ID BORG4_MOUSE Reviewed; 349 AA.
AC Q9JM96; Q3TNF3; Q9QZT8;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 165.
DE RecName: Full=Cdc42 effector protein 4;
DE AltName: Full=Binder of Rho GTPases 4;
GN Name=Cdc42ep4; Synonyms=Borg4, Cep4;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Ileal mucosa;
RX PubMed=11185749; DOI=10.1007/s100380070012;
RA Osada N., Kusuda J., Suzuki Y., Sugano S., Hashimoto K.;
RT "Sequence analysis, gene expression, and chromosomal assignment of mouse
RT Borg4 gene and its human orthologue.";
RL J. Hum. Genet. 45:374-377(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-143, AND INTERACTION WITH RHOQ AND CDC42.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-64; SER-107 AND
RP SER-223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
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 when overexpressed in fibroblasts.
CC -!- SUBUNIT: Interacts with CDC42 and RHOQ, in a GTP-dependent manner.
CC {ECO:0000269|PubMed:10490598}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11185749}.
CC -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000305}.
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DR EMBL; AB035088; BAA95932.1; -; mRNA.
DR EMBL; AK075739; BAC35920.1; -; mRNA.
DR EMBL; AK165318; BAE38136.1; -; mRNA.
DR EMBL; BC003857; AAH03857.1; -; mRNA.
DR EMBL; AF165114; AAD47822.1; -; mRNA.
DR CCDS; CCDS25604.1; -.
DR RefSeq; NP_001156818.1; NM_001163346.1.
DR RefSeq; NP_064390.1; NM_020006.2.
DR RefSeq; XP_006533880.1; XM_006533817.2.
DR RefSeq; XP_006533881.1; XM_006533818.3.
DR RefSeq; XP_006533882.1; XM_006533819.2.
DR RefSeq; XP_017170175.1; XM_017314686.1.
DR AlphaFoldDB; Q9JM96; -.
DR BioGRID; 208129; 4.
DR MINT; Q9JM96; -.
DR STRING; 10090.ENSMUSP00000102227; -.
DR iPTMnet; Q9JM96; -.
DR PhosphoSitePlus; Q9JM96; -.
DR SwissPalm; Q9JM96; -.
DR jPOST; Q9JM96; -.
DR MaxQB; Q9JM96; -.
DR PaxDb; 10090-ENSMUSP00000102227; -.
DR PeptideAtlas; Q9JM96; -.
DR ProteomicsDB; 281701; -.
DR Pumba; Q9JM96; -.
DR Antibodypedia; 31920; 179 antibodies from 29 providers.
DR DNASU; 56699; -.
DR Ensembl; ENSMUST00000053536.5; ENSMUSP00000060227.5; ENSMUSG00000041598.8.
DR Ensembl; ENSMUST00000106616.2; ENSMUSP00000102227.2; ENSMUSG00000041598.8.
DR GeneID; 56699; -.
DR KEGG; mmu:56699; -.
DR UCSC; uc007mfb.2; mouse.
DR AGR; MGI:1929760; -.
DR CTD; 23580; -.
DR MGI; MGI:1929760; Cdc42ep4.
DR VEuPathDB; HostDB:ENSMUSG00000041598; -.
DR eggNOG; ENOG502QRD6; Eukaryota.
DR GeneTree; ENSGT00940000161435; -.
DR InParanoid; Q9JM96; -.
DR OMA; HAESMMS; -.
DR OrthoDB; 4097104at2759; -.
DR PhylomeDB; Q9JM96; -.
DR TreeFam; TF331725; -.
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 BioGRID-ORCS; 56699; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Cdc42ep4; mouse.
DR PRO; PR:Q9JM96; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JM96; Protein.
DR Bgee; ENSMUSG00000041598; Expressed in floor plate of midbrain and 265 other cell types or tissues.
DR ExpressionAtlas; Q9JM96; baseline and differential.
DR Genevisible; Q9JM96; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to type II interferon; IDA: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; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR InterPro; IPR029273; Cdc42_effect-like.
DR InterPro; IPR000095; CRIB_dom.
DR PANTHER; PTHR15344:SF14; CDC42 EFFECTOR PROTEIN 4; 1.
DR PANTHER; PTHR15344; CDC42 EFFECTOR PROTEIN BORG; 1.
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; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..349
FT /note="Cdc42 effector protein 4"
FT /id="PRO_0000212656"
FT DOMAIN 27..41
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 123..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Q1"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Q1"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Q1"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Q1"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Q1"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Q1"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Q1"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Q1"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Q1"
FT CONFLICT 143
FT /note="K -> R (in Ref. 4; AAD47822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 37869 MW; 7C44125A7083E16B CRC64;
MPILKQLVSS SVNSKRRSRA DLTAEMISAP LGDFRHTMHV GRAGDAFGDT SFLTSKAREA
DDESLDEQAS ASKLSLLSRK FRGSKRSQSV TRGDREQRDM LGSLRDSALF VKNAMSLPQL
NEKEAAEKDS SKLPKSLSSS PVKKADARDG GPKSPHRNGA TGPHSPDPLL DEQAFGDLMD
LPIMPKVSYG LKHAESILSF HIDLGPSMLG DVLSIMDKDQ WGSEEEEEAG GYRDKEGPSS
IVQAPPVLEV VPPLGRQESK ASWDQASMLP PHAVEDDGWA VVAPSPSSAR SVGSHTTRDS
SSLSSYTSGV LEERSPAFRG PDRVAAAPPR QPDKEFCFMD EEEEDEIRV
//
