GBPD_DICDI
ID GBPD_DICDI Reviewed; 1312 AA.
AC Q54S40; Q8MVR0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cyclic GMP-binding protein D;
DE AltName: Full=Guanine nucleotide exchange factor for rap1;
DE AltName: Full=Ras guanine nucleotide exchange factor U;
DE AltName: Full=RasGEF domain-containing protein U;
GN Name=gbpD; Synonyms=gefU, rapgef; ORFNames=DDB_G0282373;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RX PubMed=12011437; DOI=10.1073/pnas.102167299;
RA Goldberg J.M., Bosgraaf L., Van Haastert P.J.M., Smith J.L.;
RT "Identification of four candidate cGMP targets in Dictyostelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6749-6754(2002).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=12198158; DOI=10.1093/emboj/cdf438;
RA Bosgraaf L., Russcher H., Smith J.L., Wessels D., Soll D.R.,
RA Van Haastert P.J.M.;
RT "A novel cGMP signalling pathway mediating myosin phosphorylation and
RT chemotaxis in Dictyostelium.";
RL EMBO J. 21:4560-4570(2002).
RN [4]
RP DEVELOPMENTAL STAGE.
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 [5]
RP FUNCTION.
RX PubMed=15827084; DOI=10.1242/jcs.02317;
RA Bosgraaf L., Waijer A., Engel R., Visser A.J.W.G., Wessels D., Soll D.,
RA van Haastert P.J.M.;
RT "RasGEF-containing proteins GbpC and GbpD have differential effects on cell
RT polarity and chemotaxis in Dictyostelium.";
RL J. Cell Sci. 118:1899-1910(2005).
CC -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP (By
CC similarity). Induces the formation of substrate-attached pseudopodia,
CC that leads to increased adhesion and thereby negatively influencing
CC cell speed and polarity. {ECO:0000250, ECO:0000269|PubMed:12198158,
CC ECO:0000269|PubMed:15827084}.
CC -!- DEVELOPMENTAL STAGE: Increases after starvation is initiated with a
CC peak between 8-12 hours of starvation. {ECO:0000269|PubMed:12011437,
CC ECO:0000269|PubMed:16086850}.
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DR EMBL; AF481924; AAM34042.1; -; Genomic_DNA.
DR EMBL; AAFI02000047; EAL66046.1; -; Genomic_DNA.
DR RefSeq; XP_640199.1; XM_635107.1.
DR AlphaFoldDB; Q54S40; -.
DR STRING; 44689.DDB0215332; -.
DR PaxDb; Q54S40; -.
DR EnsemblProtists; EAL66046; EAL66046; DDB_G0282373.
DR GeneID; 8623739; -.
DR KEGG; ddi:DDB_G0282373; -.
DR dictyBase; DDB_G0282373; gbpD.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_260634_0_0_1; -.
DR InParanoid; Q54S40; -.
DR OMA; WFNRISS; -.
DR PRO; PR:Q54S40; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:dictyBase.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0032060; P:bleb assembly; IGI:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0019934; P:cGMP-mediated signaling; IGI:dictyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:dictyBase.
DR GO; GO:0031271; P:lateral pseudopodium assembly; IMP:dictyBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:dictyBase.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 2: Evidence at transcript level;
KW cGMP; cGMP-binding; Guanine-nucleotide releasing factor;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1312
FT /note="Cyclic GMP-binding protein D"
FT /id="PRO_0000353104"
FT DOMAIN 26..155
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 353..582
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 940..1006
FT /note="GRAM"
FT REGION 206..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 698..857
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 1105..1218
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT BINDING 1182..1303
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="3"
FT CONFLICT 621
FT /note="G -> A (in Ref. 1; AAM34042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1312 AA; 143659 MW; 044A4E51DBA2192E CRC64;
MTDYPFYKPD DETNIIYNIN INKKEGFSAI KSCSLAKLIE KLTSTKQLHT YFSSAFFLTY
RDFTTPLEII NLLISRYTGP PPDSSKDSLR LFEIEVDIVQ ANVLSIFRTL IGTLIQVDFD
TPKLSSSIIE FFNSLPESVK NELFLEFFKA KKMARPPGSI PKPVNSNIIS SAASTMRFSY
SVSPKTQSPN STNNVLSGLL SNNGSNTMNG INGTSNNNVN SNNNNNNGTT NISSPNFDPS
RSSMKMGKGI MKLLQSNIAN FNNQQNGGGG GGSNNGTSPQ SSPSSTLSST NSLFNQQPSL
SMLNDDGSVQ NNNNNNNNNN NNNNVNEIST INVQLPPSTP PINGIPGEKT AFLPEAIAKE
LTIMEWELIT ALSVSDITSK EWNKSVNIQN LTTWFNRISS WVSTKIISKE TPEERAIIIE
AFINIANFAK ELKNYNCVME ILGSLHGSSI SRLKSSWALL SQKTNDMFQI LNNLMTTDGN
FKNYRKILTT VLPNEPCIPY LGLFLTDYTY LDESNPSLST DSNLINIDRI FLISTRVQEF
FQLFTNCNYT FISNMSVRDA ILGEKVWDEN EIFRLSKIRE ETSSLQSLKE SNGIGNSNST
SGGSSSSLVN KDGSGGGGGS GGGGSVNSKG DGKGDGKDNR DGRGDGNSNC GNGSGISSKD
KDLLLSSSSS AASHTVRRKN FVTKYRMSFT GNDPLPSVSS TLSEREWKIL TTNSKTIIYP
RGKTVLSVGE TNTNIYRVIS GRVKVETLKS FNSSDADLGA GGGGGGDNRG EDNSLMAIKA
RNRLSLNLPA QDDGYYVEEG EIFGQESFLY TDRPMLSNII VDSGECELME IEKSFVLQLF
ASEHQLSATF YKFIGVIQAQ LLKSIYINFT SNYGNGGSGG SGSNGNGGGS SNGAGGGGLS
SSVSIGNLNS PNINRIDFKR RSTIFETPSS LDILRDGNDS SFRTKFGLSQ DEVIIKRYQC
KHNNMNGTLY ITKHNLCFEG KFLGINKNKT IPFDRTDKIL TVDKNIMTVT TKEKVKKFTF
KSHDDLNEGY GISVQIWANH LNINVKQQLQ LQQQQLQQQQ QQPSQQPSQQ QSQSSQLQQS
VSASSTTPPV PNSPKVGRGE SFSNIKDLPS KDEWNQILKG TKPLTFKKGE ILICEGVEYQ
KMFQIVKGEC SVVKSLLPTP LDQNIFNNIN NNNNNNNNNN NNNNNNNNNN NNNNNNGNNN
NSIFKNNSSI SNTNSNTSID GGVGGGLSPQ TLVDPKNSVI VSKLTHGSIF GEMSFLLPGG
SATSLVVSSD EVEVYIIESY FLHILLKSKP YLASKFYKYL ACVLETRVRN LT
