CDC42_MOUSE
ID CDC42_MOUSE Reviewed; 191 AA.
AC P60766; A2A9U6; P21181; P25763; Q3THZ7; Q3TJK6; Q545V0; Q6P201; Q8BQ51;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Cell division control protein 42 homolog {ECO:0000305};
DE EC=3.6.5.2 {ECO:0000269|PubMed:24352656, ECO:0000269|PubMed:26969129};
DE AltName: Full=G25K GTP-binding protein;
DE Flags: Precursor;
GN Name=Cdc42 {ECO:0000312|MGI:MGI:106211};
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 2).
RX PubMed=8464478; DOI=10.1038/362462a0;
RA Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.;
RT "Oncogene ect2 is related to regulators of small GTP-binding proteins.";
RL Nature 362:462-465(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=9224952; DOI=10.1016/s0167-4781(97)00027-4;
RA Gong T.W., Shin J.J., Burmeister M., Lomax M.I.;
RT "Complete cDNAs for CDC42 from chicken cochlea and mouse liver.";
RL Biochim. Biophys. Acta 1352:282-292(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=8954774; DOI=10.1006/geno.1996.0586;
RA Marks P.W., Kwiatkowski D.J.;
RT "Genomic organization and chromosomal location of murine Cdc42.";
RL Genomics 38:13-18(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Amnion, Bone marrow, Heart, Kidney, Liver, Mammary gland, Placenta,
RC Spinal ganglion, 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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
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 [7]
RP PROTEIN SEQUENCE OF 108-120, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP INTERACTION WITH CDC42EP4.
RX PubMed=10490598; DOI=10.1128/mcb.19.10.6585;
RA Joberty G., Perlungher R.R., Macara I.G.;
RT "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins.";
RL Mol. Cell. Biol. 19:6585-6597(1999).
RN [9]
RP SUBUNIT OF A COMPLEX CONTAINING PARD6B; PARD3 AND PRKCZ, AND MUTAGENESIS OF
RP THR-17.
RX PubMed=10934474; DOI=10.1038/35019573;
RA Joberty G., Petersen C., Gao L., Macara I.G.;
RT "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to
RT Cdc42.";
RL Nat. Cell Biol. 2:531-539(2000).
RN [10]
RP INTERACTION WITH NET1.
RX PubMed=9535835; DOI=10.1074/jbc.273.15.8616;
RA Alberts A.S., Bouquin N., Johnston L.H., Treisman R.;
RT "Analysis of RhoA-binding proteins reveals an interaction domain conserved
RT in heterotrimeric G protein beta subunits and the yeast response regulator
RT protein Skn7.";
RL J. Biol. Chem. 273:8616-8622(1998).
RN [11]
RP INTERACTION WITH ARHGAP33/TCGAP.
RX PubMed=12773384; DOI=10.1093/emboj/cdg262;
RA Chiang S.-H., Hwang J., Legendre M., Zhang M., Kimura A., Saltiel A.R.;
RT "TCGAP, a multidomain Rho GTPase-activating protein involved in insulin-
RT stimulated glucose transport.";
RL EMBO J. 22:2679-2691(2003).
RN [12]
RP ACTIVITY REGULATION, AND INTERACTION WITH DOCK11.
RX PubMed=15710388; DOI=10.1016/j.febslet.2005.01.006;
RA Nishikimi A., Meller N., Uekawa N., Isobe K., Schwartz M.A., Maruyama M.;
RT "Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange
RT factor expressed predominantly in lymphocytes.";
RL FEBS Lett. 579:1039-1046(2005).
RN [13]
RP INTERACTION WITH DOCK11 AND IQGAP1, AND MUTAGENESIS OF THR-17 AND GLN-61.
RX PubMed=16968698; DOI=10.1074/jbc.m606248200;
RA Lin Q., Yang W., Baird D., Feng Q., Cerione R.A.;
RT "Identification of a DOCK180-related guanine nucleotide exchange factor
RT that is capable of mediating a positive feedback activation of Cdc42.";
RL J. Biol. Chem. 281:35253-35262(2006).
RN [14]
RP INTERACTION WITH CCPG1.
RX PubMed=17000758; DOI=10.1128/mcb.00670-06;
RA Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT "Ccpg1, a novel scaffold protein that regulates the activity of the Rho
RT guanine nucleotide exchange factor Dbs.";
RL Mol. Cell. Biol. 26:8964-8975(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [16]
RP ACTIVITY REGULATION, INTERACTION WITH DOCK8, AND SUBCELLULAR LOCATION.
RX PubMed=22461490; DOI=10.1182/blood-2012-01-407098;
RA Harada Y., Tanaka Y., Terasawa M., Pieczyk M., Habiro K., Katakai T.,
RA Hanawa-Suetsugu K., Kukimoto-Niino M., Nishizaki T., Shirouzu M., Duan X.,
RA Uruno T., Nishikimi A., Sanematsu F., Yokoyama S., Stein J.V., Kinashi T.,
RA Fukui Y.;
RT "DOCK8 is a Cdc42 activator critical for interstitial dendritic cell
RT migration during immune responses.";
RL Blood 119:4451-4461(2012).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF GLY-12 AND THR-17.
RX PubMed=22494997; DOI=10.1186/1742-4933-9-2;
RA Sakabe I., Asai A., Iijima J., Maruyama M.;
RT "Age-related guanine nucleotide exchange factor, mouse Zizimin2, induces
RT filopodia in bone marrow-derived dendritic cells.";
RL Immun. Ageing 9:2-2(2012).
RN [18]
RP CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24352656; DOI=10.1074/jbc.m113.534636;
RA Raynaud F., Moutin E., Schmidt S., Dahl J., Bertaso F., Boeckers T.M.,
RA Homburger V., Fagni L.;
RT "Rho-GTPase-activating protein interacting with Cdc-42-interacting protein
RT 4 homolog 2 (Rich2): a new Ras-related C3 botulinum toxin substrate 1
RT (Rac1) GTPase-activating protein that controls dendritic spine
RT morphogenesis.";
RL J. Biol. Chem. 289:2600-2609(2014).
RN [19]
RP FUNCTION.
RX PubMed=25851601; DOI=10.1091/mbc.e14-08-1310;
RA Jaudon F., Raynaud F., Wehrle R., Bellanger J.M., Doulazmi M., Vodjdani G.,
RA Gasman S., Fagni L., Dusart I., Debant A., Schmidt S.;
RT "The RhoGEF DOCK10 is essential for dendritic spine morphogenesis.";
RL Mol. Biol. Cell 26:2112-2127(2015).
RN [20]
RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=26969129; DOI=10.1186/s13041-016-0206-6;
RA Sarowar T., Grabrucker S., Foehr K., Mangus K., Eckert M., Bockmann J.,
RA Boeckers T.M., Grabrucker A.M.;
RT "Enlarged dendritic spines and pronounced neophobia in mice lacking the PSD
RT protein RICH2.";
RL Mol. Brain 9:28-28(2016).
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC an active GTP-bound and an inactive GDP-bound state (PubMed:24352656).
CC In its active state binds to a variety of effector proteins to regulate
CC cellular responses. Involved in epithelial cell polarization processes.
CC Regulates the bipolar attachment of spindle microtubules to
CC kinetochores before chromosome congression in metaphase. Regulates cell
CC migration (By similarity). In neurons, plays a role in the extension
CC and maintenance of the formation of filopodia, thin and actin-rich
CC surface projections. Required for DOCK10-mediated spine formation in
CC Purkinje cells and hippocampal neurons (PubMed:25851601). Facilitates
CC filopodia formation upon DOCK11-activation (PubMed:22494997). Upon
CC activation by CaMKII, modulates dendritic spine structural plasticity
CC by relaying CaMKII transient activation to synapse-specific, long-term
CC signaling (By similarity). Also plays a role in phagocytosis through
CC organization of the F-actin cytoskeleton associated with forming
CC phagocytic cups (By similarity). {ECO:0000250|UniProtKB:P60953,
CC ECO:0000250|UniProtKB:Q8CFN2, ECO:0000269|PubMed:22494997,
CC ECO:0000269|PubMed:24352656, ECO:0000269|PubMed:25851601}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:24352656, ECO:0000269|PubMed:26969129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:24352656, ECO:0000305|PubMed:26969129};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. Inhibited by GAPs such as ARHGAP44
CC (PubMed:24352656, PubMed:26969129). {ECO:0000269|PubMed:15710388,
CC ECO:0000269|PubMed:22461490, ECO:0000269|PubMed:24352656,
CC ECO:0000269|PubMed:26969129}.
CC -!- SUBUNIT: Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4,
CC CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-
CC dependent manner) (PubMed:10490598, PubMed:10934474). Interacts with
CC activated CSPG4 and with BAIAP2 (By similarity). Interacts with
CC DOCK11/Zizimin2; the interaction activates CDC42 by exchanging GDP for
CC GTP (PubMed:15710388, PubMed:16968698). Interacts with DOCK9; the
CC interaction activates CDC42 by exchanging GDP for GTP (By similarity).
CC Interacts with DOCK8 (via DHR-2 domain); the interaction activates
CC CDC42 by exchanging GDP for GTP (PubMed:22461490). Interacts with
CC IQGAP1 (PubMed:16968698). Interacts with NET1 and ARHGAP33/TCGAP
CC (PubMed:9535835, PubMed:12773384). Part of a complex with PARD3, PARD6A
CC or PARD6B and PRKCI or PRKCZ (PubMed:10934474). The GTP-bound form
CC interacts with CCPG1 (PubMed:17000758). Interacts with USP6 (By
CC similarity). Interacts with NEK6 (By similarity). Part of a collagen
CC stimulated complex involved in cell migration composed of CDC42, CRK,
CC TNK2 and BCAR1/p130cas (By similarity). Interacts with ITGB1BP1 (By
CC similarity). Interacts with ARHGDIA; this interaction inactivates and
CC stabilizes CDC42. Interacts with ARHGDIB; this maintains CDC42 in the
CC inactive, GDP-bound form (By similarity). Interacts in (GTP-bound form)
CC with FNBP1L and ABI1, but only in the presence of FNBP1L (By
CC similarity). {ECO:0000250|UniProtKB:P60953,
CC ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:10934474,
CC ECO:0000269|PubMed:12773384, ECO:0000269|PubMed:15710388,
CC ECO:0000269|PubMed:16968698, ECO:0000269|PubMed:17000758,
CC ECO:0000269|PubMed:22461490, ECO:0000269|PubMed:9535835}.
CC -!- INTERACTION:
CC P60766; O88643: Pak1; NbExp=2; IntAct=EBI-81763, EBI-457240;
CC P60766; P63044: Vamp2; NbExp=2; IntAct=EBI-81763, EBI-521920;
CC P60766; Q13153: PAK1; Xeno; NbExp=3; IntAct=EBI-81763, EBI-1307;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22461490};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Midbody
CC {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P60953}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P60953}.
CC Cytoplasm {ECO:0000269|PubMed:22461490}. Cell projection, lamellipodium
CC membrane {ECO:0000269|PubMed:22461490}; Peripheral membrane protein
CC {ECO:0000305|PubMed:22461490}; Cytoplasmic side
CC {ECO:0000305|PubMed:22461490}. Cell projection, dendrite
CC {ECO:0000269|PubMed:24352656}. Note=Localizes to spindle during
CC prometaphase cells (By similarity). Moves to the central spindle as
CC cells progressed through anaphase to telophase. Localizes at the end of
CC cytokinesis in the intercellular bridge formed between two daughter
CC cells (By similarity). Its localization is regulated by the activities
CC of guanine nucleotide exchange factor ECT2 and GTPase activating
CC protein RACGAP1. Colocalizes with NEK6 in the centrosome (By
CC similarity). In its active GTP-bound form localizes to the leading edge
CC membrane of migrating dendritic cells (PubMed:22461490).
CC {ECO:0000250|UniProtKB:P60953, ECO:0000269|PubMed:22461490}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=Placental;
CC IsoId=P60766-2, P21181-4;
CC Sequence=Displayed;
CC Name=1; Synonyms=Brain;
CC IsoId=P60766-1, P21181-1;
CC Sequence=VSP_040585, VSP_040586;
CC -!- PTM: Phosphorylated by SRC in an EGF-dependent manner, this stimulates
CC the binding of the Rho-GDP dissociation inhibitor RhoGDI.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42
CC subfamily. {ECO:0000305}.
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DR EMBL; L11318; AAA37410.1; -; mRNA.
DR EMBL; U37720; AAC00028.1; -; mRNA.
DR EMBL; L78075; AAB40051.1; -; Genomic_DNA.
DR EMBL; AK003098; BAB22563.1; -; mRNA.
DR EMBL; AK051543; BAC34669.1; -; mRNA.
DR EMBL; AK075567; BAC35825.1; -; mRNA.
DR EMBL; AK144216; BAE25778.1; -; mRNA.
DR EMBL; AK151087; BAE30100.1; -; mRNA.
DR EMBL; AK151726; BAE30644.1; -; mRNA.
DR EMBL; AK153564; BAE32098.1; -; mRNA.
DR EMBL; AK154870; BAE32891.1; -; mRNA.
DR EMBL; AK159470; BAE35111.1; -; mRNA.
DR EMBL; AK166281; BAE38678.1; -; mRNA.
DR EMBL; AK167195; BAE39325.1; -; mRNA.
DR EMBL; AK167400; BAE39489.1; -; mRNA.
DR EMBL; AK167609; BAE39663.1; -; mRNA.
DR EMBL; AK168013; BAE40000.1; -; mRNA.
DR EMBL; AK168076; BAE40049.1; -; mRNA.
DR EMBL; AK168089; BAE40062.1; -; mRNA.
DR EMBL; AK168276; BAE40222.1; -; mRNA.
DR EMBL; AK168758; BAE40595.1; -; mRNA.
DR EMBL; AK168820; BAE40647.1; -; mRNA.
DR EMBL; AK169122; BAE40902.1; -; mRNA.
DR EMBL; AK169232; BAE41001.1; -; mRNA.
DR EMBL; AK169805; BAE41379.1; -; mRNA.
DR EMBL; AL645468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064792; AAH64792.1; -; mRNA.
DR CCDS; CCDS18816.1; -.
DR CCDS; CCDS57305.1; -. [P60766-1]
DR RefSeq; NP_001230698.1; NM_001243769.1. [P60766-1]
DR RefSeq; NP_033991.1; NM_009861.3. [P60766-2]
DR PDB; 3EG5; X-ray; 2.70 A; A/C=1-178.
DR PDB; 5C2J; X-ray; 2.50 A; B=1-191.
DR PDBsum; 3EG5; -.
DR PDBsum; 5C2J; -.
DR AlphaFoldDB; P60766; -.
DR BMRB; P60766; -.
DR SMR; P60766; -.
DR BioGRID; 198627; 64.
DR CORUM; P60766; -.
DR DIP; DIP-32554N; -.
DR IntAct; P60766; 15.
DR MINT; P60766; -.
DR STRING; 10090.ENSMUSP00000054634; -.
DR ChEMBL; CHEMBL4523257; -.
DR iPTMnet; P60766; -.
DR PhosphoSitePlus; P60766; -.
DR SwissPalm; P60766; -.
DR EPD; P60766; -.
DR jPOST; P60766; -.
DR MaxQB; P60766; -.
DR PaxDb; P60766; -.
DR PeptideAtlas; P60766; -.
DR PRIDE; P60766; -.
DR ProteomicsDB; 280033; -.
DR ProteomicsDB; 280034; -. [P60766-1]
DR Antibodypedia; 3818; 531 antibodies from 42 providers.
DR DNASU; 12540; -.
DR Ensembl; ENSMUST00000030417; ENSMUSP00000030417; ENSMUSG00000006699. [P60766-1]
DR Ensembl; ENSMUST00000051477; ENSMUSP00000054634; ENSMUSG00000006699. [P60766-2]
DR GeneID; 12540; -.
DR KEGG; mmu:12540; -.
DR UCSC; uc008viw.3; mouse.
DR UCSC; uc008viy.2; mouse. [P60766-1]
DR CTD; 998; -.
DR MGI; MGI:106211; Cdc42.
DR VEuPathDB; HostDB:ENSMUSG00000006699; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000153675; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P60766; -.
DR OMA; ITHHQQK; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; P60766; -.
DR TreeFam; TF101109; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-418885; DCC mediated attractive signaling.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-525793; Myogenesis.
DR Reactome; R-MMU-5625970; RHO GTPases activate KTN1.
DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-8964616; G beta:gamma signalling through CDC42.
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-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 12540; 27 hits in 73 CRISPR screens.
DR ChiTaRS; Cdc42; mouse.
DR EvolutionaryTrace; P60766; -.
DR PRO; PR:P60766; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P60766; protein.
DR Bgee; ENSMUSG00000006699; Expressed in peripheral lymph node and 269 other tissues.
DR Genevisible; P60766; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0017119; C:Golgi transport complex; ISO:MGI.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031256; C:leading edge membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0000322; C:storage vacuole; IDA:MGI.
DR GO; GO:0034191; F:apolipoprotein A-I receptor binding; ISO:MGI.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0032427; F:GBD domain binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0031996; F:thioesterase binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0090135; P:actin filament branching; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0034332; P:adherens junction organization; IMP:MGI.
DR GO; GO:0003161; P:cardiac conduction system development; IGI:MGI.
DR GO; GO:0003253; P:cardiac neural crest cell migration involved in outflow tract morphogenesis; IMP:MGI.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; ISO:MGI.
DR GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; TAS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0036336; P:dendritic cell migration; IGI:MGI.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0006897; P:endocytosis; IMP:MGI.
DR GO; GO:0016197; P:endosomal transport; TAS:UniProtKB.
DR GO; GO:0086101; P:endothelin receptor signaling pathway involved in heart process; IMP:MGI.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0051683; P:establishment of Golgi localization; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0046847; P:filopodium assembly; IDA:MGI.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0060047; P:heart contraction; IGI:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0099563; P:modification of synaptic structure; ISO:MGI.
DR GO; GO:0044788; P:modulation by host of viral process; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0048664; P:neuron fate determination; IMP:MGI.
DR GO; GO:0038189; P:neuropilin signaling pathway; ISO:MGI.
DR GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR GO; GO:0051647; P:nucleus localization; IMP:MGI.
DR GO; GO:0072384; P:organelle transport along microtubule; ISO:MGI.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IMP:CACAO.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:MGI.
DR GO; GO:0048549; P:positive regulation of pinocytosis; IMP:UniProtKB.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0051835; P:positive regulation of synapse structural plasticity; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:MGI.
DR GO; GO:0099159; P:regulation of modification of postsynaptic structure; ISO:MGI.
DR GO; GO:0043393; P:regulation of protein binding; IDA:MGI.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:MGI.
DR GO; GO:0002040; P:sprouting angiogenesis; ISO:MGI.
DR GO; GO:0060661; P:submandibular salivary gland formation; IEA:Ensembl.
DR CDD; cd01874; Cdc42; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR037874; Cdc42.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Differentiation; Direct protein sequencing;
KW GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..188
FT /note="Cell division control protein 42 homolog"
FT /id="PRO_0000030427"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030428"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P60953"
FT MOD_RES 188
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 188
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 163
FT /note="K -> R (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_040585"
FT VAR_SEQ 182..191
FT /note="PKKSRRCVLL -> TQPKRKCCIF (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_040586"
FT MUTAGEN 12
FT /note="G->V: No effect on filopodia formation."
FT /evidence="ECO:0000269|PubMed:22494997"
FT MUTAGEN 17
FT /note="T->N: Constitutively inactivated. Abolishes
FT interaction with PARD6 and DOCK11. Inhibits filopodia
FT formation."
FT /evidence="ECO:0000269|PubMed:10934474,
FT ECO:0000269|PubMed:16968698, ECO:0000269|PubMed:22494997"
FT MUTAGEN 61
FT /note="Q->L: Constitutively activated. Enhances interaction
FT with DOCK11."
FT /evidence="ECO:0000269|PubMed:16968698"
FT CONFLICT 26
FT /note="N -> D (in Ref. 4; BAC34669)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="R -> G (in Ref. 6; AAH64792)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="V -> I (in Ref. 4; BAE39489)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="Q -> K (in Ref. 4; BAE40049)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="E -> G (in Ref. 6; AAH64792)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:5C2J"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:5C2J"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:5C2J"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:5C2J"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5C2J"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:5C2J"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:5C2J"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:5C2J"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:5C2J"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:5C2J"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:5C2J"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:5C2J"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:5C2J"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:5C2J"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5C2J"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:5C2J"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:5C2J"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:5C2J"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:5C2J"
SQ SEQUENCE 191 AA; 21259 MW; 51A437E22A4D8FFF CRC64;
MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG
QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCPKTPF LLVGTQIDLR
DDPSTIEKLA KNKQKPITPE TAEKLARDLK AVKYVECSAL TQKGLKNVFD EAILAALEPP
EPKKSRRCVL L
