BORG5_MOUSE
ID BORG5_MOUSE Reviewed; 409 AA.
AC Q91W92; Q9D8M1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Cdc42 effector protein 1;
DE AltName: Full=Binder of Rho GTPases 5;
GN Name=Cdc42ep1; Synonyms=Borg5, Cep1;
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=Pancreas;
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=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP 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 THR-34; SER-39; SER-121; SER-139;
RP SER-207; SER-368 AND SER-371, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and 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. Induced membrane extensions in fibroblasts (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RHOQ and CDC42, in a GTP-dependent manner.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- DOMAIN: The CRIB domain mediates interaction with CDC42. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000305}.
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DR EMBL; AK007896; BAB25335.1; -; mRNA.
DR EMBL; BC016250; AAH16250.1; -; mRNA.
DR EMBL; BC083130; AAH83130.1; -; mRNA.
DR CCDS; CCDS27624.1; -.
DR RefSeq; NP_081495.1; NM_027219.3.
DR AlphaFoldDB; Q91W92; -.
DR BioGRID; 222639; 2.
DR IntAct; Q91W92; 1.
DR MINT; Q91W92; -.
DR STRING; 10090.ENSMUSP00000060930; -.
DR iPTMnet; Q91W92; -.
DR PhosphoSitePlus; Q91W92; -.
DR jPOST; Q91W92; -.
DR MaxQB; Q91W92; -.
DR PaxDb; Q91W92; -.
DR PeptideAtlas; Q91W92; -.
DR PRIDE; Q91W92; -.
DR ProteomicsDB; 265451; -.
DR DNASU; 104445; -.
DR GeneID; 104445; -.
DR KEGG; mmu:104445; -.
DR UCSC; uc007wrl.1; mouse.
DR CTD; 11135; -.
DR MGI; MGI:1929763; Cdc42ep1.
DR eggNOG; ENOG502RZ2H; Eukaryota.
DR InParanoid; Q91W92; -.
DR OrthoDB; 1244464at2759; -.
DR PhylomeDB; Q91W92; -.
DR TreeFam; TF331725; -.
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-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 104445; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Cdc42ep1; mouse.
DR PRO; PR:Q91W92; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91W92; protein.
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:0005886; C:plasma membrane; IBA:GO_Central.
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.
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; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..409
FT /note="Cdc42 effector protein 1"
FT /id="PRO_0000212658"
FT DOMAIN 38..52
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REPEAT 235..241
FT /note="1"
FT REPEAT 242..248
FT /note="2"
FT REPEAT 255..261
FT /note="3"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..284
FT /note="3 X 7 AA tandem repeats of [PT]-[AT]-A-[ENT]-[PT]-
FT [PTS]-[AG]"
FT REGION 237..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..256
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 53
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1A5P0"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1A5P0"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 286
FT /note="A -> V (in Ref. 1; BAB25335)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="T -> A (in Ref. 1; BAB25335)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="T -> A (in Ref. 1; BAB25335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 43096 MW; 1794FD0850171F0E CRC64;
MPGPQGGTGA PTMSLGKLSP VGWVSSSHGK RRLTADMISP PLGDFRHTMH VGRGGDVFGD
TSFLSNHGGR SGNTHRSPRS FLARKLQQVR RVGVPPRRMA SPAAPSPAPP PISPIIKNAI
SLPQLNQATY DSLVMGKLSF DSTPASSTDG HSGYGLESGF CTISRLPRVE KHSNRDRDRD
PDHSQDREQS SFPSEPTPNP ELRRSDSLLS FRFDLDLGPS LLSELLGVMS LSEAPAAETP
VPTANPPAPA ANPAPTAKPP AHAITTLDAV TSLPASAVTS LPAPAAASSP SRGHFPNGVT
SVLGPAAEAK PSPVGEGPQV PSNMTFDRHG ASWGASRASW GASRASRHYT EMDARRELAG
VLPQVHGSWE SLNEDWSTPP ASVRAPVPTS VQVNAFEFAD AEEDDEVKV
