CRAC_DICDI
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 03-AUG-2022, entry version 106.
DE RecName: Full=Protein CRAC;
GN Name=dagA; ORFNames=DDB_G0285161;
OS Dictyostelium discoideum (Slime mold).
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}.
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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 STRING; 44689.DDB0191434; -.
DR PaxDb; P35401; -.
DR EnsemblProtists; EAL64837; EAL64837; DDB_G0285161.
DR GeneID; 8624989; -.
DR KEGG; ddi:DDB_G0285161; -.
DR dictyBase; DDB_G0285161; dagA.
DR eggNOG; ENOG502R7J7; Eukaryota.
DR HOGENOM; CLU_395077_0_0_1; -.
DR InParanoid; P35401; -.
DR OMA; LAMIRCE; -.
DR PRO; PR:P35401; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:dictyBase.
DR GO; GO:0031256; C:leading edge membrane; IDA:dictyBase.
DR GO; GO:0070685; C:macropinocytic cup; 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: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:1903669; P:positive regulation of chemorepellent activity; IMP: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: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; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 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 595..630
FT /note="Polar residues"
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
