GEFB_DICDI
ID GEFB_DICDI Reviewed; 1529 AA.
AC Q8IS21; Q55D60; Q9GQC2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ras guanine nucleotide exchange factor B;
DE AltName: Full=RasGEF domain-containing protein B;
GN Name=gefB; Synonyms=rasGEFB; ORFNames=DDB_G0269222;
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], FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX3;
RX PubMed=11102804; DOI=10.1016/s0960-9822(00)00797-1;
RA Wilkins A., Chubb J.R., Insall R.H.;
RT "A novel Dictyostelium RasGEF is required for normal endocytosis, cell
RT motility and multicellular development.";
RL Curr. Biol. 10:1427-1437(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=AX4;
RX PubMed=16086850; DOI=10.1186/gb-2005-6-8-r68;
RA Wilkins A., Szafranski K., Fraser D.J., Bakthavatsalam D., Mueller R.,
RA Fisher P.R., Gloeckner G., Eichinger L., Noegel A.A., Insall R.H.;
RT "The Dictyostelium genome encodes numerous RasGEFs with multiple biological
RT roles.";
RL Genome Biol. 6:R68.1-R68.12(2005).
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 DISRUPTION PHENOTYPE.
RX PubMed=12854977; DOI=10.1186/1471-2156-4-12;
RA King J., Insall R.H.;
RT "Parasexual genetics of Dictyostelium gene disruptions: identification of a
RT ras pathway using diploids.";
RL BMC Genet. 4:12-12(2003).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=15740584; DOI=10.1111/j.1440-169x.2004.00776.x;
RA Ishida K., Hata T., Urushihara H.;
RT "Gamete fusion and cytokinesis preceding zygote establishment in the sexual
RT process of Dictyostelium discoideum.";
RL Dev. Growth Differ. 47:25-35(2005).
CC -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP (By
CC similarity). Involved in phagocytosis, fluid-phase endocytosis,
CC regulation of macropinocytosis and control of cell movement.
CC {ECO:0000250, ECO:0000269|PubMed:11102804}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11102804}.
CC -!- DEVELOPMENTAL STAGE: Expressed during development; especially between 8
CC and 14 hours of development. Expression reaches a maximum at around 16
CC hours, when the cell aggregation was near completion and phagocytosis
CC started. {ECO:0000269|PubMed:11102804, ECO:0000269|PubMed:15740584,
CC ECO:0000269|PubMed:16086850}.
CC -!- DISRUPTION PHENOTYPE: Grows relatively normally on bacterial plates,
CC but is unable to grow in axenic culture due to a loss of fluid-phase
CC endocytosis. The morphology of growing cells appears flattened,
CC elongate, polarized and dominated by a single large lamella. Able to
CC aggregate but not to form slugs, and does make highly aberrant fruiting
CC bodies. Cells move unusually rapidly and have lost the ability to
CC perform macropinocytosis. Crowns, the sites of macropinocytosis, are
CC replaced by polarized lamellipodia. The majority of F-actin is
CC concentrated in a single large lamella, at the leading edge of the
CC cell. Cells lacking rasS and gefB show that the cell speed of
CC unstimulated, bacterially-grown double mutants is around three times
CC the speed of wild type cells; comparable with both rasS- and
CC gefB- parents and reveal a serious defect in phagocytosis.
CC {ECO:0000269|PubMed:11102804, ECO:0000269|PubMed:12854977,
CC ECO:0000269|PubMed:16086850}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF275723; AAG29138.1; -; mRNA.
DR EMBL; AY160091; AAN46871.1; -; Genomic_DNA.
DR EMBL; AAFI02000005; EAL71961.1; -; Genomic_DNA.
DR RefSeq; XP_646271.1; XM_641179.1.
DR AlphaFoldDB; Q8IS21; -.
DR SMR; Q8IS21; -.
DR STRING; 44689.DDB0191498; -.
DR PaxDb; Q8IS21; -.
DR PRIDE; Q8IS21; -.
DR EnsemblProtists; EAL71961; EAL71961; DDB_G0269222.
DR GeneID; 8617227; -.
DR KEGG; ddi:DDB_G0269222; -.
DR dictyBase; DDB_G0269222; gefB.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_247361_0_0_1; -.
DR InParanoid; Q8IS21; -.
DR OMA; KICYALY; -.
DR Reactome; R-DDI-1169092; Activation of RAS in B cells.
DR Reactome; R-DDI-171007; p38MAPK events.
DR Reactome; R-DDI-193648; NRAGE signals death through JNK.
DR Reactome; R-DDI-354192; Integrin signaling.
DR Reactome; R-DDI-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-DDI-392517; Rap1 signalling.
DR Reactome; R-DDI-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DDI-9013148; CDC42 GTPase cycle.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q8IS21; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; TAS:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0032060; P:bleb assembly; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:1905303; P:positive regulation of macropinocytosis; IMP:dictyBase.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:dictyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:dictyBase.
DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:dictyBase.
DR GO; GO:0019953; P:sexual reproduction; IEP:dictyBase.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 2.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Endocytosis; Guanine-nucleotide releasing factor;
KW Phagocytosis; Reference proteome.
FT CHAIN 1..1529
FT /note="Ras guanine nucleotide exchange factor B"
FT /id="PRO_0000384460"
FT DOMAIN 1075..1205
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 1282..1517
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 290..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..186
FT /evidence="ECO:0000255"
FT COILED 722..798
FT /evidence="ECO:0000255"
FT COILED 871..898
FT /evidence="ECO:0000255"
FT COMPBIAS 847..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 145
FT /note="L -> I (in Ref. 1; AAG29138)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073
FT /note="D -> G (in Ref. 1; AAG29138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1529 AA; 174053 MW; 70C0AB03348EDAC3 CRC64;
MVVILWGWNE NRFNTLDQVI SFDFIEENKK LYLKILENEK QQKIYNISNL IGRRMDNYRD
NNNNNGNGSN INNNGIIINS SMGSQYFNLN KGIIIVESDN ETFLIEEIDY LGKFPILKQF
IKCEEFIGIS TLEIISNIEK QLSNLVNLKS NTTEQTDRKY KTNLIDFKES IIQLEKDCKN
LLKQSNLINP SIKYSVVKSV KFLLKEIKFE FYHGDINIKR IELFQQLKKF LKIHFWNNPN
LILNSGSNID MTDSNDSISS EEINSPNDLN LSLSSFPSIS SPSNSSYNNI NTLTFSNNNN
NNNNNSNNNN NNNNNNNNNN SIINSNNNNN SNNNSNISNS SNNNNNNSNN SNNISINVSK
TGNNSVINSP TQSSSCYIDC DDTMSNYTDC TNTTNTNSTT TTTTTTTTYG NNLNVYNNNN
NNNTNNNNNN VPYKKPALKM MKSPSFKIQL IQEVYLEIMD QCKKIQNYLY ELLDTYLTDE
EYINNNNNNN NKDISILFEN NTSYCIAQEI FISLIKNSND FLYQVQLIDL TDTRKKSKEL
SEVSNQLFYS TQQLFPSISD HLDFIEMDIF TNNNTTTTTT TTTTTTNTTT NPSNTIKSSH
SSLLSSSYSS SKDDDIVLTI NKVLSKLDTF SKEYTKLIGN NLSSNYYVDS GNNNESVSSP
KCGLFLSHSL STDSPMTYVK RNTSSGSSAS TSSYTTPVSS SASLSFSSST QTPSSAASQH
HIQQILQQQQ QQQQQQQQQQ QQQQPQQIQS QSQQQHQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQIQSQSQ QQQQLNRKPH YSSISPTSML VYNATGGKFG VVNQNNNSAE STPTFQLNTM
DILNSLMGKE GQNSNTNNAN NPNNNNNNNN NNNNNNNNNN NNNNNNENKN ENKNETNKSG
HNYNNSSTST LSSSTTIGDL ANVSSTNSPN SSTPNLLLPP HQFHNHNREY NHSHHHLLSS
SSNNVMINNR SIGKSFSTGN FSQPQPIMPS NGIGGSGGGG LGTTLSVGNG GIVGGLQSRS
SSFEENQLQY AIESFMEVYN HLTSKDKVDT SIWLEEEKED INVYYINNTN IDDKFYRSIK
YASLNQLILK LTCESNTELR FTKTFITTYR SFTTGDIFLM KLIQRYFTPN LKNIVPYQFV
QKIQIPIQLR VLNVLRLWIE QYPSDFQQPP QITTQSTQPI QNSTTQPQPQ PQPQQPQPQL
QQSTNLQNST IQQPSLFKML TAFLNSTRRN GHGQYSDLIL KKFKQQKQKD RLQLPIINNG
QGIPKAKIFW MKYSTEFIFS QSSTDIAEQL TLLDFDSYKS IEEIELLNQA WSKPDQKTNT
PNIASMVNRF NSFSSFVSWA ILRENDIKQR SKMMLKMIKI CYALYKLSNF NGLLAGLSGL
MASGVYRLNH TKSLISKQYQ KKFDFLCKFL DTKKSHKVYR DIIHSTCPPL IPYLGIYLTD
LTFIEDGNQD EIKGLINFKK REMIFNTILE IQQYQQQGYT IKPKPSVLGF LCELPHMSDK
KKFEDDTYEQ SILLEPKNST KLEVMNAKK
