BORG2_MOUSE
ID BORG2_MOUSE Reviewed; 254 AA.
AC Q9CQC5; Q3UD77; Q8BVR7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cdc42 effector protein 3;
DE AltName: Full=Binder of Rho GTPases 2;
GN Name=Cdc42ep3; Synonyms=Borg2, Cep3;
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].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Head;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63 AND SER-108, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND SER-144, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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: Probably involved in the organization of the actin
CC cytoskeleton. May act downstream of CDC42 to induce actin filament
CC assembly leading to cell shape changes. Induces pseudopodia formation
CC in fibroblasts (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RHOQ and CDC42, in a GTP-dependent manner, and
CC with SEPT7. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36479.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK012309; BAB28155.1; -; mRNA.
DR EMBL; AK014281; BAB29241.1; -; mRNA.
DR EMBL; AK019447; BAB31723.1; -; mRNA.
DR EMBL; AK076782; BAC36479.1; ALT_FRAME; mRNA.
DR EMBL; AK150214; BAE29384.1; -; mRNA.
DR EMBL; BC021409; AAH21409.1; -; mRNA.
DR EMBL; BC034714; AAH34714.1; -; mRNA.
DR EMBL; BC092297; AAH92297.1; -; mRNA.
DR CCDS; CCDS28984.1; -.
DR RefSeq; NP_080790.1; NM_026514.2.
DR RefSeq; XP_006524358.1; XM_006524295.3.
DR AlphaFoldDB; Q9CQC5; -.
DR STRING; 10090.ENSMUSP00000067217; -.
DR iPTMnet; Q9CQC5; -.
DR PhosphoSitePlus; Q9CQC5; -.
DR MaxQB; Q9CQC5; -.
DR PaxDb; Q9CQC5; -.
DR PRIDE; Q9CQC5; -.
DR ProteomicsDB; 265450; -.
DR Antibodypedia; 29451; 213 antibodies from 27 providers.
DR DNASU; 260409; -.
DR Ensembl; ENSMUST00000068958; ENSMUSP00000067217; ENSMUSG00000036533.
DR GeneID; 260409; -.
DR KEGG; mmu:260409; -.
DR UCSC; uc008dpx.1; mouse.
DR CTD; 10602; -.
DR MGI; MGI:2384718; Cdc42ep3.
DR VEuPathDB; HostDB:ENSMUSG00000036533; -.
DR eggNOG; ENOG502RKYM; Eukaryota.
DR GeneTree; ENSGT00940000157736; -.
DR HOGENOM; CLU_073229_0_0_1; -.
DR InParanoid; Q9CQC5; -.
DR OMA; LPTIGGC; -.
DR OrthoDB; 1244464at2759; -.
DR PhylomeDB; Q9CQC5; -.
DR TreeFam; TF331725; -.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR BioGRID-ORCS; 260409; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Cdc42ep3; mouse.
DR PRO; PR:Q9CQC5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CQC5; protein.
DR Bgee; ENSMUSG00000036533; Expressed in spermatocyte and 244 other tissues.
DR ExpressionAtlas; Q9CQC5; baseline and differential.
DR Genevisible; Q9CQC5; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR InterPro; IPR029273; Cdc42_effect.
DR InterPro; IPR000095; CRIB_dom.
DR Pfam; PF14957; BORG_CEP; 1.
DR Pfam; PF00786; PBD; 1.
DR SMART; SM00285; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Cdc42 effector protein 3"
FT /id="PRO_0000212652"
FT DOMAIN 31..45
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 165..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 254 AA; 27686 MW; 9EB9991CF1EB678F CRC64;
MPAKTPIYLK AANNKKGKKF KLRDILSPDM ISPPLGDFRH TIHIGKEGQH DVFGDISFLQ
GNYELLPGNQ EKAHSGQFPG HNDFFRANST SDSMFTETPS PVLKNAISLP TIGGSQALML
PLLSPVTFHS KQESFGRPKL PRLSCEPVME EKVQEQSSLL ENGAVHQGDT SWGSSGSGSQ
SSQGRDSHSS SLSEQSSDWP ADDMFEHPAS CELVKSKTKS EESFSDLTGS LLSLQLDLGP
SLLDEVLNVM DKNK
