CYAG_DICDI
ID CYAG_DICDI Reviewed; 858 AA.
AC Q03101; Q555V4; Q86A89;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Adenylate cyclase, germination specific;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=acgA; Synonyms=acg; ORFNames=DDB_G0274569;
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].
RX PubMed=1348970; DOI=10.1016/0092-8674(92)90411-5;
RA Pitt G.S., Milona N., Borleis J., Lin K.C., Reed R.R., Devreotes P.N.;
RT "Structurally distinct and stage-specific adenylyl cyclase genes play
RT different roles in Dictyostelium development.";
RL Cell 69:305-315(1992).
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 3D-STRUCTURE MODELING OF 387-543.
RX PubMed=9391039; DOI=10.1073/pnas.94.25.13414;
RA Liu Y., Ruoho A.E., Rao V.D., Hurley J.H.;
RT "Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and
RT mutational analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13414-13419(1997).
CC -!- FUNCTION: Has a large extracellular domain which may be involved in the
CC recognition of an extracellular signal present during germination,
CC leading to activation or inhibition of cAMP synthesis by the
CC cytoplasmic domain.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC -!- ACTIVITY REGULATION: Insensitive to guanine nucleotides.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- DEVELOPMENTAL STAGE: After fruiting bodies have been formed and during
CC germination.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; M87278; AAA33164.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL70177.1; -; Genomic_DNA.
DR PIR; A42239; A42239.
DR RefSeq; XP_643956.1; XM_638864.1.
DR AlphaFoldDB; Q03101; -.
DR SMR; Q03101; -.
DR STRING; 44689.DDB0185013; -.
DR PaxDb; Q03101; -.
DR PRIDE; Q03101; -.
DR EnsemblProtists; EAL70177; EAL70177; DDB_G0274569.
DR GeneID; 8619384; -.
DR KEGG; ddi:DDB_G0274569; -.
DR dictyBase; DDB_G0274569; acgA.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_333294_0_0_1; -.
DR InParanoid; Q03101; -.
DR OMA; ERSNNAC; -.
DR Reactome; R-DDI-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:Q03101; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005034; F:osmosensor activity; IDA:dictyBase.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0006171; P:cAMP biosynthetic process; IDA:dictyBase.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:dictyBase.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:1904360; P:negative regulation of spore germination; IMP:dictyBase.
DR GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; IMP:dictyBase.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0045859; P:regulation of protein kinase activity; TAS:dictyBase.
DR GO; GO:0010447; P:response to acidic pH; IDA:dictyBase.
DR GO; GO:0031000; P:response to caffeine; IDA:dictyBase.
DR GO; GO:0006970; P:response to osmotic stress; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IMP:dictyBase.
DR GO; GO:0009847; P:spore germination; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR GO; GO:0030104; P:water homeostasis; IDA:dictyBase.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.450.350; -; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; cAMP biosynthesis; Germination; Lyase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..858
FT /note="Adenylate cyclase, germination specific"
FT /id="PRO_0000195715"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..858
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 86..317
FT /note="CHASE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00049"
FT DOMAIN 396..526
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 650..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 401
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 401
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 402
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CONFLICT 755
FT /note="L -> F (in Ref. 1; AAA33164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 98380 MW; B409D387D8A96453 CRC64;
MKKTFVKILS KSYVEGYPVG FFIGLIILAI FGSMVCIFSF MHYSEEENSN IQMDLERSSK
QIIHNIQMNA MYLLSSIDTL KALYYVNPNF DRNDFNVFLN TTLKNSEFQY LFWIKKINNN
DRNCFEEKFS KEIKDTFQIY SFDENTNSIH VAKNKSSYFP ILHAFPDINK DIIGLDINST
DYMNETIKKS IFNKKPTVHL NKKVLLSKRN IDILIVSPII VTKTLESTNE TMEDMSHISS
GLFLMEKNVQ ASRIEVENGN DFTIFLSTTN GEIVYQENYL NFKTLYQVHE SGLFEDRLKY
ESSLKIADCV LKLWIFTTEE YENNSKTYLP LLVSIISAVI LVLLITYSVD QRKQKSLIAK
IMREKNNLIN KILPLEVSVK LENGEDVVAE RSNNACVFFL DIAGFTRFSS IHSPEQVIQV
LIKIFNSMDL LCAKHGIEKI KTIGDAYMAT CGIFPKCDDI RHNTYKMLGF AMDVLEFIPK
EMSFHLGLQV RVGIHCGPVI SGVISGYAKP HFDVWGDTVN VASRMESTGI AGQIHVSDRV
YQLGKEDFNF SERCDIIHVK GKGRMKTWYL MGKKSSDFSL KKDFSRSRVQ PSLFNRKQSH
VHCIYPEFPS GLQALNIENN LNNTDAGCEN CSKILKKTYA YSPDHSTSNY YYHGDDNSPP
PPSLNSNDLI DGSEYHDDPF PSDSNVGYHD TSKDIKEDEN EQNETLLFNQ EQLKKKQIEN
IQRDLSLNDS IEAIKILNNN NNNNINDNNI NNTNLNNNNN DININNSDNV NNYENNNNFS
DKIENNDGDN NNINDNNYKS TNENNIKSKT LFKDSKSLIN DIKMAKENCD NNDDNNNNNN
NNNNNNNNDE NVESKKNK
