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Database: UniProt
Entry: G1PH49_MYOLU
LinkDB: G1PH49_MYOLU
Original site: G1PH49_MYOLU 
ID   G1PH49_MYOLU            Unreviewed;      1165 AA.
AC   G1PH49;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Adenylate cyclase type 6 {ECO:0000256|PIRNR:PIRNR039050};
DE            EC=4.6.1.1 {ECO:0000256|PIRNR:PIRNR039050};
GN   Name=ADCY6 {ECO:0000313|Ensembl:ENSMLUP00000009988.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000009988.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000009988.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000009988.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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; AAPE02023480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1PH49; -.
DR   STRING; 59463.ENSMLUP00000009988; -.
DR   Ensembl; ENSMLUT00000010961.2; ENSMLUP00000009988.2; ENSMLUG00000010943.2.
DR   eggNOG; KOG3619; Eukaryota.
DR   GeneTree; ENSGT00940000155687; -.
DR   HOGENOM; CLU_001072_2_0_1; -.
DR   InParanoid; G1PH49; -.
DR   OMA; RENHCLR; -.
DR   TreeFam; TF313845; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
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:0005080; F:protein kinase C binding; IEA:Ensembl.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0097746; P:blood vessel diameter maintenance; 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:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; IEA:Ensembl.
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:SF11; ADENYLATE CYCLASE TYPE 6; 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.
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:UP000001074};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        666..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        693..716
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        737..756
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        812..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        837..859
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        890..908
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          376..503
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          976..1115
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   BINDING         381..386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         381
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         381
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         382
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         423..425
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         425
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         425
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         469
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         1028
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         1102..1104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         1109..1113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT   BINDING         1149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
SQ   SEQUENCE   1165 AA;  130544 MW;  82624D75C0AF4327 CRC64;
     MSWFSGLLVP KVDERKTAWG ERNGQKRPRH RTRTSGFCAP RYMSCLRDAQ PPSPTPAAPP
     QCPWQEEAFI RRGGPSKGTE LGLRAVALGF DPETTVAVGV AEVAPDVAPR SRRSCWRRLV
     QVFQSKQFRS AKLERLYQRY FFQMNQSSLT LLMAVLVLLT AVLLAFHAAP ARPQPAYVAL
     LACAAVLFVV LMVVCNQHSF RQDSMWVVSY VVLGILAAVQ VGGALAANPH SPSAGLWCPV
     FFVYITYTLL PIRMRAAVFS GLGLSILHLI LAWQLNRGDA FLWKQLGANM LLFLCTNVIG
     ICTHYPAEVS QRQAFQETRG YIQARLHLQH ENRQQERLLL SVLPQHVAME MKEDINTKKE
     DMMFHKIYIQ KHDNVSILFA DIEGFTSLAS QCTAQELVMT LNELFARFDK LAAENNCLRI
     KILGDCYYCV SGLPEARTDH AHCCVEMGVD MIEAISLVRE VTGVNVNMRV GIHSGRVHCG
     VLGLRKWQFD VWSNDVTLAN HMERGARPGR IHITRATLQY LNGDYEVEPG HGGERNAYLK
     EQHIETFLIL GTSQKRKEEK AMLAKLQRTR ANSMEGPMPR WVPDRAFSRT KDSKAFRQMG
     IDDSSKDNRG AQDALNPEDE VDEFLGRAID ARSIDQLRKD HVRRFLLTFQ REDLEKKYSQ
     KVDPRFGAYV ACALLVFCFI CFIQLLIFPH STLMLGLYVG IFLLLLITVL ICAVYSCGSI
     FPEALQRLSR SIVRSRAHST AVGIFSVLLV FTSAIANMFT CNHTPIRTCA ARILNVTPAD
     VTACHLQQLN YSLGLDTPLC EGTAPTCSFP EYFVGNMLLS LLASSVFLHI SSIGKLAMIF
     VLGLIYLVLL LLGPPATIFD NYDLLLGVHG LASSNETIDG LDCPAAGRVA LKYMTPVILL
     VFALALYLHA QQVESTARLD FLWKLQATGE KEDMEELQAY NRRLLHNILP KDVAAHFLAR
     ERRNDELYYQ SCECVAVMFA SIANFSEFYV ELEANNEGVE CLRLLNEIIA DFDEIISEER
     FRQLEKIKTI GSTYMAASGL NASTYDQVGR SHITALADYA MRLMEQMKHI NEHSFNNFQM
     KIGLNMGPVV AGVIGARKPQ YDIWGNTVNV SSRMDSTGVP DRIQVTTDLY QVLAAKGYQL
     ECRGVVKVKG KGEMTTYFLN GGPSS
//
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