ID   Q86TZ7_HUMAN            Unreviewed;      1105 AA.
AC   Q86TZ7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE   Flags: Fragment;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:CAD62613.1};
RN   [1] {ECO:0000313|EMBL:CAD62613.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Placenta {ECO:0000313|EMBL:CAD62613.1};
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAD62613.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Placenta {ECO:0000313|EMBL:CAD62613.1};
RA   Genoscope;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- 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|RuleBase:RU000405}.
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DR   EMBL; BX248285; CAD62613.1; -; mRNA.
DR   RefSeq; NP_001185521.1; NM_001198592.1.
DR   AlphaFoldDB; Q86TZ7; -.
DR   PeptideAtlas; Q86TZ7; -.
DR   DNASU; 196883; -.
DR   GeneID; 196883; -.
DR   CTD; 196883; -.
DR   OrthoDB; 3686360at2759; -.
DR   BioGRID-ORCS; 196883; 14 hits in 1141 CRISPR screens.
DR   GenomeRNAi; 196883; -.
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-KW.
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:SF10; ADENYLATE CYCLASE TYPE 4; 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.
DR   Genevisible; Q86TZ7; HS.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR039050-
KW   50}; cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR039050-
KW   51}; Manganese {ECO:0000256|PIRSR:PIRSR039050-51};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR039050-51};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR039050-50};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        614..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        639..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        692..713
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        748..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        772..793
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        818..835
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          301..428
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          901..1046
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         306..311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         306
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         306
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         307
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         348..350
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         350
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         350
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         394
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         953
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         1033..1035
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         1040..1044
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         1080
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAD62613.1"
SQ   SEQUENCE   1105 AA;  122352 MW;  238E4973341EBCBB CRC64;
     SPAPSPDLAH SAAPAPRAPA PGLGAGEIMA RLFSPRPPPS EDLFYETYYS LSQQYPLLLL
     LLGIVLCALA ALLAVAWASG RELTSDPSFL TTVLCALGGF SLLLGLASRE QRLQRWTRPL
     SGLVWVALLA LGHAFLFTGG VVSAWDQVSY FLFVIFTAYA MLPLGMRDAA VAGLASSLSH
     LLVLGLYLGP QPDSRPALLP QLAANAVLFL CGNVAGVYHK ALMERALRAT FREALSSLHS
     RRRLDTEKKH QEHLLLSILP AYLAREMKAE IMARLQAGQG SRPESTNNFH SLYVKRHQGV
     SVLYADIVGF TRLASECSPK ELVLMLNELF GKFDQIAKEH ECMRIKILGD CYYCVSGLPL
     SLPDHAINCV RMGLDMCRAI RKLRAATGVD INMRVGVHSG SVLCGVIGLQ KWQYDVWSHD
     VTLANHMEAG GVPGRVHITG ATLALLAGAY AVEDAGMEHR DPYLRELGEP TYLVIDPRAE
     EEDEKGTAGG LLSSLEGLKM RPSLLMTRYL ESWGAAKPFA HLSHGDSPVS TSTPLPEKTL
     ASFSTQWSLD RSRTPRGLDD ELDTGDAKFF QVIEQLNSQK QWKQSKDFNP LTLYFREKEM
     EKEYRLSAIP AFKYYEACTF LVFLSNFIIQ MLVTNRPPAL AITYSITFLL FLLILFVCFS
     EDLMRCVLKG PKMLHWLPAL SGLVATRPGL RIALGTATIL LVFAMAITSL FFFPTSSDCP
     FQAPNVSSMI SNLSWELPGS LPLISVPYSM HCCTLGFLSC SLFLHMSFEL KLLLLLLWLA
     ASCSLFLHSH AWLSECLIVR LYLGPLDSRP GVLKEPKLMG AISFFIFFFT LLVLARQNEY
     YCRLDFLWKK KLRQEREETE TMENLTRLLL ENVLPAHVAP QFIGQNRRNE DLYHQSYECV
     CVLFASVPDF KEFYSESNIN HEGLECLRLL NEIIADFDEL LSKPKFSGVE KIKTIGSTYM
     AATGLNATSG QDAQQDAERS CSHLGTMVEF AVALGSKLDV INKHSFNNFR LRVGLNHGPV
     VAGVIGAQKP QYDIWGNTVN VASRMESTGV LGKIQVTEET AWALQSLGYT CYSRGVIKVK
     GKGQLCTYFL NTDLTRTGPP SATLG
//