CYAD_DICDI
ID CYAD_DICDI Reviewed; 2123 AA.
AC Q55F68; Q9U9S7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Adenylate cyclase, terminal-differentiation specific;
DE Short=ACR {ECO:0000303|PubMed:10556070};
DE EC=4.6.1.1 {ECO:0000269|PubMed:10556070};
DE AltName: Full=ACB;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=acrA; Synonyms=acb; ORFNames=DDB_G0267376;
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], SUBUNIT, FUNCTION, CATALYTIC ACTIVITY,
RP DEVELOPMENTAL STAGE, COFACTOR, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX4;
RX PubMed=10556070; DOI=10.1242/dev.126.23.5463;
RA Soederbom F., Anjard C., Iranfar N., Fuller D., Loomis W.F.;
RT "An adenylyl cyclase that functions during late development of
RT Dictyostelium.";
RL Development 126:5463-5471(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 AS AN ADENYLYL CYCLASE ACTIVITY.
RC STRAIN=AX2;
RX PubMed=9812977; DOI=10.1074/jbc.273.47.30859;
RA Kim H.-J., Chang W.-T., Meima M., Gross J.D., Schaap P.;
RT "A novel adenylyl cyclase detected in rapidly developing mutants of
RT Dictyostelium.";
RL J. Biol. Chem. 273:30859-30862(1998).
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=NC-4;
RX PubMed=10419694; DOI=10.1006/dbio.1999.9352;
RA Meima M.E., Schaap P.;
RT "Fingerprinting of adenylyl cyclase activities during Dictyostelium
RT development indicates a dominant role for adenylyl cyclase B in terminal
RT differentiation.";
RL Dev. Biol. 212:182-190(1999).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX4;
RX PubMed=11566867; DOI=10.1242/dev.128.18.3649;
RA Anjard C., Soederbom F., Loomis W.F.;
RT "Requirements for the adenylyl cyclases in the development of
RT Dictyostelium.";
RL Development 128:3649-3654(2001).
RN [6]
RP ACTIVITY REGULATION.
RC STRAIN=NC-4;
RX PubMed=16952277; DOI=10.1042/bj20060880;
RA Alvarez-Curto E., Weening K.E., Schaap P.;
RT "Pharmacological profiling of the Dictyostelium adenylate cyclases ACA, ACB
RT and ACG.";
RL Biochem. J. 401:309-316(2007).
CC -!- FUNCTION: Through the production of cAMP, activates cAMP-dependent
CC protein kinases (PKAs), triggering terminal differential and the
CC production of spores. {ECO:0000269|PubMed:10419694,
CC ECO:0000269|PubMed:10556070, ECO:0000269|PubMed:11566867,
CC ECO:0000269|PubMed:9812977}.
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 Evidence={ECO:0000269|PubMed:10556070};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15390;
CC Evidence={ECO:0000269|PubMed:10556070};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10556070};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by high osmolarity. Inhibited by
CC caffeine and 2',5'-dideoxyadenosine (DDA).
CC {ECO:0000269|PubMed:16952277}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:10556070}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Present at low levels in growing cells;
CC accumulates to high levels throughout development (PubMed:10556070).
CC Highly expressed during early culmination and in fruiting bodies,
CC especially in the prestalk region. {ECO:0000269|PubMed:10419694,
CC ECO:0000269|PubMed:10556070, ECO:0000269|PubMed:11566867}.
CC -!- DISRUPTION PHENOTYPE: Cells cannot complete sporulation and have
CC abnormally long, thin stalks, though able to aggregate and form normal
CC slugs. {ECO:0000269|PubMed:10556070}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AF153362; AAD50121.1; -; Genomic_DNA.
DR EMBL; AAFI02000003; EAL73140.1; -; Genomic_DNA.
DR RefSeq; XP_647665.1; XM_642573.1.
DR AlphaFoldDB; Q55F68; -.
DR SMR; Q55F68; -.
DR STRING; 44689.DDB0191294; -.
DR PaxDb; Q55F68; -.
DR PRIDE; Q55F68; -.
DR EnsemblProtists; EAL73140; EAL73140; DDB_G0267376.
DR GeneID; 8616482; -.
DR KEGG; ddi:DDB_G0267376; -.
DR dictyBase; DDB_G0267376; acrA.
DR eggNOG; ENOG502RSS4; Eukaryota.
DR HOGENOM; CLU_232101_0_0_1; -.
DR InParanoid; Q55F68; -.
DR OMA; ICKSITI; -.
DR PRO; PR:Q55F68; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:dictyBase.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR GO; GO:0006171; P:cAMP biosynthetic process; IDA:dictyBase.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IMP:dictyBase.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IMP:dictyBase.
DR GO; GO:0031000; P:response to caffeine; IDA:dictyBase.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF52172; SSF52172; 2.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP biosynthesis; Lyase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Sporulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..2123
FT /note="Adenylate cyclase, terminal-differentiation
FT specific"
FT /id="PRO_0000328240"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 654..928
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 954..1076
FT /note="Response regulatory 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 1125..1310
FT /note="Response regulatory 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 1583..1712
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2039..2123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2054..2123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1588
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1588
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1589
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1632
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1632
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT MOD_RES 1010
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 1174
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 1936
FT /note="Q -> R (in Ref. 1; AAD50121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2123 AA; 243012 MW; D99245C5D8C2902B CRC64;
MTNNRLKNRK KPNQIHTISE EEEEEEPLFN NEDLQTQHLN SPSSDSISTS SSSSLSSVGG
SVVGNNNSNS NGIDNNNSNN NNNNNNNNNN NNNNNNSNNN NNYTGNSIGG NDFKNKASSS
SSTPTTSTGI GSSKFPNIKR KNSFSNRYDS GGGGSGSSRS NSFGGSNSSG GASKEFFYFD
NDDMIQDDDL IPMLMQDQEH QLQTQYQNQQ QVQQQQNIIN SFINHENLKF PFSIIYTNKL
HIWLSYFLFT FVLIFCCLAV GPLLWIELPP NSGCMWCRIF KLEWVISFMS LISAMFHYTI
RRDMFPLYLS IIGFYHVLTY SEPFLEPFRV NNFFSLILTV ICIFIAFYPK NKLRRQQASN
HHQQQQQQQQ QQRQRQQNNN RQPEKSIIKR IIQNEWFHSL IQILIVLGIV VLLFFSIFIL
ALFMKDDKTF SGDVIDGNIN SNNNNNNNNN NNINNNNIDN NNNNIKNNNK GFIEEIEQGE
EQLELYLENA YHIFKELVFK KFISSSVVYL ILITLLFCIS LVYHWEVRKP YTLMALASMI
PQLTQALYKV ELTLTGVMDK GTMSHNVTPL GGGIFYILNV ISYTSFYCGL AIDVVVASGE
KYKRLKKRGE KYHRRLSTQI NEQNAFVNKI YASGTAQLLQ KVEFMQKFVD KILFSTLEIS
NRLQRLESSD QDIPSSLVDQ LNDIQYQTNR SLLLLNDTKL ILAIESGVIS REDVSVNLFD
FLEDVLERTS KDIKFNNIEL VYKIDKDVPL NIILDPTALT QICFQLLSNA IKYTEEGEIG
ILIKRILRND YEYQQEQQQP QQDNELPPFG TISEEDEEYN SNNPPPPLNQ QQQQRQQQQQ
QEPKQIYLEI SIFDSGPGMD DDELDICNQF QPFPDIGDED DIEIKKKGSG LGLLICNKVL
KSIGGDLIVE RYLETGGCIF KCCIPVLVDP QPKENFTFQI PLSQETNELL SDLSVLVIDD
NPYARDSVGF IFSSVFNSAI VKSANSSVEG VRDLKYAIAT DSNFKLLLVD YHMPGCDGIE
AIQMIVDNPA FSDIKIILMI LPSDSFAHMN EKTKNITTLI KPVTPTNLFN AISKTFKLKE
FSSVVDLVDL NAPDTSTQIP LKRNRLKFKI DFPFRLPETG KPIMRVLIGE SDKSTQSKIQ
KVIESFGYFS TFVTDGTALI SLSKKNYYDL VIVDLELQST DGFECAQIIR DTHGEIFSNT
IFVPKPISTN SNDDNNNNNN NNNNNNNNDN NNNNNNNNNN NNNNNNNNNN NNNNNNNSIL
TSSVDTDGNH IVSSSTSTSS SFPTRRSSIG SFQTASPSMT EISHRRRVKL PIIGIWHHSD
IIPDDIIKKI KRVGFDGYCS FDNLEFYLQE FLLEFDRKRK SNILSPIRLF PNGSPSTNIY
DYSSIISNLN QASGNNNNSS PISGILNENV ISSPISLDLD LNSVSSIQSQ SSSSSSSFQH
NNQQQQQQQH QHQLTPTQQS IGGGNNGINQ LSFSSQQSTP IFNQSQIQHQ IISNRSKHSS
LSSSTSSNGS GGSGGKSRFS IPMLPSSTNR DSSPHSSSKM ALKRVQDLES VISKFVPIEF
QQLIAPSGME NVYLGDAICK SITIFFSDIR DFTSTTEKML VDDVIDFLNT YLAFALPSIT
DSGGFIDKFI GDAIMAIFPN SDMKLQAINA VKAAIRMMRS LDFMSISGFR FSSVETGVGI
NTGKTIIGIV GTENRMEPTA LGDAVNLASR TEQLCKEYQS RILITQFTME AIGTSIDEFV
IRLVDSVTVK GKSEAVNIYE VIDGEREDKR VLKMKILPWY QNGMDLYKRH CYEEALSYFQ
LCTEIMPNDK PTLIYIQRCI QNIKTLELQQ IQLQQLQRQQ LLQQQQQQLL LQQQLQQQQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ SQNIQQPQSQ QSQYVQQPQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQPQQQQQL QQQQQHQQQK QPSPQQQQQP
QQPQQQQQQQ IQNQYQHQLQ YQRQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQHHHHH HQQQQFQQQS QQSQQQSQQQ QQQQQQQSQQ QSQQQSQQIQ KKSQHPHSQQ
IQSQRHQSQP QNVDTNVKTK PQQ
