ID   F5H4D1_HUMAN            Unreviewed;       734 AA.
AC   F5H4D1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   02-OCT-2024, entry version 87.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN   Name=ADCY7 {ECO:0000313|Ensembl:ENSP00000457409.2};
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|Ensembl:ENSP00000457409.2, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000457409.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11237011; DOI=10.1038/35057062;
RG   International Human Genome Sequencing Consortium;
RA   Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J.,
RA   Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K.,
RA   Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P.,
RA   McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J.,
RA   Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C.,
RA   Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J.,
RA   Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C.,
RA   Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I.,
RA   Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S.,
RA   Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S.,
RA   Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S.,
RA   Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A.,
RA   Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R.,
RA   Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A.,
RA   Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W.,
RA   Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T.,
RA   Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E.,
RA   Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B.,
RA   Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L.,
RA   Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y.,
RA   Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C.,
RA   Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W.,
RA   Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P.,
RA   Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M.,
RA   Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A.,
RA   Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A.,
RA   Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M.,
RA   Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R.,
RA   Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A.,
RA   Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J.,
RA   Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N.,
RA   Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L.,
RA   Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G.,
RA   Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R.,
RA   Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G.,
RA   Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W.,
RA   Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J.,
RA   Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M.,
RA   McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J.,
RA   Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E.,
RA   Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J.,
RA   Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F.,
RA   Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A.,
RA   Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K.,
RA   Shizuya H., Choi S., Chen Y.J.;
RT   "Initial sequencing and analysis of the human genome.";
RL   Nature 409:860-921(2001).
RN   [2] {ECO:0000313|Ensembl:ENSP00000457409.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496913; DOI=10.1038/nature03001;
RG   International Human Genome Sequencing Consortium;
RT   "Finishing the euchromatic sequence of the human genome.";
RL   Nature 431:931-945(2004).
RN   [3] {ECO:0000313|Ensembl:ENSP00000457409.2, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.R., Wu K., Yang J.,
RA   Dejong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [4] {ECO:0000313|Ensembl:ENSP00000457409.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2024) to UniProtKB.
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=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}.
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DR   EMBL; AC007597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF456186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001272986.1; NM_001286057.1.
DR   RefSeq; XP_016878387.1; XM_017022898.1.
DR   AlphaFoldDB; F5H4D1; -.
DR   SMR; F5H4D1; -.
DR   MassIVE; F5H4D1; -.
DR   PeptideAtlas; F5H4D1; -.
DR   ProteomicsDB; 26536; -.
DR   Antibodypedia; 28237; 191 antibodies from 28 providers.
DR   DNASU; 113; -.
DR   Ensembl; ENST00000566433.6; ENSP00000457409.2; ENSG00000121281.13.
DR   GeneID; 113; -.
DR   UCSC; uc002egb.3; human.
DR   CTD; 113; -.
DR   DisGeNET; 113; -.
DR   HGNC; HGNC:238; ADCY7.
DR   VEuPathDB; HostDB:ENSG00000121281; -.
DR   GeneTree; ENSGT00940000159096; -.
DR   OrthoDB; 3686360at2759; -.
DR   BioGRID-ORCS; 113; 18 hits in 1157 CRISPR screens.
DR   ChiTaRS; ADCY7; human.
DR   Proteomes; UP000005640; Chromosome 16.
DR   Bgee; ENSG00000121281; Expressed in granulocyte and 186 other cell types or tissues.
DR   ExpressionAtlas; F5H4D1; baseline and differential.
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:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR032628; AC_N.
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; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F5H4D1,
KW   ECO:0007829|ProteomicsDB:F5H4D1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        122..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        597..614
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        620..641
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        666..689
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          279..406
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          454..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  81478 MW;  F2FA68E3C5F2E504 CRC64;
     MPAKGRYFLN EGEEGPDQDA LYEKYQLTSQ HGPLLLTLLL VAATACVALI IIAFSQGDPS
     RHQAILGMAF LVLAVFAALS VLMYVECLLR RWLRALALLT WACLVALGYV LVFDAWTKAA
     CAWEQVPFFL FIVFVVYTLL PFSMRGAVAV GAVSTASHLL VLGSLMGGFT TPSVRVGLQL
     LANAVIFLCG NLTGAFHKHQ MQDASRDLFT YTVKCIQIRR KLRIEKRQQE NLLLSVLPAH
     ISMGMKLAII ERLKEHGDRR CMPDNNFHSL YVKRHQNVSI LYADIVGFTQ LASDCSPKEL
     VVVLNELFGK FDQIAKANEC MRIKILGDCY YCVSGLPVSL PTHARNCVKM GLDMCQAIKQ
     VREATGVDIN MRVGIHSGNV LCGVIGLRKW QYDVWSHDVS LANRMEAAGV PGRVHITEAT
     LKHLDKAYEV EDGHGQQRDP YLKEMNIRTY LVIDPRSQQP PPPSQHLPRP KGDAALKMRA
     SVRMTRYLES WGAARPFAHL NHRESVSSGE THVPNGRRPK SVPQRHRRTP DRSMSPKGRS
     EDDSYDDEML SAIEGLSSTR PCCSKSDDFY TFGSIFLEKG FEREYRLAPI PRARHDFACA
     SLIFVCILLV HVLLMPRTAA LGVSFGLVAC VLGLVLGLCF ATKFSRCCPA RGTLCTISER
     VETQPLLRLT LAVLTIGSLL TVAIINLPLM PFQVPELPVG NETGLLAASS KTRALCEPLP
     HLHTVFSRLN ELTS
//