ID BORG3_HUMAN Reviewed; 148 AA.
AC Q6NZY7; B0VJZ2; Q8TB51;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 134.
DE RecName: Full=Cdc42 effector protein 5;
DE AltName: Full=Binder of Rho GTPases 3;
GN Name=CDC42EP5; Synonyms=BORG3, CEP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, and Pancreas;
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CDC42, in a GTP-dependent manner, and with
CC 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; CU467002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU207370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72252.1; -; Genomic_DNA.
DR EMBL; BC024327; AAH24327.1; -; mRNA.
DR EMBL; BC065910; AAH65910.1; -; mRNA.
DR CCDS; CCDS12896.1; -.
DR RefSeq; NP_659494.2; NM_145057.3.
DR AlphaFoldDB; Q6NZY7; -.
DR BioGRID; 127125; 6.
DR IntAct; Q6NZY7; 1.
DR STRING; 9606.ENSP00000301200; -.
DR iPTMnet; Q6NZY7; -.
DR PhosphoSitePlus; Q6NZY7; -.
DR BioMuta; CDC42EP5; -.
DR DMDM; 71152342; -.
DR jPOST; Q6NZY7; -.
DR MassIVE; Q6NZY7; -.
DR MaxQB; Q6NZY7; -.
DR PaxDb; 9606-ENSP00000301200; -.
DR PeptideAtlas; Q6NZY7; -.
DR ProteomicsDB; 66800; -.
DR Antibodypedia; 50438; 94 antibodies from 23 providers.
DR DNASU; 148170; -.
DR Ensembl; ENST00000301200.3; ENSP00000301200.2; ENSG00000167617.3.
DR Ensembl; ENST00000611094.1; ENSP00000484985.1; ENSG00000273622.1.
DR Ensembl; ENST00000617756.1; ENSP00000484158.1; ENSG00000273633.1.
DR Ensembl; ENST00000619217.1; ENSP00000479726.1; ENSG00000278444.1.
DR GeneID; 148170; -.
DR KEGG; hsa:148170; -.
DR MANE-Select; ENST00000301200.3; ENSP00000301200.2; NM_145057.4; NP_659494.2.
DR UCSC; uc002qfz.3; human.
DR AGR; HGNC:17408; -.
DR CTD; 148170; -.
DR DisGeNET; 148170; -.
DR GeneCards; CDC42EP5; -.
DR HGNC; HGNC:17408; CDC42EP5.
DR HPA; ENSG00000167617; Tissue enhanced (intestine, prostate).
DR MIM; 609171; gene.
DR neXtProt; NX_Q6NZY7; -.
DR OpenTargets; ENSG00000167617; -.
DR PharmGKB; PA134989100; -.
DR VEuPathDB; HostDB:ENSG00000167617; -.
DR eggNOG; ENOG502S9WH; Eukaryota.
DR GeneTree; ENSGT00940000162969; -.
DR HOGENOM; CLU_067835_1_0_1; -.
DR InParanoid; Q6NZY7; -.
DR OMA; GVMDKDW; -.
DR OrthoDB; 4605633at2759; -.
DR PhylomeDB; Q6NZY7; -.
DR TreeFam; TF331725; -.
DR PathwayCommons; Q6NZY7; -.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR SignaLink; Q6NZY7; -.
DR BioGRID-ORCS; 148170; 9 hits in 1142 CRISPR screens.
DR ChiTaRS; CDC42EP5; human.
DR GenomeRNAi; 148170; -.
DR Pharos; Q6NZY7; Tbio.
DR PRO; PR:Q6NZY7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6NZY7; Protein.
DR Bgee; ENSG00000167617; Expressed in mucosa of transverse colon and 90 other cell types or tissues.
DR Genevisible; Q6NZY7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR InterPro; IPR029273; Cdc42_effect-like.
DR InterPro; IPR000095; CRIB_dom.
DR PANTHER; PTHR15344:SF15; CDC42 EFFECTOR PROTEIN 5; 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 2: Evidence at transcript level;
KW Cell shape; Cytoplasm; Cytoskeleton; Membrane; Methylation;
KW Reference proteome.
FT CHAIN 1..148
FT /note="Cdc42 effector protein 5"
FT /id="PRO_0000212653"
FT DOMAIN 23..37
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0X0"
FT CONFLICT 59
FT /note="E -> Q (in Ref. 3; AAH24327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 15207 MW; 48BC1A9B9307CEEC CRC64;
MPVLKQLGPA QPKKRPDRGA LSISAPLGDF RHTLHVGRGG DAFGDTSFLS RHGGGPPPEP
RAPPAGAPRS PPPPAVPQSA APSPADPLLS FHLDLGPSML DAVLGVMDAA RPEAAAAKPD
AEPRPGTQPP QARCRPNADL ELNDVIGL
//
