CAR1_DICDI
ID CAR1_DICDI Reviewed; 392 AA.
AC P13773; Q557I7;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cyclic AMP receptor 1;
DE Short=cAMP receptor 1;
GN Name=carA-1; Synonyms=car1; ORFNames=DDB_G0273397;
GN and
GN Name=carA-2; Synonyms=car1; ORFNames=DDB_G0273533;
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], AND FUNCTION.
RX PubMed=3047871; DOI=10.1126/science.3047871;
RA Klein P.S., Sun T.J., Saxe C.L. III, Kimmel A.R., Johnson R.L.,
RA Devreotes P.N.;
RT "A chemoattractant receptor controls development in Dictyostelium
RT discoideum.";
RL Science 241:1467-1472(1988).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=1692327; DOI=10.1083/jcb.110.5.1549;
RA Sun T.J., Van Haastert P.J.M., Devreotes P.N.;
RT "Surface cAMP receptors mediate multiple responses during development in
RT Dictyostelium: evidenced by antisense mutagenesis.";
RL J. Cell Biol. 110:1549-1554(1990).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=1989903; DOI=10.1101/gad.5.1.1;
RA Saxe C.L. III, Johnson R.L., Devreotes P.N., Kimmel A.R.;
RT "Expression of a cAMP receptor gene of Dictyostelium and evidence for a
RT multigene family.";
RL Genes Dev. 5:1-8(1991).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=1849108; DOI=10.1101/gad.5.4.572;
RA Sun T.J., Devreotes P.N.;
RT "Gene targeting of the aggregation stage cAMP receptor cAR1 in
RT Dictyostelium.";
RL Genes Dev. 5:572-582(1991).
RN [7]
RP INDUCTION.
RX PubMed=8392183; DOI=10.1073/pnas.90.13.5969;
RA Louis J.M., Saxe C.L. III, Kimmel A.R.;
RT "Two transmembrane signaling mechanisms control expression of the cAMP
RT receptor gene CAR1 during Dictyostelium development.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5969-5973(1993).
RN [8]
RP FUNCTION.
RX PubMed=7925004; DOI=10.1242/dev.120.7.1997;
RA Soede R.D.M., Insall R.H., Devreotes P.N., Schaap P.;
RT "Extracellular cAMP can restore development in Dictyostelium cells lacking
RT one, but not two subtypes of early cAMP receptors (cARs). Evidence for
RT involvement of cAR1 in aggregative gene expression.";
RL Development 120:1997-2002(1994).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=8150078; DOI=10.1016/0014-5793(94)80509-1;
RA Abe F., Maeda Y.;
RT "Precise expression of the cAMP receptor gene, CAR1, during transition from
RT growth to differentiation in Dictyostelium discoideum.";
RL FEBS Lett. 342:239-241(1994).
RN [10]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-299; SER-302; SER-303; SER-304;
RP SER-308; SER-324; SER-325; SER-331; 360-SER--SER-368; SER-383 AND SER-385.
RX PubMed=8120068; DOI=10.1016/s0021-9258(17)37479-3;
RA Hereld D., Vaughan R., Kim J.-Y., Borleis J.A., Devreotes P.N.;
RT "Localization of ligand-induced phosphorylation sites to serine clusters in
RT the C-terminal domain of the Dictyostelium cAMP receptor, cAR1.";
RL J. Biol. Chem. 269:7036-7044(1994).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=7876207; DOI=10.1074/jbc.270.9.4418;
RA Caterina M.J., Hereld D., Devreotes P.N.;
RT "Occupancy of the Dictyostelium cAMP receptor, cAR1, induces a reduction in
RT affinity which depends upon COOH-terminal serine residues.";
RL J. Biol. Chem. 270:4418-4423(1995).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=9334341; DOI=10.1083/jcb.139.2.365;
RA Xiao Z., Zhang N., Murphy D.B., Devreotes P.N.;
RT "Dynamic distribution of chemoattractant receptors in living cells during
RT chemotaxis and persistent stimulation.";
RL J. Cell Biol. 139:365-374(1997).
RN [13]
RP PHOSPHORYLATION AT SER-302; SER-303 AND SER-304, AND MUTAGENESIS OF
RP SER-299; SER-302; SER-303 AND SER-304.
RX PubMed=7721769; DOI=10.1074/jbc.270.15.8667;
RA Caterina M.J., Devreotes P.N., Borleis J.A., Hereld D.;
RT "Agonist-induced loss of ligand binding is correlated with phosphorylation
RT of cAR1, a G protein-coupled chemoattractant receptor from Dictyostelium.";
RL J. Biol. Chem. 270:8667-8672(1995).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF 288-LYS--ASN-392.
RX PubMed=9341180; DOI=10.1074/jbc.272.43.27313;
RA Kim J.-Y., Soede R.D.M., Schaap P., Valkema R., Borleis J.A.,
RA Van Haastert P.J.M., Devreotes P.N., Hereld D.;
RT "Phosphorylation of chemoattractant receptors is not essential for
RT chemotaxis or termination of G-protein-mediated responses.";
RL J. Biol. Chem. 272:27313-27318(1997).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF ASN-148; VAL-154; SER-155; PHE-156 AND
RP THR-157.
RX PubMed=9578623; DOI=10.1006/dbio.1998.8882;
RA Kim J.-Y., Borleis J.A., Devreotes P.N.;
RT "Switching of chemoattractant receptors programs development and
RT morphogenesis in Dictyostelium: receptor subtypes activate common responses
RT at different agonist concentrations.";
RL Dev. Biol. 197:117-128(1998).
RN [16]
RP PHOSPHORYLATION.
RX PubMed=9880518; DOI=10.1074/jbc.274.3.1440;
RA Xiao Z., Yao Y., Long Y., Devreotes P.N.;
RT "Desensitization of G-protein-coupled receptors. agonist-induced
RT phosphorylation of the chemoattractant receptor cAR1 lowers its intrinsic
RT affinity for cAMP.";
RL J. Biol. Chem. 274:1440-1448(1999).
RN [17]
RP FUNCTION.
RX PubMed=11319871; DOI=10.1006/dbio.2001.0217;
RA Briscoe C., Moniakis J., Kim J.-Y., Brown J.M., Hereld D., Devreotes P.N.,
RA Firtel R.A.;
RT "The phosphorylated C-terminus of cAR1 plays a role in cell-type-specific
RT gene expression and STATa tyrosine phosphorylation.";
RL Dev. Biol. 233:225-236(2001).
RN [18]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11422293; DOI=10.1046/j.1440-169x.2001.00572.x;
RA Tsujioka M., Yokoyama M., Nishio K., Kuwayama H., Morio T., Katoh M.,
RA Urushihara H., Saito T., Ochiai H., Tanaka Y., Takeuchi I., Maeda M.;
RT "Spatial expression patterns of genes involved in cyclic AMP responses in
RT Dictyostelium discoideum development.";
RL Dev. Growth Differ. 43:275-283(2001).
RN [19]
RP FUNCTION.
RX PubMed=11559759; DOI=10.1242/jcs.114.13.2513;
RA Dormann D., Kim J.-Y., Devreotes P.N., Weijer C.J.;
RT "cAMP receptor affinity controls wave dynamics, geometry and morphogenesis
RT in Dictyostelium.";
RL J. Cell Sci. 114:2513-2523(2001).
RN [20]
RP DEVELOPMENTAL STAGE [LARGE SCALE ANALYSIS].
RX PubMed=11923193; DOI=10.1242/dev.129.7.1543;
RA Van Driessche N., Shaw C., Katoh M., Morio T., Sucgang R., Ibarra M.,
RA Kuwayama H., Saito T., Urushihara H., Maeda M., Takeuchi I., Ochiai H.,
RA Eaton W., Tollett J., Halter J., Kuspa A., Tanaka Y., Shaulsky G.;
RT "A transcriptional profile of multicellular development in Dictyostelium
RT discoideum.";
RL Development 129:1543-1552(2002).
RN [21]
RP DEVELOPMENTAL STAGE [LARGE SCALE ANALYSIS].
RX PubMed=12796308; DOI=10.1128/ec.2.3.627-637.2003;
RA Maeda M., Sakamoto H., Iranfar N., Fuller D., Maruo T., Ogihara S.,
RA Morio T., Urushihara H., Tanaka Y., Loomis W.F.;
RT "Changing patterns of gene expression in Dictyostelium prestalk cell
RT subtypes recognized by in situ hybridization with genes from microarray
RT analyses.";
RL Eukaryot. Cell 2:627-637(2003).
RN [22]
RP DEVELOPMENTAL STAGE [LARGE SCALE ANALYSIS].
RX PubMed=12912885; DOI=10.1128/ec.2.4.664-670.2003;
RA Iranfar N., Fuller D., Loomis W.F.;
RT "Genome-wide expression analyses of gene regulation during early
RT development of Dictyostelium discoideum.";
RL Eukaryot. Cell 2:664-670(2003).
RN [23]
RP DEVELOPMENTAL STAGE [LARGE SCALE ANALYSIS].
RX PubMed=15470253; DOI=10.1128/ec.3.5.1241-1248.2004;
RA Maruo T., Sakamoto H., Iranfar N., Fuller D., Morio T., Urushihara H.,
RA Tanaka Y., Maeda M., Loomis W.F.;
RT "Control of cell type proportioning in Dictyostelium discoideum by
RT differentiation-inducing factor as determined by in situ hybridization.";
RL Eukaryot. Cell 3:1241-1248(2004).
RN [24]
RP MUTAGENESIS OF LEU-100; ILE-102; ILE-104; VAL-136 AND ASN-225.
RX PubMed=15574880; DOI=10.1091/mbc.e04-06-0456;
RA Zhang M., Goswami M., Hereld D.;
RT "Constitutively active G protein-coupled receptor mutants block
RT dictyostelium development.";
RL Mol. Biol. Cell 16:562-572(2005).
RN [25]
RP MUTAGENESIS OF ILE-104.
RX PubMed=17630977; DOI=10.1111/j.1365-2958.2007.05803.x;
RA Zhang M., Goswami M., Sawai S., Cox E.C., Hereld D.;
RT "Regulation of G protein-coupled cAMP receptor activation by a hydrophobic
RT residue in transmembrane helix 3.";
RL Mol. Microbiol. 65:508-520(2007).
CC -!- FUNCTION: Receptor for cAMP. Coordinates the aggregation of individual
CC cells into a multicellular organism and regulates the expression of a
CC large number of developmentally regulated genes. The activity of this
CC receptor is mediated by G proteins. {ECO:0000269|PubMed:11319871,
CC ECO:0000269|PubMed:11559759, ECO:0000269|PubMed:1692327,
CC ECO:0000269|PubMed:1849108, ECO:0000269|PubMed:3047871,
CC ECO:0000269|PubMed:7925004, ECO:0000269|PubMed:9341180,
CC ECO:0000269|PubMed:9578623}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7876207,
CC ECO:0000269|PubMed:9334341}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:7876207, ECO:0000269|PubMed:9334341}.
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly during early aggregation
CC and at low levels during later stage. {ECO:0000269|PubMed:11422293,
CC ECO:0000269|PubMed:11923193, ECO:0000269|PubMed:12796308,
CC ECO:0000269|PubMed:12912885, ECO:0000269|PubMed:15470253,
CC ECO:0000269|PubMed:1692327, ECO:0000269|PubMed:1849108,
CC ECO:0000269|PubMed:1989903, ECO:0000269|PubMed:8150078}.
CC -!- PTM: C-terminal Ser or Thr residues may be phosphorylated.
CC {ECO:0000269|PubMed:7721769, ECO:0000269|PubMed:8120068,
CC ECO:0000269|PubMed:9880518}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 5 family.
CC {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; M21824; AAA33177.1; -; mRNA.
DR EMBL; AAFI02000010; EAL70653.1; -; Genomic_DNA.
DR EMBL; AAFI02000010; EAL70721.1; -; Genomic_DNA.
DR PIR; A41238; A41238.
DR RefSeq; XP_644603.1; XM_639511.1.
DR RefSeq; XP_644648.1; XM_639556.1.
DR AlphaFoldDB; P13773; -.
DR SMR; P13773; -.
DR STRING; 44689.DDB0185024; -.
DR TCDB; 9.A.14.5.1; the g-protein-coupled receptor (gpcr) family.
DR iPTMnet; P13773; -.
DR PaxDb; P13773; -.
DR EnsemblProtists; EAL70653; EAL70653; DDB_G0273397.
DR EnsemblProtists; EAL70721; EAL70721; DDB_G0273533.
DR GeneID; 8618967; -.
DR GeneID; 8619010; -.
DR KEGG; ddi:DDB_G0273397; -.
DR KEGG; ddi:DDB_G0273533; -.
DR dictyBase; DDB_G0273397; carA-1.
DR dictyBase; DDB_G0273533; carA-2.
DR eggNOG; ENOG502RYGP; Eukaryota.
DR HOGENOM; CLU_050319_0_0_1; -.
DR InParanoid; P13773; -.
DR OMA; IACFCAT; -.
DR PhylomeDB; P13773; -.
DR PRO; PR:P13773; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0009986; C:cell surface; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0005769; C:early endosome; IDA:dictyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030552; F:cAMP binding; IDA:dictyBase.
DR GO; GO:0001646; F:cAMP receptor activity; IDA:dictyBase.
DR GO; GO:0001637; F:G protein-coupled chemoattractant receptor activity; IDA:dictyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; IMP:dictyBase.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IGI:dictyBase.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:dictyBase.
DR GO; GO:0032148; P:activation of protein kinase B activity; IMP:dictyBase.
DR GO; GO:0023058; P:adaptation of signaling pathway; IMP:dictyBase.
DR GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IDA:dictyBase.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0002029; P:desensitization of G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IMP:dictyBase.
DR GO; GO:1900275; P:negative regulation of phospholipase C activity; IMP:dictyBase.
DR GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:dictyBase.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:dictyBase.
DR GO; GO:0097696; P:receptor signaling pathway via STAT; IMP:dictyBase.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0050764; P:regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IMP:dictyBase.
DR GO; GO:1902168; P:response to catechin; IDA:dictyBase.
DR GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
DR GO; GO:1903013; P:response to differentiation-inducing factor 1; HDA:dictyBase.
DR GO; GO:0010225; P:response to UV-C; IDA:dictyBase.
DR InterPro; IPR022343; GCR1-cAMP_receptor.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000848; GPCR_cAMP.
DR PRINTS; PR02001; GCR1CAMPR.
DR PRINTS; PR00247; GPCRCAMP.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..392
FT /note="Cyclic AMP receptor 1"
FT /id="PRO_0000195080"
FT TOPO_DOM 1..13
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..83
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..109
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..139
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..181
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..224
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..260
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 292..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7721769"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7721769"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7721769"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 100
FT /note="L->H: In DN3; constitutive phosphorylation and
FT greatly increased affinity for cAMP."
FT /evidence="ECO:0000269|PubMed:15574880"
FT MUTAGEN 102
FT /note="I->T: In DN2; constitutive phosphorylation and
FT greatly increased affinity for cAMP; when associated with
FT D-225."
FT /evidence="ECO:0000269|PubMed:15574880"
FT MUTAGEN 104
FT /note="I->N: In DN4; constitutive phosphorylation and
FT greatly increased affinity for cAMP. In DN1; Constitutive
FT phosphorylation and greatly increased affinity for cAMP;
FT when associated with A-136."
FT /evidence="ECO:0000269|PubMed:15574880,
FT ECO:0000269|PubMed:17630977"
FT MUTAGEN 104
FT /note="I->X: Most substitutions increase affinity for cAMP
FT and the most polar substitutions block development."
FT /evidence="ECO:0000269|PubMed:15574880,
FT ECO:0000269|PubMed:17630977"
FT MUTAGEN 136
FT /note="V->A: In DN1; constitutive phosphorylation and
FT greatly increased affinity for cAMP; when associated with
FT N-104."
FT /evidence="ECO:0000269|PubMed:15574880"
FT MUTAGEN 148
FT /note="N->G: Reduces the affinity for cAMP by 100 to 1000-
FT fold when associated with D-154; N-155; Y-156 and D-157."
FT /evidence="ECO:0000269|PubMed:9578623"
FT MUTAGEN 154
FT /note="V->D: Reduces the affinity for cAMP by 100 to 1000-
FT fold when associated with G-148; N-155; Y-156 and D-157."
FT /evidence="ECO:0000269|PubMed:9578623"
FT MUTAGEN 155
FT /note="S->N: Reduces the affinity for cAMP by 100 to 1000-
FT fold when associated with G-148; D-154; Y-156 and D-157."
FT /evidence="ECO:0000269|PubMed:9578623"
FT MUTAGEN 156
FT /note="F->Y: Reduces the affinity for cAMP by 100 to 1000-
FT fold when associated with G-148; D-154; N-155 and D-157."
FT /evidence="ECO:0000269|PubMed:9578623"
FT MUTAGEN 157
FT /note="T->D: Reduces the affinity for cAMP by 100 to 1000-
FT fold when associated with G-148; D-154; N-155 and Y-156."
FT /evidence="ECO:0000269|PubMed:9578623"
FT MUTAGEN 225
FT /note="N->D: In DN2; constitutive phosphorylation and
FT greatly increased affinity for cAMP; when associated with
FT T-102."
FT /evidence="ECO:0000269|PubMed:15574880"
FT MUTAGEN 288..392
FT /note="Missing: No effect on cAMP-dependent gene
FT expression, chemotaxis, aggregation and differentiation."
FT /evidence="ECO:0000269|PubMed:9341180"
FT MUTAGEN 299
FT /note="S->A: Greatly reduces ligand induced
FT phosphorylation; when associated with G-302; A-303; G-304
FT and A-308."
FT /evidence="ECO:0000269|PubMed:7721769,
FT ECO:0000269|PubMed:8120068"
FT MUTAGEN 302
FT /note="S->G: Greatly reduces ligand induced
FT phosphorylation; when associated with A-299; A-303; G-304
FT and A-308."
FT /evidence="ECO:0000269|PubMed:7721769,
FT ECO:0000269|PubMed:8120068"
FT MUTAGEN 303
FT /note="S->A: Greatly reduces ligand induced
FT phosphorylation; when associated with A-299; G-302; G-304
FT and A-308."
FT /evidence="ECO:0000269|PubMed:7721769,
FT ECO:0000269|PubMed:8120068"
FT MUTAGEN 304
FT /note="S->G: Greatly reduces ligand induced
FT phosphorylation; when associated with A-299; G-302; A-303
FT and A-308."
FT /evidence="ECO:0000269|PubMed:7721769,
FT ECO:0000269|PubMed:8120068"
FT MUTAGEN 308
FT /note="S->A: Greatly reduces ligand induced
FT phosphorylation; when associated with A-299; G-302; A-303
FT and G-304."
FT /evidence="ECO:0000269|PubMed:8120068"
FT MUTAGEN 324
FT /note="S->G: Slightly reduces ligand induced and basal
FT phosphorylation; when associated with A-325 and A-331."
FT /evidence="ECO:0000269|PubMed:8120068"
FT MUTAGEN 325
FT /note="S->A: Slightly reduces ligand induced and basal
FT phosphorylation; when associated with G-324 and A-331."
FT /evidence="ECO:0000269|PubMed:8120068"
FT MUTAGEN 331
FT /note="S->A: Slightly reduces ligand induced and basal
FT phosphorylation; when associated with G-324 and A-325."
FT /evidence="ECO:0000269|PubMed:8120068"
FT MUTAGEN 360..368
FT /note="Missing: Greatly reduces basal phosphorylation."
FT /evidence="ECO:0000269|PubMed:8120068"
FT MUTAGEN 383
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:8120068"
FT MUTAGEN 385
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:8120068"
SQ SEQUENCE 392 AA; 44312 MW; 38C4561EE1CC9A69 CRC64;
MGLLDGNPAN ETSLVLLLFA DFSSMLGCMA VLIGFWRLKL LRNHVTKVIA CFCATSFCKD
FPSTILTLTN TAVNGGFPCY LYAIVITYGS FACWLWTLCL AISIYMLIVK REPEPERFEK
YYYLLCWGLP LISTIVMLAK NTVQFVGNWC WIGVSFTGYR FGLFYGPFLF IWAISAVLVG
LTSRYTYVVI HNGVSDNKEK HLTYQFKLIN YIIVFLVCWV FAVVNRIVNG LNMFPPALNI
LHTYLSVSHG FWASVTFIYN NPLMWRYFGA KILTVFTFFG YFTDVQKKLE KNKNNNNPSP
YSSSRGTSGK TMGGHPTGDD VQCSSDMEQC SLERHPNMVN NQQNLNNNYG LQQNYNDEGS
SSSSLSSSDE EKQTVEMQNI QISTSTNGQG NN
