ID   B8JK56_MOUSE            Unreviewed;      1144 AA.
AC   B8JK56;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 113.
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:ENSMUSP00000122073.2,
GN   ECO:0000313|MGI:MGI:99675};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000122073.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000122073.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122073.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000122073.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122073.2};
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   RefSeq; NP_001153008.1; NM_001159536.1.
DR   RefSeq; NP_001153009.1; NM_001159537.1.
DR   ProteomicsDB; 333181; -.
DR   Antibodypedia; 4130; 173 antibodies from 26 providers.
DR   DNASU; 104111; -.
DR   Ensembl; ENSMUST00000124505.8; ENSMUSP00000122073.2; ENSMUSG00000020654.16.
DR   Ensembl; ENSMUST00000152065.8; ENSMUSP00000115644.2; ENSMUSG00000020654.16.
DR   GeneID; 104111; -.
DR   UCSC; uc007mxk.2; mouse.
DR   AGR; MGI:99675; -.
DR   CTD; 109; -.
DR   MGI; MGI:99675; Adcy3.
DR   VEuPathDB; HostDB:ENSMUSG00000020654; -.
DR   GeneTree; ENSGT00940000156549; -.
DR   HOGENOM; CLU_001072_2_0_1; -.
DR   OrthoDB; 3686360at2759; -.
DR   TreeFam; TF313845; -.
DR   BioGRID-ORCS; 104111; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Adcy3; mouse.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; ENSMUSG00000020654; Expressed in gastrula and 243 other cell types or tissues.
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; 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   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|EPD:B8JK56,
KW   ECO:0007829|MaxQB:B8JK56};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
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        632..652
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        664..686
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        707..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        752..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        776..794
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        840..857
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          923..1075
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          504..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..547
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         975
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         1062..1064
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         1069..1073
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         1109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
SQ   SEQUENCE   1144 AA;  128998 MW;  989F69F858CEC87C CRC64;
     MPRNQGFSDP EYSAEYSAEY SVSLPSDPDR GVGRTHEISV RNSGSCLCLP RFMRLTFVPE
     SLENLYQTYF KRQRHETLLV LVVFAALFDC YVVVMCAVVF SSDKLAPLMV AGFGLVLDII
     LFVLCKKGLL PDRVSRKVVP YLLWLLISAQ IFSYLGLNFS RAHAASDTVG WQAFFVFSFF
     ITLPLSLSPI VIISVVSCVV HTLVLGVTVA QQQQDELEGM QLLREILANV FLYLCAIIVG
     IMSYYMADRK HRKAFLEARQ SLEVKMNLEE QSQQQENLML SILPKHVADE MLKDMKKDES
     QKDQQQFNTM YMYRHENVSI LFADIVGFTQ LSSACSAQEL VKLLNELFAR FDKLAAKYHQ
     LRIKILGDCY YCICGLPDYR EDHAVCSILM GLAMVEAISY VREKTKTGVD MRVGVHTGTV
     LGGVLGQKRW QYDVWSTDVT VANKMEAGGI PGRVHISQST MDCLKGEFDV EPGDGGSRCD
     YLDEKGIETY LIIASKPEVK KTAQNGLNGS AVPNGAPASS KPSSPALIET KEPNGSAHAS
     GSTSEEAEEQ EAQADNPSFP NPRRRLRLQD LADRVVDASE DEHELNQLLN EALLERESAQ
     VVKKRNTFLL TMRFMDPEME TRYSVEKEKQ SGAAFSCSCV VLFCTAMVEI LIDPWLMTNY
     VTFVVGEVLL LILTICSMAA IFPRSFPKKL VAFSSWIDRT RWARNTWAML AIFILVMANV
     VDMLSCLQYY MGPYNMTAGM ELDGGCMENP KYYNYVAVLS LIATIMLVQV SHMVKLTLML
     LVTGAVTALN LYAWCPVFDE YDHKRFQEKD SPMVALEKMQ VLATPGLNGT DRLPLVPSKY
     SMTVMMFVMM LSFYYFSRHV EKLARTLFLW KIEVHDQKER VYEMRRWNEA LVTNMLPEHV
     ARHFLGSKKR DEELYSQSYD EIGVMFASLP NFADFYTEES INNGGIECLR FLNEIISDFD
     SLLDNPKFRV ITKIKTIGST YMAASGVTPD VNTNGFTSSS KEEKSDKERW QHLADLADFA
     LAMKDTLTNI NNQSFNNFML RIGMNKGGVL AGVIGARKPH YDIWGNTVNV ASRMESTGVM
     GNIQVVEETQ VILREYGFRF VRRGPIFVKG KGELLTFFLK GRDRPAAFPN GSSVTLPHQV
     VDNP
//