CYAA_SCHPO
ID CYAA_SCHPO Reviewed; 1692 AA.
AC P14605;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Adenylate cyclase;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=cyr1; ORFNames=SPBC19C7.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2682634; DOI=10.1073/pnas.86.20.7989;
RA Young D., Riggs M., Field J., Vojtek A., Broek D., Wigler M.;
RT "The adenylyl cyclase gene from Schizosaccharomyces pombe.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7989-7993(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2668944; DOI=10.1073/pnas.86.15.5693;
RA Yamawaki-Kataoka Y., Tamaoki T., Choe H.-R., Tanaka H., Kataoka T.;
RT "Adenylate cyclases in yeast: a comparison of the genes from
RT Schizosaccharomyces pombe and Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5693-5697(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP ACTIVATION BY GIT1, INTERACTION WITH GIT1, AND SUBCELLULAR LOCATION.
RX PubMed=16489217; DOI=10.1534/genetics.106.055699;
RA Kao R.S., Morreale E., Wang L., Ivey F.D., Hoffman C.S.;
RT "Schizosaccharomyces pombe Git1 is a C2-domain protein required for glucose
RT activation of adenylate cyclase.";
RL Genetics 173:49-61(2006).
CC -!- FUNCTION: Plays essential roles in regulation of cellular metabolism by
CC catalyzing the synthesis of a second messenger, cAMP.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: In contrast to yeast cyclase, S.pombe cyclase is
CC not likely to be regulated by RAS proteins. Activated by git1.
CC -!- SUBUNIT: Interacts with git1. {ECO:0000269|PubMed:16489217}.
CC -!- INTERACTION:
CC P14605; Q9P7K5: git1; NbExp=3; IntAct=EBI-1542835, EBI-1542810;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16489217}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000305}.
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DR EMBL; M26699; AAA35284.1; -; Genomic_DNA.
DR EMBL; M24942; AAA35301.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19571.1; -; Genomic_DNA.
DR PIR; A33988; A33988.
DR RefSeq; NP_596159.1; NM_001022079.2.
DR AlphaFoldDB; P14605; -.
DR SMR; P14605; -.
DR BioGRID; 277329; 36.
DR IntAct; P14605; 1.
DR STRING; 4896.SPBC19C7.03.1; -.
DR iPTMnet; P14605; -.
DR MaxQB; P14605; -.
DR PaxDb; P14605; -.
DR PRIDE; P14605; -.
DR EnsemblFungi; SPBC19C7.03.1; SPBC19C7.03.1:pep; SPBC19C7.03.
DR GeneID; 2540810; -.
DR KEGG; spo:SPBC19C7.03; -.
DR PomBase; SPBC19C7.03; cyr1.
DR VEuPathDB; FungiDB:SPBC19C7.03; -.
DR eggNOG; KOG0618; Eukaryota.
DR HOGENOM; CLU_000430_4_1_1; -.
DR InParanoid; P14605; -.
DR OMA; HDPAEPN; -.
DR PhylomeDB; P14605; -.
DR Reactome; R-SPO-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
DR PRO; PR:P14605; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; NAS:PomBase.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IDA:PomBase.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0010619; P:adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IMP:PomBase.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0061987; P:negative regulation of transcription from RNA polymerase II promoter by glucose; IMP:PomBase.
DR CDD; cd07302; CHD; 1.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 5.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR013716; Adenylate_cyclase_G-a-bd.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR000159; RA_dom.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00789; Ad_cyc_g-alpha; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 14.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP biosynthesis; Cytoplasm; Leucine-rich repeat; Lyase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1692
FT /note="Adenylate cyclase"
FT /id="PRO_0000195733"
FT DOMAIN 292..380
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REPEAT 430..450
FT /note="LRR 1"
FT REPEAT 454..474
FT /note="LRR 2"
FT REPEAT 477..498
FT /note="LRR 3"
FT REPEAT 503..524
FT /note="LRR 4"
FT REPEAT 526..547
FT /note="LRR 5"
FT REPEAT 549..570
FT /note="LRR 6"
FT REPEAT 572..594
FT /note="LRR 7"
FT REPEAT 596..617
FT /note="LRR 8"
FT REPEAT 618..639
FT /note="LRR 9"
FT REPEAT 660..681
FT /note="LRR 10"
FT REPEAT 684..705
FT /note="LRR 11"
FT REPEAT 707..729
FT /note="LRR 12"
FT REPEAT 730..751
FT /note="LRR 13"
FT REPEAT 753..774
FT /note="LRR 14"
FT REPEAT 783..805
FT /note="LRR 15"
FT REPEAT 807..827
FT /note="LRR 16"
FT REPEAT 831..852
FT /note="LRR 17"
FT REPEAT 855..876
FT /note="LRR 18"
FT REPEAT 878..899
FT /note="LRR 19"
FT REPEAT 901..922
FT /note="LRR 20"
FT REPEAT 930..951
FT /note="LRR 21"
FT DOMAIN 995..1275
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT DOMAIN 1332..1469
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1692 AA; 190334 MW; D137CBE8770A8655 CRC64;
MDQSKRLLKS AVPNPPEHFK TGISWLDDLD EKDDDSATSV NYDIPEITEA NLCNDSHEAL
SPCTQPVGNS GRPVEAFKTY PSTPAVPSKS VLFHFYEPDE NFSLSDTGRT KSDTALAARE
SSEKSEVPRD TRSAGIKPYK ENNSSNCAIS KEAGLRRLID KDRESFDKNL NQSFTNLTFP
EPISDDSDSV EFQRDSLNNN WPASLEGSIH ELPRNSDDDG IPASAAHILD LDYHRDSYDS
PWKKFLPYPS ILSDDSWKAP ESWGTSLPTE AIPKQVFTTR FFARPSLGNR KKEFFLRVYR
DDRTSVSFIC PIGIQTHEVI KLLARLFFLP SSANFYLLLI QFNTERILLP HEQPCIIFER
LLSLFGCKVT SDEEINEEDN YSVARLVFTT MDIGADVLRK FSEKKITANL DISRSNLEVI
PVKIYPYAHE LISLNVSHNL SLDLPLDFME RCVKLKRLDI SNNLRSPRGK PITALRQLEV
LNMSRNDIYE LDPLIFSGLS RNSLKELNIA NNKLFFLPHS TRYLVNLTYL DLSYNNFVTF
PLIITELSQL ETLNFSHNLL SQISSKIGSL VKLKHLYLQF NDLSNRLPQE IGLLKNLETI
DLSYNAITNI ASLSECPKLN SINVACNLLS FYEYSNPSAT FIDFSFCPLT TIDPAFSYSN
LVYFDISHAK LIGLKDSVIE TLVNVETVKV NYNHFTSISD AISAMQNLKY LSCTNCEMSY
VSPNLGKLKH LVHLDLHANN IKIFPEEVWQ VSSLKVVNLS SNILEKIKLP VATSKKLTRT
ISQLKIMRTL SGNPVSSLSS QEFVMPTVEE LYLVDNRLGN DCFTALEYFK CLKVLNLSYN
YLTEIPSKFF QNFSDLKHLF VSGNELANLS ISSTAQVLLE TLYANGNRLS SFPKNEALSK
SLRFLDISTN NLQNLAVEKA EKKSLTKLPQ LEYLNLSGNT WFRFSEHEDT NFTKSYLKNL
KFLSIMDLNT KFSNAPSDVL NHFIQRNSPQ PNILRYGVCG YLSRSIPVIS ACELVVNNFL
HPQSSLYCVL DSDISAGKNN RVLKFVYDNL ASCLAHEINA ADSSSEQICN ALRRGFLRLN
KKLGNVIHYD LRKSSEGDVD SNYVTTMNIS EKGYSMDSSC LDIGVSIILV YVRDTRAFVA
NVGTSMAIMS TRNDSEPTTL SVMHDVYNRD EIRRIVDSCG FISGEIKSTT TRAIGRLSQF
PGVQAVPYVN VQYLSELNEF IILANQEFWS VLSKRTVIDV VRANRHSPLL ASTKLRDYAI
AYGAEKNVLV VIVELNGLFE ENSLNFNQLR GDEKTLAISE KNDNMSFVQD LPDDSSLARM
NREVSPPKGC IAMVFTDIKN STLLWERHPI AMRSAIKTHN TIMRRQLRAT GGYEVKTEGD
AFMVCFQTVP AALLWCFSVQ LQLLSADWPN EIVESVQGRL VLGSKNEVLY RGLSVRIGVN
YGVTVSELDP ITRRMDYYGP VVNRTSRVVS VADGGQIAVS AEVVSVLNQL DSETMSSEKT
NVNEMEVRAL KQIGYIIHNL GEFKLKGLDT TEMISLVYPV QLQGRLERLI KSRSLGTPTA
LPETQTYTPV RSRSNSLRPM LARLSDSKSV HGEEGGSGKR SVSSLRNVSP SESTGGYEGC
IFDDQQYQLL YELCERLEDH AAILHGFPEP PPCDTGLAAP VNQAEEYSLF YRLTLRIENT
IYCVSQMLGH TG
