PHR_DICDI
ID PHR_DICDI Reviewed; 1019 AA.
AC Q1ZXQ0;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Sca1 complex protein phr {ECO:0000303|PubMed:20493808};
DE AltName: Full=Pleckstrin homology domain-containing protein {ECO:0000303|PubMed:20493808};
GN Name=phr {ECO:0000303|PubMed:20493808}; ORFNames=DDB_G0270932;
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 IN THE SCA1 COMPLEX, INTERACTION WITH GEFH, FUNCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20493808; DOI=10.1016/j.devcel.2010.03.017;
RA Charest P.G., Shen Z., Lakoduk A., Sasaki A.T., Briggs S.P., Firtel R.A.;
RT "A Ras signaling complex controls the RasC-TORC2 pathway and directed cell
RT migration.";
RL Dev. Cell 18:737-749(2010).
CC -!- FUNCTION: Component of the Sca1 complex, a regulator of cell motility,
CC chemotaxis and signal relay (PubMed:20493808). The Sca1 complex is
CC recruited to the plasma membrane in a chemoattractant- and F-actin-
CC dependent manner and is enriched at the leading edge of chemotaxing
CC cells where it regulates F-actin dynamics and signal relay by
CC controlling the activation of rasC and the downstream target of
CC rapamycin complex 2 (TORC2)-Akt/protein kinase B (PKB) pathway
CC (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
CC -!- SUBUNIT: Component of the Sca1 complex composed of at least gefA, gefH,
CC scaA, phr, and the protein phosphatase 2A subunits pppA and pho2B
CC (PubMed:20493808). Interacts directly with gefH (PubMed:20493808).
CC {ECO:0000269|PubMed:20493808}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20493808}.
CC Note=The Sca1 complex is recruited to the plasma membrane in a
CC chemoattractant- and F-actin-dependent manner and is enriched at the
CC leading edge of chemotaxing cells (PubMed:20493808). Membrane
CC localization of the Sca1 complex is regulated by scaA phosphorylation
CC by PKB and PKB-related PKBR1 (PubMed:20493808).
CC {ECO:0000269|PubMed:20493808}.
CC -!- DISRUPTION PHENOTYPE: Display directionality defects during chemotaxis
CC and increased motility (PubMed:20493808).
CC {ECO:0000269|PubMed:20493808}.
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DR EMBL; AAFI02000005; EAS66938.1; -; Genomic_DNA.
DR RefSeq; XP_001134474.1; XM_001134474.1.
DR AlphaFoldDB; Q1ZXQ0; -.
DR STRING; 44689.DDB0233269; -.
DR PaxDb; Q1ZXQ0; -.
DR EnsemblProtists; EAS66938; EAS66938; DDB_G0270932.
DR GeneID; 8617180; -.
DR KEGG; ddi:DDB_G0270932; -.
DR dictyBase; DDB_G0270932; phr.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_296377_0_0_1; -.
DR InParanoid; Q1ZXQ0; -.
DR OMA; QGFIFVY; -.
DR Reactome; R-DDI-1169092; Activation of RAS in B cells.
DR Reactome; R-DDI-171007; p38MAPK events.
DR Reactome; R-DDI-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-DDI-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-DDI-9648002; RAS processing.
DR PRO; PR:Q1ZXQ0; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1905742; C:Ras guanyl-nucleotide exchange factor complex; IDA:dictyBase.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00071; Ras; 2.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; GTP-binding; Membrane; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1019
FT /note="Sca1 complex protein phr"
FT /id="PRO_0000438889"
FT DOMAIN 735..836
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 89..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 158..188
FT /evidence="ECO:0000255"
FT COMPBIAS 139..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 111583 MW; 25C167494A955873 CRC64;
MLLLNYTQNF QLITFLLFPF INTFDYNCLK PTTTTTTSPT SSKLGFLNRS KSNSNININE
LKNKFLEQQQ EGSISNIAGV ATTQQNPSIV INSSSSSSSS SSHHPHHQKT PSNSSSNFNL
IKASFNQIGV AFNNNISPRS NRKEKEKDKD KDHQDNSNIN NINNINNNIN NNINNNNNNN
NNNNNNNNMH NPTSSSPSIN NNLKGKNVAS IIAANGANLN NSLSNLHQHV NNNSNNNLTN
SFNSVSHNNI SISSGGSALS YNYTQQLNQN GGSNNGSTSN STSNSANNSL LSLASSINGN
IGSDENGSNV MYGGDIASSY HSMSIDPLKS STNTETIEIM VVGDELSNKA RFISSFLNNG
IGEDPTLEIS TKKSIAIQSG AYNVNINTTV GQEEFWGIND VYYRSSQGFI FVYNVNSRES
FLSFLKFRDK IIHEKGTENI LMAMVGLTSP LINQESGEES CIREVTQQEA KRMADLYSCS
FVELNSFGLD CEHQIQSIVT DLLGRITSGL SSTNNNNSGN NSNNNNGNSN GNSSNNNSNN
NSTNNLNNSA ILNESIAQSI EVLMLGDIFV GKTQIIQRLL GNPFQNAYKE TTEWNRNVYQ
MTVNDVRYLL KIVDTCGLDI EETLNRERLV STQGFIFVYS IASRESFLMI EQLRKKLSSI
KSETKIPSVL IANKGDSLIR QVTFDEGSKM AQHLGSHYFE VSSMFSDDES IGRPFEQLLI
DIQKSGNASG FEPSEIKKKG YLFKEGKKLK SMSKYFFKAS RGNLSYCKNE SNKSKVKSIQ
LSEQIQLAIP HNVHEKKDVW PFSIILDPVS KHSINLIAST EEERNAWIKA IKFNCFLEDI
TSNIIDDVVK SMVSEIASGV AGSGSNNGNN NGHLKRSDTT QQLNNSGSFI NGINANKPVP
NFSNLSISGG GSSNNSNNST PMSSPYGSSN NFSSHLSQST SSMSMSPQQQ LQSVLLSSSN
LSSSMNSSFS YSSSISSSYT DSMSGSPPDS NGQVFPQSPQ LKKTLFQRTT SFSKGSKLK
