ID BORG5_RAT Reviewed; 388 AA.
AC A1A5P0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=Cdc42 effector protein 1;
DE AltName: Full=Binder of Rho GTPases 5;
GN Name=Cdc42ep1 {ECO:0000312|EMBL:AAI28745.1};
GN Synonyms=Borg5 {ECO:0000250|UniProtKB:Q00587};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAI28745.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung {ECO:0000312|EMBL:AAI28745.1};
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-207; SER-209;
RP SER-298; SER-318; SER-347 AND SER-350, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Probably involved in the organization of the actin
CC cytoskeleton. Induced membrane extensions in fibroblasts (By
CC similarity). {ECO:0000250|UniProtKB:Q00587}.
CC -!- SUBUNIT: Interacts with RHOQ and CDC42, in a GTP-dependent manner.
CC {ECO:0000250|UniProtKB:Q00587}.
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.
CC {ECO:0000250|UniProtKB:Q00587}.
CC -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000255}.
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DR EMBL; BC128744; AAI28745.1; -; mRNA.
DR RefSeq; NP_001073168.1; NM_001079700.1.
DR RefSeq; XP_017450354.1; XM_017594865.1.
DR RefSeq; XP_017450355.1; XM_017594866.1.
DR RefSeq; XP_017450356.1; XM_017594867.1.
DR RefSeq; XP_017450357.1; XM_017594868.1.
DR AlphaFoldDB; A1A5P0; -.
DR IntAct; A1A5P0; 2.
DR STRING; 10116.ENSRNOP00000011269; -.
DR iPTMnet; A1A5P0; -.
DR PhosphoSitePlus; A1A5P0; -.
DR PaxDb; 10116-ENSRNOP00000011269; -.
DR PeptideAtlas; A1A5P0; -.
DR Ensembl; ENSRNOT00000011270.5; ENSRNOP00000011269.2; ENSRNOG00000008517.5.
DR Ensembl; ENSRNOT00055051377; ENSRNOP00055042344; ENSRNOG00055029655.
DR Ensembl; ENSRNOT00060036196; ENSRNOP00060029767; ENSRNOG00060020877.
DR GeneID; 315121; -.
DR KEGG; rno:315121; -.
DR AGR; RGD:1311131; -.
DR CTD; 11135; -.
DR RGD; 1311131; Cdc42ep1.
DR eggNOG; ENOG502RZ2H; Eukaryota.
DR GeneTree; ENSGT00940000160068; -.
DR HOGENOM; CLU_787446_0_0_1; -.
DR InParanoid; A1A5P0; -.
DR OMA; SWESQDE; -.
DR OrthoDB; 5317526at2759; -.
DR PhylomeDB; A1A5P0; -.
DR TreeFam; TF331725; -.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:A1A5P0; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000008517; Expressed in stomach and 20 other cell types or tissues.
DR Genevisible; A1A5P0; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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:0031267; F:small GTPase binding; 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:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR InterPro; IPR029273; Cdc42_effect-like.
DR InterPro; IPR000095; CRIB_dom.
DR PANTHER; PTHR15344:SF7; CDC42 EFFECTOR PROTEIN 1; 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; Repeat.
FT CHAIN 1..388
FT /note="Cdc42 effector protein 1"
FT /id="PRO_0000278120"
FT DOMAIN 38..52
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REPEAT 237..243
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 250..256
FT /note="2"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..270
FT /note="2 X 7 AA tandem repeats of [PT]-[AT]-A-[ENT]-[PT]-
FT [PTS]-[AG]"
FT /evidence="ECO:0000255"
FT REGION 237..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Polar 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:0000250|UniProtKB:Q91W92"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91W92"
FT MOD_RES 53
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
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:22673903"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91W92"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00587"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 388 AA; 41029 MW; 62D900F6AEDBEC3E CRC64;
MPGPQGGTGA PSMSLGKLSP VGWVPSSHGK RRLTADMISP PLGDFRHTMH VGRGGDVFGD
TSFLSNHGGR SGNTHRSPRS FLARKLQQVR RVGVPPRRMA SPAATSPAPP PISPIIKNAI
SLPQLNQATY DSLVVSKLSF DSTPASSTDG RSGYGLESGF CTISRLPRVE KHSSRDRDHD
RDPDHSQDRE QSSSPSEPNP NPELRRSDSL LSFRFDLDLG PSLLSELLGV MSLSEAPAAN
PPAPAANPAP TAKPPADAVT TLDTVTSLPA PTASSPSSGR FPNGVTAVLG PVAEVKASPV
GEGPQVPSKM AFDRRGASWG AIRASRHYTE MDARRELAGV LPQVHGSWES LNEEWSAPPA
SSRAPVPSTV QANAFEFADA DEDDEVKV
//
