GXCDD_DICDI
ID GXCDD_DICDI Reviewed; 1632 AA.
AC Q1ZXH8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Guanine exchange factor for Rac 30;
GN Name=gxcDD; ORFNames=DDB_G0279733;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORMS 1 AND 2).
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN CH, AND DISRUPTION PHENOTYPE.
RX PubMed=17584488; DOI=10.1186/1471-2121-8-23;
RA Mondal S., Neelamegan D., Rivero F., Noegel A.A.;
RT "GxcDD, a putative RacGEF, is involved in Dictyostelium development.";
RL BMC Cell Biol. 8:23-23(2007).
CC -!- FUNCTION: GTPase-activating protein for Rac involved in streaming and
CC development. {ECO:0000269|PubMed:17584488}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17584488};
CC Peripheral membrane protein {ECO:0000269|PubMed:17584488}. Cytoplasmic
CC vesicle, phagosome membrane {ECO:0000269|PubMed:17584488}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17584488}. Note=Accumulates in
CC cortical regions of the cell and on phagosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1ZXH8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1ZXH8-2; Sequence=VSP_041271;
CC -!- DOMAIN: The membrane association is mediated by the calponin-homology
CC (CH) domain. {ECO:0000269|PubMed:17584488}.
CC -!- DISRUPTION PHENOTYPE: Cells display defective streaming during
CC development under different conditions and a delay in developmental
CC timing. {ECO:0000269|PubMed:17584488}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAS66880.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AAFI02000032; EAS66880.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001134564.2; XM_001134564.2.
DR AlphaFoldDB; Q1ZXH8; -.
DR SMR; Q1ZXH8; -.
DR STRING; 44689.DDB0233183; -.
DR PaxDb; Q1ZXH8; -.
DR PRIDE; Q1ZXH8; -.
DR EnsemblProtists; EAS66880; EAS66880; DDB_G0279733.
DR GeneID; 8622170; -.
DR KEGG; ddi:DDB_G0279733; -.
DR dictyBase; DDB_G0279733; gxcDD.
DR eggNOG; KOG0518; Eukaryota.
DR eggNOG; KOG0703; Eukaryota.
DR eggNOG; KOG3522; Eukaryota.
DR InParanoid; Q1ZXH8; -.
DR Reactome; R-DDI-193648; NRAGE signals death through JNK.
DR Reactome; R-DDI-9013148; CDC42 GTPase cycle.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q1ZXH8; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005938; C:cell cortex; IMP:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005856; C:cytoskeleton; IDA:dictyBase.
DR GO; GO:0032009; C:early phagosome; IMP:dictyBase.
DR GO; GO:0016020; C:membrane; IDA:dictyBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:dictyBase.
DR GO; GO:0031267; F:small GTPase binding; IDA:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 3.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00233; PH; 3.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 4: Predicted;
KW Alternative splicing; Cytoplasmic vesicle; GTPase activation; Membrane;
KW Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1632
FT /note="Guanine exchange factor for Rac 30"
FT /id="PRO_0000327580"
FT DOMAIN 16..122
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 388..417
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 432..461
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 460..638
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 940..1038
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1271..1389
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT DOMAIN 1532..1631
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 1286..1309
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 134..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1125..1282
FT /note="VLYHINNFISTSTSTSASQSQSQSPSPSPSHSINQKQKIRKLSFYQSRSNTL
FT ININNDEDRLNSFPTSTLSVSCLLNNDNHGNNDFDGKSFTNNIDITTTTTTNDDNNNNT
FT TTTQVKKGKDLSCSKELNCSISHDDNSKGSSGYGNNSCGDNINNDES -> DSILNIPG
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041271"
SQ SEQUENCE 1632 AA; 181123 MW; 7C5FEA83CECCAB76 CRC64;
MQPKDYMSSS HANWENIQID SFTSWINQHL SERGLSVKDL SVDFQDGVLL LNLLEILSGK
KIARYVRSPK FLQHKIDNIM IAFNFMEKAF DIKVFGCNAK DIVDGNLKQT MGVIFLLIQK
IKVNLHLDHL QEQQGETTGT TTTITSTNTT TTPTKPRFYR ASMQVNAANR FSHISPNKDQ
SSSTVATTTT TSTSVVQPQP QPTTATPTTT TATTLTPPVA SQQPVSTAPA TVTPSTVIPT
VTPLNTTTTT TTATSTSTNV PTATTNVPPT ATTTTTGTRI SPTTGVSVST IRSKFLFEGG
TGNTTGGNEK YNTYSPGSGN TSGVVGPSTS SSLNISSERV LKRTESGYLI SGGLSLSGSG
SGGIHEPLQR TVSLIEIKLN DHQSKFYDLK KIIFMQSVIR GYLVRSKWRN VLEKYKQHLN
EYKKHFMNNK KAYRGLIRVQ AIVKGKIQRK KLFKMFPLYR RNEIVKEILS TEDKYVTSLA
MVTTHYLKPS EAFLSTQQVR SIFSQIEIIH RYNSLILEKL VSRNKIWYSS GQKIGDIFIE
MSAFLKVYTI YVNNYNNSIQ TITECMEIPK FASLLEKNRN QFGLDLSAFL IAPIQRIPRY
ILLLQDLLKN TKESHPDHQD LSLALKKMKD VAEYVNEKKR EAENLNQVLT IQSSLTGKFN
NLAEPHRRYV KKGTLISNDK IHLYFLFNDL LVKTENKIVS KIRDSARLSN NNSSDKNSKS
TFHSPKEIIN EGKSKYLNSY FLAGSSLVDS NPDGFTFQII GVGDANELNS QINNQINNQN
NNQNNNQNNN LNNNNDDSPI LSFSPFSSSF ASTITNSLSS IGNSNNVNNN NNTSSNSGFV
NSSNNNINIV NSNGSSPLTN SGHGLNSSFG ISSNNNNNLT MPTTSIQLEA LSLNEKMTWM
GELDECIFQL LEKSKSKKRS LITDADELTT VPFDISVVKD SEFSNVLEKK HSEISWRSKK
FYLKNTHLYY HRYSSTESPK EPTKIKCINL ILCSVKLAQV VDHPHCFQLI TPSRIYFFSC
EDSTVLFQWI SLIRLSIKKK LESLKDENNN INNFTSIASA TSPTSSSSNT TPIVVPIASH
SNATGSLSAS LGSSFLNQQQ RSLEQQQHLN TSNSNLTPLA LSSQVLYHIN NFISTSTSTS
ASQSQSQSPS PSPSHSINQK QKIRKLSFYQ SRSNTLININ NDEDRLNSFP TSTLSVSCLL
NNDNHGNNDF DGKSFTNNID ITTTTTTNDD NNNNTTTTQV KKGKDLSCSK ELNCSISHDD
NSKGSSGYGN NSCGDNINND ESNNNCAECG ASDPSWVSIN YGVVVCLDCS SIHKNLPEGN
VKSVRSLSVA FSDIVKKQEG NIKANNKYEK NIPSGLTKPN PKDSYEIKLS WIKAKYINNN
NNNNNSQNGD STTPTPTPTS TTIHVNNDST PTSPNLNSQS SPPPTATTTQ TENVKLDNGR
SSPTPTPTQT ENNNNNVLTP TTTTTNTTTS TTTGSRPTTP TILNNEEEHI QGINLKDSTD
TSNGKGTWSR GSSHAITERK TSFLDKPRVP VKKEHQGYLF KTSSPTSNNS SDWKKYLFVY
KNDVLTYYKV SKKNKRKEKG IIDLFHSVKQ ESRPKQKYSF TLVTSQRLYF LASETEEEMK
IWLDVLSSHT TH
