ID A0A2R9BLU9_PANPA Unreviewed; 1145 AA.
AC A0A2R9BLU9;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Adenylate cyclase type 3 {ECO:0000256|PIRNR:PIRNR039050};
DE EC=4.6.1.1 {ECO:0000256|PIRNR:PIRNR039050};
GN Name=ADCY3 {ECO:0000313|Ensembl:ENSPPAP00000030669.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000030669.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000030669.1}
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 EMBL; AJFE02094962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02094963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02094964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02094965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02094966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02094967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008950647.1; XM_008952399.1.
DR AlphaFoldDB; A0A2R9BLU9; -.
DR STRING; 9597.ENSPPAP00000030669; -.
DR Ensembl; ENSPPAT00000053532.1; ENSPPAP00000030669.1; ENSPPAG00000038289.1.
DR GeneID; 100995134; -.
DR KEGG; pps:100995134; -.
DR CTD; 109; -.
DR GeneTree; ENSGT00940000156549; -.
DR OMA; YLLCRYG; -.
DR OrthoDB; 3686360at2759; -.
DR Proteomes; UP000240080; Unplaced.
DR Bgee; ENSPPAG00000038289; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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:0007340; P:acrosome reaction; IEA:Ensembl.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1904322; P:cellular response to forskolin; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0008355; P:olfactory learning; IEA:Ensembl.
DR GO; GO:0007608; P:sensory perception of smell; 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; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF12; ADENYLATE CYCLASE TYPE 3; 1.
DR Pfam; PF16214; AC_N; 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:UP000240080};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 665..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 777..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 841..858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 319..446
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 924..1076
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 504..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 324..329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 324
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 324
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 325
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 366..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 368
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 368
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 412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 976
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1063..1065
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1070..1074
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
SQ SEQUENCE 1145 AA; 129013 MW; 4F88ABEED123AADB CRC64;
MPRNQGFSEP EYSAEYSAEY SVSLPSDPDR GVGRTHEISV RNSGSCLCLP RFMRLTFVPE
SLENLYQTYF KRQRHETLLV LVVFAALFDC YVVVMCAVVF SSDKLAPLAV AGIGLVLDII
LFVLCKKGLL PDRVTRRVVP YVLWLLITAQ IFSYLGLNFA RAHAASDTVG WQVFFVFSFF
ITLPLSLSPI VIISVVSCVV HTLVLGVTVA QQQQEELKGM QLLREILANV FLYLCAIAVG
IMSYYMADRK HRKAFLEARQ SLEVKMNLEE QSQQQENLML SILPKHVADE MLKDMKKDES
QKDQQQFNTM YMYRHENVSI LFADIVGFTQ LSSACSAQEL VKLLNELFAR FDKLAAKYHQ
LRIKILGDCY YCICGLPDYR EDHAVCSILM GLAMVEAISY VREKTKTGVD MRVGVHTGTV
LGGVLGQKRW QYDVWSTDVT VANKMEAGGI PGRVHISQST MDCLKGEFDV EPGDGGSRCD
YLEEKGIETY LIIASKPEVK KTATQNGLNG SALPNGAPAS SKSSSPALIE TKEPNGSAHS
SGSTSEKPEE QDAQADNPSF PNPRRRLRLQ DLADRVVDAS EDEHELNQLL NEALLERESA
QVVKKRNTFL LSMRFMDPEM ETRYSVEKEK QSGAAFSCSC VVLLCTALVE ILIDPWLMTN
YVTFMVGEIL LLILTICSLA AIFPRAFPKK LVAFSTWIDR TRWARNTWAM LAIFILVMAN
VVDMLSCLQY YTGPGNATAG METEGSCLEN PKYYNYVAVL SLIATIMLVQ VSHMVKLTLM
LLVAGAVATI NLYAWRPVFD EYDHKRFREH DLPMVALEQM QGFNPGLNGT DSRLPLVPSK
YSMTVMVFLM MLSFYYFSRH VEKLARTLFL WKIEVHDQKE RVYEMRRWNE ALVTNMLPEH
VARHFLGSKK RDEELYSQTY DEIGVMFASL PNFADFYTEE SINNGGIECL RFLNEIISDF
DSLLDNPKFR VITKIKTIGS TYMAASGVTP DVNTNGFASS NKEDKSERER WQHLADLADF
ALAMKDTLTN INNQSFNNFM LRIGMNKGGV LAGVIGARKP HYDIWGNTVN VASRMESTGV
MGNIQVVEET QVILREYGFR FVRRGPIFVK GKGELLTFFL KGRDKLATFP NGPSVTLPHQ
VVDNS
//
