ID H3BXV9_TETNG Unreviewed; 1101 AA.
AC H3BXV9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Adenylate cyclase type 2 {ECO:0000256|PIRNR:PIRNR039050};
DE EC=4.6.1.1 {ECO:0000256|PIRNR:PIRNR039050};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000000822.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000000822.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; H3BXV9; -.
DR Ensembl; ENSTNIT00000000046.1; ENSTNIP00000000822.1; ENSTNIG00000009256.1.
DR GeneTree; ENSGT00940000156424; -.
DR HOGENOM; CLU_001072_2_5_1; -.
DR Proteomes; UP000007303; 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:UP000007303};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 598..619
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 625..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 676..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 746..767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..831
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 288..415
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 897..1042
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT BINDING 293..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 293
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 293
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 294
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 335..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 337
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 337
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 381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 949
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1029..1031
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1036..1040
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1076
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
SQ SEQUENCE 1101 AA; 124393 MW; 1990F6F93FF10E55 CRC64;
WTRGRYLLEK SDGGEGAEGG EAEGQKPQDW LYESYYRMSQ QHPLIVFLLL IVMGTCLALL
AVFFASGLNT EDHLTFLVTV PAALFLFLSI FILVCIESVF KRMLRLFSLL IWACLVTMGY
LFMFSGGILS PWDQVSFFLF IVFVVYTMLP FSMRGAIIAS AITCSSHTVT LSVFLAARVP
ELEPLVWQIL ANVIIFICGN LAGAYHKHLM DLALKQTYQD TCNCIKSPMK LEFEKHQQER
LLLSLLPAHI ARVMKAEIIQ RLQGPNFGRT ESTNNFHNLY VQRHTNVSIL YADIVGFTRL
ASDCSPGELV HTLNELFGKF DQIAKENECM RIKILGDCYY CVSGLPESLP HHARNCVKMG
LDMCEAIKKV RDATGVDINM RVGVHSGNVL CGVIGLRKWQ YDVWSHDVTL ANHMEAGGVP
GRVHISSVTL EHLNGSYKVE PGDGQSRDSY LKEHGVVTFL VVNPKTERHS PLLCLRSRPS
LDGGKMRASV RMTRYLESWG AAKPFANLHH RDSMTTDNGK INTTDVPMGQ YHFQRRSLRS
KSQRRRFEEE LNERMIRTID GINSQKQWLK SEDIQRISLF FHNKALEKEY RSTTLPAFKY
YVACACLIFS CIFIVQVLVL PKTAVLGISF GLAFLLLALI LLLCFVDHIL QGRKGSFCPL
SWFPTSSRII VTNNPWLRLV LTMTTTALIL VMAVLNMFFV EDPGGSPAGV LTTSPPEVLV
SAPPLNLTND SLFGNREENA AEIKFYLPYF IYCCILGLVS CSVFLRINYE LKMVVMLVAV
VIYNVIILHT HSWLLDEFSK ALYPTPGVLK DLKTMGSVNL FIFFITLLVL ARQNEYYCRL
DFLWRDKFKR ECEEIETMEN LNRVLLENVL PAHVAEHFLG RNWKNEDLYH QSYESVCVMF
ASIPDFKEFY TESDVNKEGL ECLRLLNEII ADFDELLSKP KFSGVEKIKT IGSTYMAATG
LNVTPGPDCA QEHDRQYMHI GTMVEFAFAL VGKLDVINKH SFNDFRLRIG INHGPVIAGV
IGAQKPQYDI WGNSVNVASR METTGVLGKI QVTEETSRIL SSLGYACSCR GIINVKGKGE
LKTYFVHTEM TRSQSQGTVM P
//
