RIP3_DICDI
ID RIP3_DICDI Reviewed; 838 AA.
AC Q9Y0C9; Q54P98;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ras-interacting protein RIP3;
DE AltName: Full=Ras-interacting protein A;
GN Name=ripA; Synonyms=rip3; ORFNames=DDB_G0284611;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RASG, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10473630; DOI=10.1091/mbc.10.9.2829;
RA Lee S., Parent C.A., Insall R., Firtel R.A.;
RT "A novel Ras-interacting protein required for chemotaxis and cyclic
RT adenosine monophosphate signal relay in Dictyostelium.";
RL Mol. Biol. Cell 10:2829-2845(1999).
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, IDENTIFICATION IN A TORC2 COMPLEX, DISRUPTION PHENOTYPE,
RP MUTAGENESIS OF LYS-680 AND ARG-681, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND INTERACTION WITH RASG.
RX PubMed=16079174; DOI=10.1091/mbc.e05-04-0342;
RA Lee S., Comer F.I., Sasaki A., McLeod I.X., Duong Y., Okumura K.,
RA Yates J.R. III, Parent C.A., Firtel R.A.;
RT "TOR complex 2 integrates cell movement during chemotaxis and signal relay
RT in Dictyostelium.";
RL Mol. Biol. Cell 16:4572-4583(2005).
CC -!- FUNCTION: Component of a Ras-regulated pathway involved in integrating
CC chemotaxis and signal relay pathways that are essential for
CC aggregation. {ECO:0000269|PubMed:10473630,
CC ECO:0000269|PubMed:16079174}.
CC -!- SUBUNIT: Interacts with activated RasG. Part of a complex, TORC2,
CC consisting of tor, lst8, piaA and ripA. Additional proteins, such as
CC 14-3-3 and heat-shock proteins, may also belong to the TORC2 complex.
CC {ECO:0000269|PubMed:10473630, ECO:0000269|PubMed:16079174}.
CC -!- DISRUPTION PHENOTYPE: Null cells have serious developmental defects,
CC because they are unable to activate the aggregation-stage adenylyl
CC cyclase acaA in response to chemoattractant and are defective in
CC chemotaxis. Cells are unable to properly polarize in a cAMP gradient.
CC {ECO:0000269|PubMed:10473630, ECO:0000269|PubMed:16079174}.
CC -!- SIMILARITY: Belongs to the SIN1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF159241; AAD43567.1; -; mRNA.
DR EMBL; AAFI02000070; EAL65075.1; -; Genomic_DNA.
DR RefSeq; XP_638477.1; XM_633385.1.
DR AlphaFoldDB; Q9Y0C9; -.
DR SMR; Q9Y0C9; -.
DR STRING; 44689.DDB0304430; -.
DR PaxDb; Q9Y0C9; -.
DR PRIDE; Q9Y0C9; -.
DR EnsemblProtists; EAL65075; EAL65075; DDB_G0284611.
DR GeneID; 8624728; -.
DR KEGG; ddi:DDB_G0284611; -.
DR eggNOG; ENOG502RFE8; Eukaryota.
DR InParanoid; Q9Y0C9; -.
DR OMA; IINARQT; -.
DR Reactome; R-DDI-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DDI-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-DDI-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DDI-6804757; Regulation of TP53 Degradation.
DR PRO; PR:Q9Y0C9; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IDA:dictyBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IMP:dictyBase.
DR GO; GO:0019887; F:protein kinase regulator activity; IDA:dictyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:dictyBase.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IMP:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IMP:dictyBase.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:dictyBase.
DR GO; GO:1904515; P:positive regulation of TORC2 signaling; IGI:dictyBase.
DR GO; GO:0043520; P:regulation of myosin II filament assembly; IMP:dictyBase.
DR GO; GO:0051602; P:response to electrical stimulus; IMP:dictyBase.
DR GO; GO:0038203; P:TORC2 signaling; IDA:dictyBase.
DR InterPro; IPR031567; CRIM_dom.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR008828; Sin1/Avo1.
DR PANTHER; PTHR13335; PTHR13335; 2.
DR Pfam; PF16978; CRIM; 1.
DR Pfam; PF02196; RBD; 1.
PE 1: Evidence at protein level;
KW Chemotaxis; Reference proteome.
FT CHAIN 1..838
FT /note="Ras-interacting protein RIP3"
FT /id="PRO_0000328037"
FT DOMAIN 648..717
FT /note="RBD"
FT REGION 66..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 680
FT /note="K->E: Loss of interaction with rasG-GTP; when
FT associated with arg-681."
FT /evidence="ECO:0000269|PubMed:16079174"
FT MUTAGEN 681
FT /note="R->E: Loss of interaction with rasG-GTP; when
FT associated with Lys-680."
FT /evidence="ECO:0000269|PubMed:16079174"
SQ SEQUENCE 838 AA; 94059 MW; EAAD911294226808 CRC64;
MSVYCELVDV VQQIRYKTQI FYETFKRDSI AEQIYNFSNE STSEIDPDIP FSKSLDKDYS
LLYRPVSTSN NNATSGNSTP PNNAISPNQQ QQQQQQAQQQ QQQQQQQQQQ QQHQQQQQQQ
QQQQQQQQQQ QQQQQAQQQQ QQAQQQAQVQ AQQQQQKPTT ATTASTVTTT PQQQPSPNNT
TSSCTSSSSG SSSGTTNTTS NTTTSTNTST VTSATNSSTI SSLTSTNAST SSAYSTDQQK
PNQPPQQPQN ISQPQNISQQ QNTNNVQQNN QQQQQQQQQQ QQQQTSTSPK KCKIVTFTGT
SVKLNSKTLQ KSDKTSEKEN KQQQPDSSKT QQQQQAQQQQ SQQQQQAQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQQQQPV FIFVKEKVNK VNHDLPITPP PSLLTRLVKP NSEEAEYGDI
VPPPGMGLTL SIHTGNTGAG QLKVRVIEKA TIIQTIFATL KLHHNNGGTG LIPDPKAYNL
RIADSNGRID QDFPPLDPNQ YITKFKDEVL VLCPNPKFDL KKSSSSLSIS GGVPQQNNNN
SVNSNSSNNS NSSNNNMKSS GFQPQQSQQQ QQQTQQTQQT QQQAQQAPQQ QQSQQQQQQQ
QQHPQQIQQQ LSSNQLQPDQ VGGGGGGGGG NFHRTHHRNV SSGPDAPLVV KITLPDSSIT
KVVFQKTMLL KDLLESTCKK RKLLISDHYF TLENGQTCNG TLPMEKLGGA DLILVSRRPI
EQMTALSPTD TDSTGSSSDL QQDIFWYDAL AWQYKTYEVT KTKKYGPKQD RIIGIDRERV
TNMSPKDTET KRPARLIKDI SKVALLEKPK YFTIEYNDGK SYIYEAKTTS LANNYLCK
