RGAP1_DICDI
ID RGAP1_DICDI Reviewed; 1055 AA.
AC Q75J96; Q55AJ8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=RapA guanosine triphosphatase-activating protein 1;
GN Name=rapgap1; ORFNames=DDB_G0271734;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(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, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18039932; DOI=10.1083/jcb.200705068;
RA Jeon T.J., Lee D.-J., Lee S., Weeks G., Firtel R.A.;
RT "Regulation of Rap1 activity by RapGAP1 controls cell adhesion at the front
RT of chemotaxing cells.";
RL J. Cell Biol. 179:833-843(2007).
CC -!- FUNCTION: Mediates the deactivation of rap1 and plays an important role
CC in spatially and temporally regulating cell adhesion and chemotaxis by
CC controlling attachment disassembly in the leading edge through the
CC regulation of myosin II assembly and disassembly. Overexpression leads
CC to defective chemotaxis. {ECO:0000269|PubMed:18039932}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18039932}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:18039932}. Note=Translocates
CC to the cell cortex in response to chemoattractant stimulation and
CC localizes to the leading edge of chemotaxing cells via an F-actin-
CC dependent pathway. Cortical localization is negatively regulated by
CC ctx.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of development.
CC {ECO:0000269|PubMed:18039932}.
CC -!- DISRUPTION PHENOTYPE: Null cells show defects in spatial regulation of
CC the cell attachment at the leading edge. They also have extended
CC chemoattractant-mediated rap1 activation kinetics and decreased myosin
CC II assembly. {ECO:0000269|PubMed:18039932}.
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DR EMBL; AAFI02000006; EAL71557.1; -; Genomic_DNA.
DR RefSeq; XP_645524.1; XM_640432.1.
DR AlphaFoldDB; Q75J96; -.
DR SMR; Q75J96; -.
DR STRING; 44689.DDB0233726; -.
DR PaxDb; Q75J96; -.
DR EnsemblProtists; EAL71557; EAL71557; DDB_G0271734.
DR GeneID; 8618153; -.
DR KEGG; ddi:DDB_G0271734; -.
DR dictyBase; DDB_G0271734; rapgap1.
DR eggNOG; KOG3686; Eukaryota.
DR HOGENOM; CLU_290263_0_0_1; -.
DR InParanoid; Q75J96; -.
DR OMA; VMESTRI; -.
DR Reactome; R-DDI-392517; Rap1 signalling.
DR PRO; PR:Q75J96; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005096; F:GTPase activator activity; IDA:dictyBase.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:dictyBase.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEP:dictyBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:dictyBase.
DR GO; GO:0043520; P:regulation of myosin II filament assembly; IMP:dictyBase.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR Pfam; PF02145; Rap_GAP; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..1055
FT /note="RapA guanosine triphosphatase-activating protein 1"
FT /id="PRO_0000368229"
FT DOMAIN 779..1048
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 76..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1055 AA; 118502 MW; 68B98F8ACE42CF9D CRC64;
MSIYHGIIGS SDHIQNIFPP PSPRKNISLS TNNISSLTTP KNFTAIVVTK PLSQSTTSTQ
EMMNTSDILF DIQQPLSPQH HSRQIQQQQH EKITPEEEER RSDELQKILL DTIPILIKGV
ETLGIEVEQI CNGDSANEKR SNCQVLVDIQ KTLREYPRGM GYRSKTIPSN IVGKPKLIAF
RHSMDQLVWE NISKLSILKD FVEFTLDFQK LCVIGISIRD AINSFVNNKC EYLIKGFEFN
NTNSILSGIN IHHHLNHQPG ASTPRPSHSS SSSLSHSLSS SPMSQSLPSS LTSGGVSLLN
TSDDAIVPSL SSGNDDSSGS SLSSSDANVI SINISTVIQN GVRDEINNTS ISALKKSQKQ
QPVVLSRAPK QVMESTRILV DTVVNRKCMY REEKASIYRE MMNDRLTLLK EDPKKFKQQL
LQQRRQKLTN SDQPHETDYN EDFNLNNNST NNNNNIKKES NGSSVNSQTT TTTTTTNNNN
NNISPQHSGT SGSPSDKENS PIFSPGYLST SPPKSPPKSP EFLGVPIGKK AHLLGHARSF
SADTHATKEA AANQHHHSHN NIGSVLSPPL SSQNERILRN YKLLSSSPSS SSSAVVTNPV
SLTTQLQQQQ QQQQQQQTTS QPTQPPPSEY QLLDLEWEEP IDSDFILPCK GYKIDSGNSK
CQQVNYDELI VLYTDEDEYH YCDDFCSLEH FNFLGVNKNQ PDNPMCISVV VQHDTNELLY
IIRTGEKDEK YRLSLPYGKK EISSKDMLKM IKKSRFNQMS NFKLKEVKSD QNQQFIKQLI
QFEAKNIHKT FKFGVLYCSE NQGTDENELY SNSSTSDEFQ EFLRILGDRV QLQGWTKYRG
GLDIKDNTTG THSIYKKWRD FEIMYHVAPM IPCRAADEQS VERKRHLGND IVLIIYKEGN
TKLFDPSIIK SNFNHIFAVV QKVDPIPNVD GAAVINLGNS FNNNNSSNNN NNNNNNNNNN
NNSDSNLPTT NNLPIITNVN YKISIGCKEE VQNFGPAFPK NHIFSTSTGE NLTDFLLTRL
INGERATLKS PVFAQKLKRT RKEFLHSFIT DFGSE
