ID A0A091E6Q6_FUKDA Unreviewed; 973 AA.
AC A0A091E6Q6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201, ECO:0000256|PIRNR:PIRNR039050};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201, ECO:0000256|PIRNR:PIRNR039050};
GN ORFNames=H920_00107 {ECO:0000313|EMBL:KFO38458.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO38458.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO38458.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO38458.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP in
CC response to G-protein signaling. {ECO:0000256|PIRNR:PIRNR039050}.
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 ECO:0000256|PIRNR:PIRNR039050};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR039050-51};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR039050-51};
CC Note=Binds 2 magnesium ions per subunit. Is also active with manganese
CC (in vitro). {ECO:0000256|PIRSR:PIRSR039050-51};
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|PIRNR:PIRNR039050, ECO:0000256|RuleBase:RU000405}.
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DR EMBL; KN120510; KFO38458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091E6Q6; -.
DR STRING; 885580.ENSFDAP00000007671; -.
DR eggNOG; KOG3619; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR032628; AC_N.
DR InterPro; IPR030672; Adcy.
DR InterPro; IPR009398; Adcy_conserved_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF6; ADENYLATE CYCLASE TYPE 2; 1.
DR Pfam; PF16214; AC_N; 1.
DR Pfam; PF06327; Adcy_cons_dom; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR PIRSF; PIRSF039050; Ade_cyc; 1.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR039050};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998,
KW ECO:0000256|PIRNR:PIRNR039050};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR039050};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR039050};
KW Manganese {ECO:0000256|PIRSR:PIRSR039050-51};
KW Membrane {ECO:0000256|PIRNR:PIRNR039050, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR039050};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR039050,
KW ECO:0000256|PIRSR:PIRSR039050-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 508..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 561..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 171..298
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 769..914
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT BINDING 176..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-51"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-51"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-51"
FT BINDING 218..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-51"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-51"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 901..903
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 908..912
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 948
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
SQ SEQUENCE 973 AA; 109813 MW; 3F6D424C7F011B0C CRC64;
MGYLFMCFGG TVSAWDQVSF FLFIVFVVYT MLPFSMRDAI IASVLTSSSH TIVLSACLSA
TPGVKEHLVW QILANVIIFI CGNLAGAYHK HLMELALQQT YQDTCNCIKS RIKLEFEKRQ
QERLLLSLLP AHIAMEMKAE IIQRLQGPKA GQMENTNNFH NLYVKRHTNV SILYADIVGF
TRLASDCSPG ELVHMLNELF GKFDQIAKEN ECMRIKILGD CYYCVSGLPI SLPNHAKNCV
KMGLDMCEAI KKVRDATGVD INMRVGVHSG NVLCGVIGLQ KWQYDVWSHD VTLANHMEAG
GVPGRVHISS VTLEHLNGAY KVEEGDGDIR DPYLKQHLVK TYFVINPKGE RRSPQHLFRP
RHTLDGAKMR ASVRMTRYLE SWGAAKPFAH LHHRDSMTTE NGKISTTDVP MGQHNFQNRT
LRTKSQKKRF EEELNERMIQ AIDGINAQKQ WLKSEDIQRI SLLFYNKILE KEYRATALPA
FKYYVTCACL IFFCIFIVQV LVLPKTSILG ISFGAAFLSL AFILFVCFAG QLLQCSKKAS
ASLMWLLKSS GIIANRPWPR ISLTVVTTAI ILIMAVFNMF FLSDSEETVL PTANASDTNF
SASPSQAAVL RAQNLFFLPV RRSHSSLLLL FSYTVWLVKV SPARERQPWS SMAVALEKHS
RVETETHRGS HAVMLQRPGI WKDLKTMGSV SLSIFFITLL VLGRQNEYYC RLDFLWKNKF
KKEREEIETM ENLNRVLLEN VLPAHVAEHF LARSLKNEDL YHQSYDCVCV MFASIPDFKE
FYTESDVNKE GLECLRLLNE IIADFDDLLS KPKFSGVEKI KTIGSTYMAA TGLSAVPSQE
HAQEPERQYM HIGTMVEFAF ALVAKLDAIN KHSFNDFKLR VGINHGPVIA GVIGAQKPQY
DIWGNTVNVA SRMDSTGILD KIQVTEETSL ALQTLGYTCT CRGIINVKGK GDLKTYFVNT
EMSRSLSQSN MAS
//
