GACII_DICDI
ID GACII_DICDI Reviewed; 817 AA.
AC Q54YV1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Rho GTPase-activating protein gacII;
DE AltName: Full=GTPase activating factor for raC protein II;
GN Name=gacII; ORFNames=DDB_G0278069;
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].
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).
CC -!- FUNCTION: Rho GTPase-activating protein involved in the signal
CC transduction pathway. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; AAFI02000023; EAL68207.1; -; Genomic_DNA.
DR RefSeq; XP_642101.1; XM_637009.1.
DR AlphaFoldDB; Q54YV1; -.
DR SMR; Q54YV1; -.
DR STRING; 44689.DDB0233794; -.
DR PaxDb; Q54YV1; -.
DR EnsemblProtists; EAL68207; EAL68207; DDB_G0278069.
DR GeneID; 8621312; -.
DR KEGG; ddi:DDB_G0278069; -.
DR dictyBase; DDB_G0278069; gacII.
DR eggNOG; KOG4270; Eukaryota.
DR HOGENOM; CLU_345958_0_0_1; -.
DR InParanoid; Q54YV1; -.
DR PRO; PR:Q54YV1; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0022607; P:cellular component assembly; IEA:UniProt.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTPase activation; Reference proteome; SH3 domain.
FT CHAIN 1..817
FT /note="Rho GTPase-activating protein gacII"
FT /id="PRO_0000380206"
FT DOMAIN 20..204
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 238..298
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 318..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 89956 MW; AB66ED1F04FCD06C CRC64;
MVRKLFNTSH KKELILDVDT TIVKIGTPKN VVLLTKWLDA NGAIKEEGVF RVNGNTTTME
QIKKNFSQGK DDLTKYTSAD IHSMAGCLKF ILRELPEPIF TWDFYPIFIK IQCLQDESRK
LFFLKMLIHG LPYTSRTLVF QLFGFLSKFS VHQDQNKMTP KNLATVFAPN VLRPKKEEDN
FQLMNNQDSI GVIETLIEEF QYISNIQKNT LNSQEIKVKS VLPFDETTNA ITQQSLVEDY
LIAKANTPQE SSSFKKNLPF KKGDIIKLLY IKNDGNFIGE INGITGNLSQ TYVDIIDISE
LAEAFTLTPP PIPTLPIAST ILHTPPTSSS SSSSSSSSSI LLTDNQPKLC SSTPRINNSP
SSFSPSLSST TPQLLVQQSP RQSPRQIPSI SLIVEPNNTN QPSFGHGTLQ RTSTGYFSSK
PLSISQPINM SKPTNMSPPT HHAMSMHNLP PSNTTRENHL PPLPTKPPPL TIPSSSSLPT
TPIKQQPQQP IQQPLTPQNH HHHHHHNNLS SSVNTANTGN CANILSPNSD RYLSSRSQSS
VHLSGSSSSS SSSSSSSSSS SSSSSSTSNR KFDFSLKSKS SKNSPSKNLP PQPTTTSTLT
PPPPPTITTT TTTTTTTTTT TIATTPPPPS KPLPNIPVKD QQFNTLKRST IEIPPPTITS
TNINNNNNTI NPRTLNYSFS SFSITYNNSQ LGGQLSQEEP PGGVKSQSSY LDNNNLPSRN
TNIPNLPPRP PPLNIPQQQQ QYKPLPSPPQ LQSPQSSLNQ SLQIPLQQQQ QVQQQKLTTH
YILPPQNTNL SGKNLQRSST SMLLNKLPPP PFSFNKN
