM_001159486.2.
DR   RefSeq; NP_835177.2; NM_178076.4.
DR   AlphaFoldDB; Q6PDM6; -.
DR   IntAct; Q6PDM6; 1.
DR   DNASU; 17207; -.
DR   GeneID; 17207; -.
DR   KEGG; mmu:17207; -.
DR   AGR; MGI:103263; -.
DR   CTD; 23263; -.
DR   MGI; MGI:103263; Mcf2l.
DR   OrthoDB; 10004999at2759; -.
DR   PhylomeDB; Q6PDM6; -.
DR   BioGRID-ORCS; 17207; 4 hits in 77 CRISPR screens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd01227; PH_Dbs; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd00170; SEC14; 1.
DR   CDD; cd11857; SH3_DBS; 1.
DR   CDD; cd00176; SPEC; 1.
DR   FunFam; 1.20.900.10:FF:000001; Guanine nucleotide exchange factor DBS; 1.
DR   FunFam; 2.30.29.30:FF:000078; Guanine nucleotide exchange factor DBS; 1.
DR   FunFam; 2.30.30.40:FF:000198; Guanine nucleotide exchange factor DBS; 1.
DR   FunFam; 1.20.58.60:FF:000136; MCF.2 cell line derived transforming sequence like; 1.
DR   Gene3D; 1.20.58.60; -; 1.
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; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR035534; DBS_PH.
DR   InterPro; IPR035532; DBS_SH3.
DR   InterPro; IPR000219; DH_dom.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR051336; RhoGEF_Guanine_NuclExch_SF.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR055251; SOS1_NGEF_PH.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR056466; Spectrin_DBS.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR22826:SF115; GUANINE NUCLEOTIDE EXCHANGE FACTOR DBS; 1.
DR   PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF22697; SOS1_NGEF_PH; 1.
DR   Pfam; PF00435; Spectrin; 1.
DR   Pfam; PF23289; Spectrin_5; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          13..185
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   DOMAIN          593..773
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          791..907
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1072..1133
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          516..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          917..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..555
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..939
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1166 AA;  131131 MW;  D969135E4592F851 CRC64;
     MALEEMVQRL NAVSKNTDEI MHQDIVPLCA ADIQEQLKKR FAYLSGGRGQ DGSPVITFPD
     YPAFSEIPDK EFQNVMTYLT SIPSLQDAGI GFILVIDRRQ DKWTSVKASV LRIAASFPAN
     LQLVLVLRPT GFFQRTLSDI AFKFNRDEFK MKVPVMMLSS VPELHGYIDK SQLTEDLGGT
     LDYCHSRWLC HRTAIESFAL MVKQTAQMLQ AFGTELAETE LPNDVQSTSL VLSAHTEKKA
     KVKEDLQLAL KEGNSILESL REPLAESAAH SVNQDQLDNQ ATVQRLLAQL NETEAAFDEF
     WAKHQQKLEQ CLQLRHFEQG FREVKTTLDS MSQKIAAFTD VGNSLAHVQH LLKDLTAFEE
     KSSVAVDKAR ALSLEGQQLI ENRHYAVDSI HPKCEELQHL CDHFASEVTR RRGLLSKSLE
     LHSLLETSMK WSDEGIFLLA SQPVDKCQSQ DGAEAALQEI EKFLETGAEN KIQELNEIYK
     EYECILNQDL LEHVQKVFQK QESTEEMFHR RQASLKKLAA KQTRPVQPVA PRPEALTKSP
     SPSPGSWRSS ENSSSEGNAL RRGPYRRAKS EMSEPRQGRT SSTGEEEESL AILRRHVMNE
     LLDTERAYVE ELLCVLEGYA AEMDNPLMAH LISTGLQNKK NILFGNMEEI YHFHNRIFLR
     ELESCIDCPE LVGRCFLERM EEFQIYEKYC QNKPRSESLW RQCSDCPFFQ ECQKKLDHKL
     SLDSYLLKPV QRITKYQLLL KEMLKYSKHC EGAEDLQEAL SSILGILKAV NDSMHLIAIT
     GYDGNLGDLG KLLMQGSFSV WTDHKKGHTK VKELARFKPM QRHLFLHEKA VLFCKKREEN
     GEGYEKAPSY SYKQSLNMTA VGITENVKGD TKKFEIWYNA REEVYIIQAP TPEIKAAWVN
     EIRKVLTSQL QACREASQHR ALEQSHSLPL PTPSSTSPTK GNTRNVKKLE DRKTDPLSLE
     GYVSSSLPKP PEKGKDDAVP SSTSESSALS RKRFTLQGLA NLKGQKASPT SPDKKAKRHE
     VKSDPTPFGL RGWSKTSHSL EAPEEDGGWS SAEELINSSD AEEDGGVGPK KLVPGKYTVV
     MDDEKGGPDT LAMRSGDMVE VVEEGAEGLW YVRDLTSSKE GWVPASSLST LLGKSSSAQC
     LSSSGKIHCA RQLCPEPAEI LSPEPV
//