BORG1_RAT
ID BORG1_RAT Reviewed; 214 AA.
AC Q5PQP4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cdc42 effector protein 2;
DE AltName: Full=Binder of Rho GTPases 1;
GN Name=Cdc42ep2; Synonyms=Borg1, Cep2;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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-101; SER-137 AND SER-141, AND
RP IDENTIFICATION BY MASS 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. May act downstream of CDC42 to induce actin filament
CC assembly leading to cell shape changes. Induces pseudopodia formation
CC in fibroblasts in a CDC42-dependent manner (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CDC42 and RHOQ, 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 -!- 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; BC087091; AAH87091.1; -; mRNA.
DR RefSeq; NP_001009689.1; NM_001009689.1.
DR RefSeq; XP_006230868.1; XM_006230806.3.
DR RefSeq; XP_006230869.1; XM_006230807.3.
DR RefSeq; XP_017444741.1; XM_017589252.1.
DR RefSeq; XP_017444742.1; XM_017589253.1.
DR RefSeq; XP_017444743.1; XM_017589254.1.
DR RefSeq; XP_017444744.1; XM_017589255.1.
DR AlphaFoldDB; Q5PQP4; -.
DR STRING; 10116.ENSRNOP00000028379; -.
DR iPTMnet; Q5PQP4; -.
DR PhosphoSitePlus; Q5PQP4; -.
DR PaxDb; Q5PQP4; -.
DR Ensembl; ENSRNOT00000028379; ENSRNOP00000028379; ENSRNOG00000020904.
DR Ensembl; ENSRNOT00000096503; ENSRNOP00000079453; ENSRNOG00000020904.
DR Ensembl; ENSRNOT00000105520; ENSRNOP00000095646; ENSRNOG00000020904.
DR GeneID; 309175; -.
DR KEGG; rno:309175; -.
DR UCSC; RGD:1310253; rat.
DR CTD; 10435; -.
DR RGD; 1310253; Cdc42ep2.
DR eggNOG; ENOG502RY28; Eukaryota.
DR GeneTree; ENSGT00940000161776; -.
DR HOGENOM; CLU_073229_0_0_1; -.
DR InParanoid; Q5PQP4; -.
DR OMA; MQCDISS; -.
DR OrthoDB; 1244464at2759; -.
DR PhylomeDB; Q5PQP4; -.
DR TreeFam; TF331725; -.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR PRO; PR:Q5PQP4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020904; Expressed in jejunum and 20 other tissues.
DR Genevisible; Q5PQP4; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0001515; F:opioid peptide activity; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
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; IBA:GO_Central.
DR InterPro; IPR029273; Cdc42_effect.
DR InterPro; IPR017363; Cdc42_effector_prot_2.
DR InterPro; IPR000095; CRIB_dom.
DR Pfam; PF14957; BORG_CEP; 2.
DR Pfam; PF00786; PBD; 1.
DR PIRSF; PIRSF038036; Cdc42_effector_p2; 1.
DR SMART; SM00285; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell shape; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14613"
FT CHAIN 2..214
FT /note="Cdc42 effector protein 2"
FT /id="PRO_0000212650"
FT DOMAIN 30..44
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 118..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O14613"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14613"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZX9"
SQ SEQUENCE 214 AA; 23048 MW; 93BCAF80D7D2C903 CRC64;
MSTKVPIYLK RGSRKGKKEK LRDLLSSDMI SPPLGDFRHT IHIGSGGGDD MFGDISFLQG
KFHLLPGTAV EEAEEDGSFD LPFQFTRTTT VCGRELPGGL SPLLKNAISL PVIGGPQALT
LPTTQAPPKP PRLHLESPQP SPKSSPQEAG NVDIWRVPEA GLPHNGMSPE PEAEEPFLSH
ASSLLSLHVD LGPSILDDVL QIMDQDLGRV QIPT
