ID CRAC_DICDI Reviewed; 698 AA. AC P35401; Q54NJ7; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 4. DT 04-NOV-2026, entry version 118. DE RecName: Full=Protein CRAC; GN Name=dagA; ORFNames=DDB_G0285161; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=8089184; DOI=10.1083/jcb.126.6.1537; RA Insall R., Kupsa A., Lilly P.J., Shaulsky G., Levin L.R., Loomis W.F., RA Devreotes P.N.; RT "CRAC, a cytosolic protein containing a pleckstrin homology domain, is RT required for receptor and G protein-mediated activation of adenylyl cyclase RT in Dictyostelium."; RL J. Cell Biol. 126:1537-1545(1994). 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 PROTEIN SEQUENCE OF 2-9. RX PubMed=8188693; DOI=10.1016/s0021-9258(17)36763-7; RA Lilly P.J., Devreotes P.N.; RT "Identification of CRAC, a cytosolic regulator required for guanine RT nucleotide stimulation of adenylyl cyclase in Dictyostelium."; RL J. Biol. Chem. 269:14123-14129(1994). RN [4] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=9389653; DOI=10.1101/gad.11.23.3218; RA Chen M.-Y., Long Y., Devreotes P.N.; RT "A novel cytosolic regulator, Pianissimo, is required for chemoattractant RT receptor and G protein-mediated activation of the 12 transmembrane domain RT adenylyl cyclase in Dictyostelium."; RL Genes Dev. 11:3218-3231(1997). CC -!- FUNCTION: Couples activated G protein to adenylyl cyclase signal CC transduction from surface cAMP receptor. Pianissimo a cytosolic CC regulator and CRAC, are both essential for activation of the enzyme CC adenylyl cyclase. Pianissimo and CRAC do not function redundantly. Both CC proteins are integral components of the adenylyl cyclase activation CC pathway. {ECO:0000269|PubMed:9389653}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DEVELOPMENTAL STAGE: Tightly developmentally regulated. CC -!- DISRUPTION PHENOTYPE: dagA and piaA double mutants require both CC proteins for reconstitution and activation of adenylyl cyclase. CC {ECO:0000269|PubMed:9389653}. 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; U06228; AAA61782.1; -; Genomic_DNA. DR EMBL; AAFI02000075; EAL64837.1; -; Genomic_DNA. DR PIR; A54796; A54796. DR RefSeq; XP_638365.1; XM_633273.1. DR AlphaFoldDB; P35401; -. DR SMR; P35401; -. DR FunCoup; P35401; 448. DR STRING; 44689.P35401; -. DR PaxDb; 44689-P35401; -. DR GeneID; 8624989; -. DR KEGG; ddi:DDB_G0285161; -. DR dictyBase; DDB_G0285161; dagA. DR VEuPathDB; AmoebaDB:DDB_G0285161; -. DR eggNOG; ENOG502R7J7; Eukaryota. DR HOGENOM; CLU_395077_0_0_1; -. DR InParanoid; P35401; -. DR OMA; AHKHRIY; -. DR PRO; PR:P35401; -. DR Proteomes; UP000002195; Chromosome 4. DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:dictyBase. DR GO; GO:0005829; C:cytosol; IDA:dictyBase. DR GO; GO:0031256; C:leading edge membrane; IDA:dictyBase. DR GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase. DR GO; GO:0016020; C:membrane; IDA:dictyBase. DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase. DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase. DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase. DR GO; GO:0008047; F:enzyme activator activity; IMP:dictyBase. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:dictyBase. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IMP:dictyBase. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0019887; F:protein kinase regulator activity; IMP:dictyBase. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:dictyBase. DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase. DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase. DR GO; GO:0000165; P:MAPK cascade; IMP:dictyBase. DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:dictyBase. DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IMP:dictyBase. DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:dictyBase. DR GO; GO:0046688; P:response to copper ion; HDA:dictyBase. DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase. DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; TAS:dictyBase. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR051707; PI-Interact_SigTrans_Reg. DR PANTHER; PTHR14336:SF19; PROTEIN CRAC; 1. DR PANTHER; PTHR14336; TANDEM PH DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 1: Evidence at protein level; KW Cytoplasm; Developmental protein; Direct protein sequencing; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8188693" FT CHAIN 2..698 FT /note="Protein CRAC" FT /id="PRO_0000079325" FT DOMAIN 22..122 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 594..630 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 601..626 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 653 FT /note="R -> G (in Ref. 1; AAA61782)" FT /evidence="ECO:0000305" SQ SEQUENCE 698 AA; 78630 MW; 3CC3D8FF6D9D849B CRC64; MGKTERKKEL LELFEYEKIK GDVSYSSIMK KAGGNGKGFL DRYFALHRNY ILYYKLGKSS LKPDDKQEPQ GYINLMDCNP DDTKEIAPLM FQISHKHRTY IVKAKDESSM KQFLTLLIAR IRSLEKIDID KLGCTVVVLT KVKKFREVLT NPLILPDRVS PEMAEEWVKQ MKNYNASFNL ADPFIKQVEQ ISEFCRGEVK EYIDWFGGPE GPRLAMIRCE ETVLSNWVEY INKTSSEITT YQDNRFFRED FKDIAVHLKN MTTFIDCYND YMIHCRKYNN NKPNTKFLEE KQTFKEYIEK FIPKVASCND VSLNQFYDRS LIQSSDGIVT INTSGIKKTL INQSNIISIT STTTTTTTTT TTTCSMPNMS NLIHSLDHTN LNIIDLNHSK SQQQLHPPPS PHHQHLHHQI VSNSKDFNIS VSSNNFNDGN SEFPNLDINC DFDLTSASNL SSPILSSEVP SNVVDPIGSG QGGGGSGGGG VTAVTEEAIN EKWHFDCNTS MIFKPPSEDG RNEGSNMSTS SITSKMSLSL NGGFDMKWVY QCGYFKSKNM GSISWNGKHW CWSHPRTSYK IKYIWDPTKQ SFLNIPFKSR VGATGGGSVP SSQSTNNLQS STSSMSSLSS SSTSTTKRSH PTTLYPDYQF KDNLLTPIII EGRHQPSLTL IDSPLTIPNA CLLTIAMTQY IQDALIHLSL GPKVLSSK //