MGP4_DICDI
ID MGP4_DICDI Reviewed; 909 AA.
AC Q54QF4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=GTPase activating protein homolog 4;
DE AltName: Full=GTPase activating factor for raC protein DD;
DE AltName: Full=Rho GTPase-activating protein gacDD;
GN Name=mgp4; Synonyms=gacDD; ORFNames=DDB_G0283899;
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).
RN [2]
RP IDENTIFICATION.
RX PubMed=18334553; DOI=10.1242/jcs.021113;
RA Heath R.J., Insall R.H.;
RT "Dictyostelium MEGAPs: F-BAR domain proteins that regulate motility and
RT membrane tubulation in contractile vacuoles.";
RL J. Cell Sci. 121:1054-1064(2008).
CC -!- FUNCTION: Rho GTPase-activating protein involved in the signal
CC transduction pathway. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Contractile vacuole {ECO:0000250}.
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DR EMBL; AAFI02000057; EAL65564.1; -; Genomic_DNA.
DR RefSeq; XP_638917.1; XM_633825.1.
DR AlphaFoldDB; Q54QF4; -.
DR SMR; Q54QF4; -.
DR STRING; 44689.DDB0233871; -.
DR PaxDb; Q54QF4; -.
DR EnsemblProtists; EAL65564; EAL65564; DDB_G0283899.
DR GeneID; 8624314; -.
DR KEGG; ddi:DDB_G0283899; -.
DR dictyBase; DDB_G0283899; mgp4.
DR eggNOG; ENOG502RSTN; Eukaryota.
DR HOGENOM; CLU_319697_0_0_1; -.
DR InParanoid; Q54QF4; -.
DR OMA; EIMFKQK; -.
DR PhylomeDB; Q54QF4; -.
DR PRO; PR:Q54QF4; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0000331; C:contractile vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; GTPase activation; Reference proteome; Vacuole.
FT CHAIN 1..909
FT /note="GTPase activating protein homolog 4"
FT /id="PRO_0000380227"
FT DOMAIN 1..257
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 322..513
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 529..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 672..809
FT /evidence="ECO:0000255"
FT COMPBIAS 529..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..624
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 101591 MW; A69271C9BF4F255E CRC64;
MASLIGSAKL PFNNEVELIS DEIEKGLNDS TTIRKFFEKR AQIEEEYAKN LQKLCKATPI
LLKSGGTSDA FSMIVESTNQ FSNHTISTIQ RFNQDVNDPL AGFIKDLRGE LKQYSLEGQN
LAKERKQAFD SLKSSKALYE QMCNNPESDV MKVQQSEEEY KLQVQACNQY HSLYHQEKLP
KIQNEIIRLE TVRMQKMKTN LKKYITEFES IPQKQQQSIK DSEELINSID TKQDIQSFTN
FNKTLNTPTP DFQFESCESI NGGGGGAAGR KSKKGGWRQT ISVLKIGNAF MKDDGTIVNG
NSSLNSSSSN INILNNPIVF KIPIEEIMFK QKSKFPNLDI PYILVLLVNL IKKLDNGMGM
KTEGIFRIPG HTSEVNALKK LINEQGEYQF PPDLYSIHPI ASLLKLWLRE MPQPLIPNYV
YDKSLECQSI EEFIVFFKFL PASNQKIITY LAGFLNELVQ PDNVVTSKMN LDNVAMVFAP
SFLRCDSQDM ILANVDREKT LVKLIIEGYL KLSDVCPIQL DDIDSKIQIP SFSNNNNNST
TTTTTTTTTT VPSSTSTNIT TNGASALGAE SSTTPLPSLT TFSQSQSSSP PNQPSPSITP
QQVSNLPPSY QPPQPPPTMA PPPLFNIPQQ QQQQQVTNNN NSGGYTPPPL QYTQSSSNLP
PIQLGVTNSP SKPQLSDKQK EKEKEKEKEK EKEKEREKEK EKEKEKEKEK EKEKEKKGHK
KSSSSTSPNS SSLSISNFLS SNKDKDKEKD KEKEKEKEKE KDKEILATNS TPEKPVSNRM
SLIFSQQLQQ QLQQQIQQHQ QLQQQSNGSP TSPISPSSAN NSPSMSPSMV KRTIRPNLPP
LQSGTSATTS SSSLTSSSSP TLTSSKDNIQ KQQLPELNQQ QQQQSPQAEL KSSGIKSLLQ
RVPPPPSQS
