BORG3_MOUSE
ID BORG3_MOUSE Reviewed; 150 AA.
AC Q9Z0X0; Q3SYK1; Q9QZT9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cdc42 effector protein 5;
DE AltName: Full=Binder of Rho GTPases 3;
GN Name=Cdc42ep5; Synonyms=Borg3, Cep5;
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], FUNCTION, INTERACTION WITH CDC42, MUTAGENESIS
RP OF 23-ILE-SER-24, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH CDC42.
RX PubMed=11035016; DOI=10.1074/jbc.m007039200;
RA Hirsch D.S., Pirone D.M., Burbelo P.D.;
RT "A new family of Cdc42 effector proteins, CEPs, function in fibroblast and
RT epithelial cell shape changes.";
RL J. Biol. Chem. 276:875-883(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and 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 [5]
RP FUNCTION, AND INTERACTION WITH SEPT7.
RX PubMed=11584266; DOI=10.1038/ncb1001-861;
RA Joberty G., Perlungher R.R., Sheffield P.J., Kinoshita M., Noda M.,
RA Haystead T., Macara I.G.;
RT "Borg proteins control septin organization and are negatively regulated by
RT Cdc42.";
RL Nat. Cell Biol. 3:861-866(2001).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-38, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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. Inhibits MAPK8 independently of CDC42 binding. Controls
CC septin organization and this effect is negatively regulated by CDC42.
CC {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016,
CC ECO:0000269|PubMed:11584266}.
CC -!- SUBUNIT: Interacts with CDC42 in a GTP-dependent manner, and with
CC SEPT7. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016,
CC ECO:0000269|PubMed:11584266}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:11035016}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11035016}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11035016}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the skeletal muscle.
CC {ECO:0000269|PubMed:10490598}.
CC -!- DOMAIN: The CRIB domain mediates interaction with CDC42.
CC -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000305}.
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DR EMBL; AF164119; AAD48816.1; -; mRNA.
DR EMBL; AF102773; AAD17906.1; -; mRNA.
DR EMBL; AK008154; BAB25498.1; -; mRNA.
DR EMBL; BC006758; AAH06758.1; -; mRNA.
DR EMBL; BC103774; AAI03775.1; -; mRNA.
DR CCDS; CCDS20733.1; -.
DR RefSeq; NP_067429.1; NM_021454.3.
DR RefSeq; XP_006540313.1; XM_006540250.3.
DR AlphaFoldDB; Q9Z0X0; -.
DR STRING; 10090.ENSMUSP00000092508; -.
DR iPTMnet; Q9Z0X0; -.
DR PhosphoSitePlus; Q9Z0X0; -.
DR jPOST; Q9Z0X0; -.
DR MaxQB; Q9Z0X0; -.
DR PaxDb; Q9Z0X0; -.
DR PeptideAtlas; Q9Z0X0; -.
DR PRIDE; Q9Z0X0; -.
DR ProteomicsDB; 281700; -.
DR Antibodypedia; 50438; 81 antibodies from 23 providers.
DR Ensembl; ENSMUST00000076831; ENSMUSP00000092508; ENSMUSG00000063838.
DR GeneID; 58804; -.
DR KEGG; mmu:58804; -.
DR UCSC; uc009exe.1; mouse.
DR CTD; 148170; -.
DR MGI; MGI:1929745; Cdc42ep5.
DR VEuPathDB; HostDB:ENSMUSG00000063838; -.
DR eggNOG; ENOG502S9WH; Eukaryota.
DR GeneTree; ENSGT00940000162969; -.
DR InParanoid; Q9Z0X0; -.
DR OMA; GVMDKDW; -.
DR OrthoDB; 1500881at2759; -.
DR PhylomeDB; Q9Z0X0; -.
DR TreeFam; TF331725; -.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR BioGRID-ORCS; 58804; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cdc42ep5; mouse.
DR PRO; PR:Q9Z0X0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z0X0; protein.
DR Bgee; ENSMUSG00000063838; Expressed in intestinal villus and 202 other tissues.
DR ExpressionAtlas; Q9Z0X0; baseline and differential.
DR Genevisible; Q9Z0X0; MM.
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:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:MGI.
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.
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; Methylation;
KW Reference proteome.
FT CHAIN 1..150
FT /note="Cdc42 effector protein 5"
FT /id="PRO_0000212654"
FT DOMAIN 23..37
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MUTAGEN 23..24
FT /note="IS->AA: No binding with CDC42."
FT /evidence="ECO:0000269|PubMed:10490598"
FT CONFLICT 20
FT /note="A -> R (in Ref. 2; AAD17906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 150 AA; 15545 MW; 9AB9A49A9518B200 CRC64;
MPVMKQLGPA QPKKRLDRGA LSISAPLGDF RHTLHVGRGG DAFGDTSFLS RHGGGPPPEP
GAPPVVAPHS VAPPAAPQPP VAVPSPADPL LSFHLDLGPS MLDAVLGVMD AERSETTATK
PDGDAHPRVQ HPKTRCCSNA DLQLDDVIGL
