ID G1QJ62_NOMLE Unreviewed; 983 AA.
AC G1QJ62;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Adenylate cyclase type 7 {ECO:0000256|PIRNR:PIRNR039050};
DE EC=4.6.1.1 {ECO:0000256|PIRNR:PIRNR039050};
GN Name=ADCY7 {ECO:0000313|Ensembl:ENSNLEP00000000956.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000000956.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000000956.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000000956.2}
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 EMBL; ADFV01012659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01012660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01012661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01012662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01012663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01012664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01012665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01012666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01012667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1QJ62; -.
DR STRING; 61853.ENSNLEP00000000956; -.
DR Ensembl; ENSNLET00000001015.2; ENSNLEP00000000956.2; ENSNLEG00000000816.3.
DR eggNOG; KOG3619; Eukaryota.
DR GeneTree; ENSGT00940000159096; -.
DR HOGENOM; CLU_001072_2_5_1; -.
DR InParanoid; G1QJ62; -.
DR OMA; LIMPKTA; -.
DR TreeFam; TF313845; -.
DR Proteomes; UP000001073; Chromosome 2.
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:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0002819; P:regulation of adaptive immune response; IEA:Ensembl.
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:SF9; ADENYLATE CYCLASE TYPE 7; 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; 3.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 546..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 569..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..359
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 798..926
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 407..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 241
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 241
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 242
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 281
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 281
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"
SQ SEQUENCE 983 AA; 109027 MW; 99225E6F9BC7C4C5 CRC64;
MPAKGRYFLN EGEEGPDQDA LYEKYQLTSQ HGPLLLTLLL VAATACVALI IIAFSQGVSE
GRPWASRLSP NLGQAAACAW EQVPFFLFII FVVYTLLPFS MRGAVAVGAI STASHLLVLG
ALMGGFTTPS VRVGLQLLAN AVIFLCGNLT GAFHKHQMQD ASRDLFTYTV KCIQIRRKLR
IEKRQQENLL LSVLPAHISM GMKLAIIERL KEHGDRRCMP DNNFHSLYVK RHQNVSILYA
DIVGFTQLAS DCSPKELVVF DQIAKVSLPA NECMRIKILG DCYYCVSGLP VSLPTHARNC
VKMGLDMCQA IKQVREATGV DINMRVGIHS GNVLCGVIGL RKWQYDVWSH DVSLANRMEA
AGVPGRVHIT EATLKHLDEA YEVEDGHGQQ RDPYLKEMNI RTYLVIDPRS QQPPPPSQHL
PRPKGDAALK MRASVRMTRY LESWGAARPF AHLNHRESVS SGETPVPNGR RPKVGPPPAQ
RARDWGPKPG YSQDVCGLDD PDTLSCVSSA CCSKSDDFYT FGSIFLEKSF EREYRLAPIP
RARHDFACAS LIFICILLIH VLLMPRTAAL GVSFGLVACV LGLVLGLCFA TKFSVSGEVW
PRGPSLPPLM PFPVPELPVG NETGLPATSS KTRALCEPLP YYTAAVSWAS SLLRLLRMSL
EPKVVLLTVA LVAYLVLFNL SPCWQWDCCG QGLGNLTDPN GTTSGTASCS WKDLKTMTNF
YLVLFYITLL TLSRQIDYYC RLDCLWKKKF KKEHEEFETM ENVNRLLLEN VLPAHVAAHF
IGDKLNEDWY HQSYDCVCVM FASVPDFKVF YTECDVNKEG LECLRLLNEI IADFDEVQPL
AQPCAAAPTH AGEGRELERQ HAHIGVMVEF SIALMSKLDG INRHSFNSFR LRVGINHGPV
IAGVIGARKP QYDIWGNTVN VASRMESTGE LGKIQVTEET CTILQGLGYS CECRGLINVK
GKGELRTYFV CTDTAKFQGL GLN
//
