ID I7G4M3_MACFA Unreviewed; 294 AA.
AC I7G4M3; A0A2K5WKE5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|EMBL:BAE88840.1};
RN [1] {ECO:0000313|EMBL:BAE88840.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17194215; DOI=10.1371/journal.pbio.0050013;
RA Wang H.-Y., Chien H.-C., Osada N., Hashimoto K., Sugano S., Gojobori T.,
RA Chou C.-K., Tsai S.-F., Wu C.-I., Shen C.-K.J.;
RT "Rate of evolution in brain-expressed genes in humans and other primates.";
RL PLoS Biol. 5:e13-e13(2007).
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000037628.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSMFAP00000037628.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001593};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR EMBL; AB171777; BAE88840.1; -; mRNA.
DR Ensembl; ENSMFAT00000011879.2; ENSMFAP00000037628.2; ENSMFAG00000061282.1.
DR VEuPathDB; HostDB:ENSMFAG00000038024; -.
DR GeneTree; ENSGT00940000154872; -.
DR Proteomes; UP000233100; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016849; F:phosphorus-oxygen lyase activity; IEA:InterPro.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF26; ADENYLATE CYCLASE TYPE 1; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT DOMAIN 43..185
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 275..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 32637 MW; A4D30F95BC006ED1 CRC64;
MEKVKLDNRR ILFNLLPAHV AQHFLMSNPR NMDLYYQSYS QVGVMFASIP NFNDFYIELD
GNNMGVECLR LLNEIIADFD ELMEKDFYKD IEKIKTIGST YMAAVGLAPT SGTKAKKSIS
SHLSTLADFA IEMFDVLDEI NYQSYNDFVL RVGINVGPVV AGVIGARRPQ YDIWGNTVNV
ASRMDSTGVQ GRIQVTEEVH RLLRRCPYHF VCRGKVSVKG KGEMLTYFLE GRTDGNGSQI
RSLGLDRKMG PYGRAGLQGR RPPVCPMPGV SVRAGLPPHS PGQYLSSAAA GKEA
//