RAC1B_DICDI
ID RAC1B_DICDI Reviewed; 194 AA.
AC P34145; Q55EG7; Q9GPT7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Rho-related protein rac1B;
DE Flags: Precursor;
GN Name=rac1B; ORFNames=DDB_G0268622;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RX PubMed=8294042; DOI=10.1016/0378-1119(93)90448-c;
RA Bush J.M. IV, Franek K., Cardelli J.A.;
RT "Cloning and characterization of seven novel Dictyostelium discoideum rac-
RT related genes belonging to the rho family of GTPases.";
RL Gene 136:61-68(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=11222756; DOI=10.1093/nar/29.5.1068;
RA Rivero F., Dislich H., Gloeckner G., Noegel A.A.;
RT "The Dictyostelium discoideum family of Rho-related proteins.";
RL Nucleic Acids Res. 29:1068-1079(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP INTERACTION WITH RGAA.
RX PubMed=9739079; DOI=10.1242/jcs.111.20.3059;
RA Faix J., Clougherty C., Konzok A., Mintert U., Murphy J., Albrecht R.,
RA Muhlbauer B., Kuhlmann J.;
RT "The IQGAP-related protein DGAP1 interacts with Rac and is involved in the
RT modulation of the F-actin cytoskeleton and control of cell motility.";
RL J. Cell Sci. 111:3059-3071(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH RGAA.
RX PubMed=10825297; DOI=10.1242/jcs.113.12.2253;
RA Dumontier M., Hoecht P., Mintert U., Faix J.;
RT "Rac1 GTPases control filopodia formation, cell motility, endocytosis,
RT cytokinesis and development in Dictyostelium.";
RL J. Cell Sci. 113:2253-2265(2000).
RN [6]
RP INTERACTION WITH PAKB.
RX PubMed=15509655; DOI=10.1091/mbc.e04-06-0534;
RA de la Roche M., Mahasneh A., Lee S.-F., Rivero F., Cote G.P.;
RT "Cellular distribution and functions of wild-type and constitutively
RT activated Dictyostelium PakB.";
RL Mol. Biol. Cell 16:238-247(2005).
CC -!- FUNCTION: Overexpression promotes the formation of filopodia and
CC membrane ruffles. {ECO:0000269|PubMed:10825297}.
CC -!- SUBUNIT: Interacts with pakB. Interacts (in GTP-bound form) with rgaA.
CC {ECO:0000269|PubMed:10825297, ECO:0000269|PubMed:15509655,
CC ECO:0000269|PubMed:9739079}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; L11589; AAC37392.1; -; mRNA.
DR EMBL; AF310884; AAG45110.1; -; Genomic_DNA.
DR EMBL; AAFI02000004; EAL72900.2; -; Genomic_DNA.
DR RefSeq; XP_647053.2; XM_641961.2.
DR AlphaFoldDB; P34145; -.
DR SMR; P34145; -.
DR IntAct; P34145; 1.
DR STRING; 44689.DDB0219941; -.
DR PaxDb; P34145; -.
DR EnsemblProtists; EAL72900; EAL72900; DDB_G0268622.
DR GeneID; 8616748; -.
DR KEGG; ddi:DDB_G0268622; -.
DR dictyBase; DDB_G0268622; rac1B.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P34145; -.
DR OMA; DRRMQPI; -.
DR PhylomeDB; P34145; -.
DR Reactome; R-DDI-9013406; RHOQ GTPase cycle.
DR Reactome; R-DDI-9013407; RHOH GTPase cycle.
DR Reactome; R-DDI-9013409; RHOJ GTPase cycle.
DR Reactome; R-DDI-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DDI-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-DDI-9706019; RHOBTB3 ATPase cycle.
DR PRO; PR:P34145; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0043326; P:chemotaxis to folate; IMP:dictyBase.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IMP:dictyBase.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:dictyBase.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:dictyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:dictyBase.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:dictyBase.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0019953; P:sexual reproduction; IEP:dictyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..191
FT /note="Rho-related protein rac1B"
FT /id="PRO_0000198896"
FT PROPEP 192..194
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281247"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 191
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 109
FT /note="P -> R (in Ref. 1; AAC37392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 21676 MW; 6392823A12624E50 CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP INLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSIVSPASF ENVNGKWHPE ICHHAPNVPI ILVGTKLDMR
EDRDTQDRLK EKKLYPVSYE QGLSKMKEIN AVKYLECSAL TQKGLKTVFD EAIRSVINPT
LKKKPKSSKG CIIM
