ID A0A3B3R355_9TELE Unreviewed; 1065 AA.
AC A0A3B3R355;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Adenylate cyclase type 7 {ECO:0000256|PIRNR:PIRNR039050};
DE EC=4.6.1.1 {ECO:0000256|PIRNR:PIRNR039050};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000012345.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000012345.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B3R355; -.
DR Ensembl; ENSPKIT00000036736.1; ENSPKIP00000012345.1; ENSPKIG00000000122.1.
DR GeneTree; ENSGT00940000159096; -.
DR Proteomes; UP000261540; Unplaced.
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; IPR030672; Adcy.
DR InterPro; IPR009398; Adcy_conserved_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF9; ADENYLATE CYCLASE TYPE 7; 1.
DR Pfam; PF06327; Adcy_cons_dom; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR PIRSF; PIRSF039050; Ade_cyc; 2.
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 590..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 691..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 779..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..357
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 863..1008
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT BINDING 235..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 235
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 235
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 236
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 277..279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 279
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 279
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 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 915
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 995..997
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1002..1006
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1042
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
SQ SEQUENCE 1065 AA; 120416 MW; 1214E221DBBF48FD CRC64;
MPTKGKYLLN NQELKQEALY RKFSCISQYQ LLVLLLGLTM LSCAILIILF FSLRLDASEH
SAFVSAVSCG LCVFLAVFVL VCTESLSQRW RRLLGVVVWA TLLTMSFTFI FSSHVIHAWD
QVPFFLFIIF TVYTMLPFQM RYAVLLSIIS SLSHIIVLAI YLSVTSHTSH PILAKQENLL
QSVLPVYISM KMKLAIMERL QDCKDKQEQQ RLVRDNNFHS LYVKRHENVS ILYADIVGFT
RLASDCSPKE LVIMLNELFG KFDQIAKENE CMRIKILGDC YYCVSGLPVS LPKHAKNCVK
MGLDMCEAIK QVREATGVDI NMRVGVHSGN VLCGVIGLRK WQFDVWSHDV TLANHMEAGG
LPGRVHITEA TLKHLNKAYE VEEGYGHLRD PYLKEQNIRT YLVIDPRSKE QCPNDTSKAR
MSDGLKMRAS VRMTRYLESW GAVKPFAHLQ SREGYGTDAM VNGKVRCKDI PLRSIPCSKI
PESLDESLEE SFVSPTPPFA SYKNKSQKSK FDEELHNEMT TTIDELSSSK QWVKSEEICS
LTLWFTKKEL EKQYRAIDLP SFKYYIGCAT LIFLCIFLVQ MFVTKEPQKL GVSFGVLACI
LLLILGVSFA GHLQRLFPEK LASCHWLPTV SEAVCKKPWV RLPLAILSTA VILIIAVFNL
CFMSHLTPCE ANSTSSITFL NVSQLLEMED LLFYLPYSVY CCLLALIACG VFLRVSFELK
LAFLILASTA YYIIILSAGD HLFQCYSGIL YHHCHGSNSS SNASYRDVLA YLGLVKHPQV
MSCMYITLFL VTMLIIIRQN EYCCRQDFLL KKKNRTEQDE IETRENLNRL LLENVLPAHV
ATLFIGENKK NEDLYYKSYD CVCVMFASVP DFKEFYTECD INKEGLECLR LLNEIIADFD
ELLSKPKFSG VEKIKTIGST YMAAAGLSGT LGQETKRDRD KQQAQIGIMV EFAIALIGKL
DGINRHSFNS FRLRVGINHG PVIAGVIGAR KPQYDIWGNT VNVASRMEST GELGKIQVTE
ETSIVLQILG YSCECRGLIN VKGKGELRTY FVCTDTSKSQ GLGLS
//
