ID   B7Z2C7_HUMAN            Unreviewed;       978 AA.
AC   B7Z2C7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=adenylate cyclase {ECO:0000256|PIRNR:PIRNR039050};
DE            EC=4.6.1.1 {ECO:0000256|PIRNR:PIRNR039050};
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:BAH11813.1};
RN   [1] {ECO:0000313|EMBL:BAH11813.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Amygdala {ECO:0000313|EMBL:BAH11813.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC       projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {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; AK294565; BAH11813.1; -; mRNA.
DR   RefSeq; NP_899200.1; NM_183357.2.
DR   AlphaFoldDB; B7Z2C7; -.
DR   PeptideAtlas; B7Z2C7; -.
DR   DNASU; 111; -.
DR   GeneID; 111; -.
DR   KEGG; hsa:111; -.
DR   CTD; 111; -.
DR   OrthoDB; 3686360at2759; -.
DR   BioGRID-ORCS; 111; 12 hits in 1149 CRISPR screens.
DR   GenomeRNAi; 111; -.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.
DR   CDD; cd07556; Nucleotidyl_cyc_III; 1.
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:SF7; ADENYLATE CYCLASE TYPE 5; 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; B7Z2C7; HS.
PE   2: Evidence at transcript 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
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   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR039050,
KW   ECO:0000256|PIRSR:PIRSR039050-50};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        17..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        478..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        505..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        551..572
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        626..644
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        651..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        701..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          186..313
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          788..927
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   BINDING         191..196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         191
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         191
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         192
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         233..235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         235
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         235
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         279
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         840
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         914..916
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         921..925
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         961
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
SQ   SEQUENCE   978 AA;  110064 MW;  1FF7FB611BD419A8 CRC64;
     MAVLCNRAAF HQDHMGLACY ALIAVVLAVQ VVGLLLPQPR SASEGIWWTV FFIYTIYTLL
     PVRMRAAVLS GVLLSALHLA IALRTNAQDQ FLLKQLVSNV LIFSCTNIVG VCTHYPAEVS
     QRQAFQETRE CIQARLHSQR ENQQQERLLL SVLPRHVAME MKADINAKQE DMMFHKIYIQ
     KHDNVSILFA DIEGFTSLAS QCTAQELVMT LNELFARFDK LAAENHCLRI KILGDCYYCV
     SGLPEARADH AHCCVEMGMD MIEAISLVRE VTGVNVNMRV GIHSGRVHCG VLGLRKWQFD
     VWSNDVTLAN HMEAGGKAGR IHITKATLNY LNGDYEVEPG CGGERNAYLK EHSIETFLIL
     RCTQKRKEEK AMIAKMNRQR TNSIGHNPPH WGAERPFYNH LGGNQVSKEM KRMGFEDPKD
     KNAQESANPE DEVDEFLGRA IDARSIDRLR SEHVRKFLLT FREPDLEKKY SKQVDDRFGA
     YVACASLVFL FICFVQITIV PHSIFMLSFY LTCSLLLTLV VFVSVIYSCV KLFPSPLQTL
     SRKIVRSKMN STLVGVFTIT LVFLAAFVNM FTCNSRDLLG CLAQEHNISA SQVNACHVAE
     SAVNYSLGDE QGFCGSPWPN CNFPEYFTYS VLLSLLACSV FLQISCIGKL VLMLAIELIY
     VLIVEVPGVT LFDNADLLVT ANAIDFFNNG TSQCPEHATK VALKVVTPII ISVFVLALYL
     HAQQVESTAR LDFLWKLQAT EEKEEMEELQ AYNRRLLHNI LPKDVAAHFL ARERRNDELY
     YQSCECVAVM FASIANFSEF YVELEANNEG VECLRLLNEI IADFDEIISE DRFRQLEKIK
     TIGSTYMAAS GLNDSTYDKV GKTHIKALAD FAMKLMDQMK YINEHSFNNF QMKIGLNIGP
     VVAGVIGARK PQYDIWGNTV NVASRMDSTG VPDRIQVTTD MYQVLAANTY QLECRGVVKV
     KGKGEMMTYF LNGGPPLS
//