ID Q6RSD4_MOUSE Unreviewed; 781 AA.
AC Q6RSD4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE Flags: Fragment;
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|EMBL:AAR88429.1};
RN [1] {ECO:0000313|EMBL:AAR88429.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/SvEv {ECO:0000313|EMBL:AAR88429.1};
RX PubMed=17135423; DOI=10.1523/JNEUROSCI.1040-06.2006;
RG World Health Organization/International Society for Biomedical Research on Alcoholism Study on State and Trait Markers of Alcohol Use and Dependence Investigators;
RA Hines L.M., Hoffman P.L., Bhave S., Saba L., Kaiser A., Snell L.,
RA Goncharov I., LeGault L., Dongier M., Grant B., Pronko S., Martinez L.,
RA Yoshimura M., Tabakoff B.;
RT "A sex-specific role of type VII adenylyl cyclase in depression.";
RL J. Neurosci. 26:12609-12619(2006).
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|ARBA:ARBA00001946};
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; AY494946; AAR88429.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6RSD4; -.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:InterPro.
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; 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; PF06327; Adcy_cons_dom; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..90
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 580..724
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 138..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAR88429.1"
SQ SEQUENCE 781 AA; 87001 MW; 2BE44E5D1AC60133 CRC64;
ANECMRIKIL GDCYYCVSGL PVSLPTHARN CVKMGLDICE AIKQVREATG VDISMRVGIH
SGNVLCGVIG LRKWQYDVWS HDVSLANRME AAGVPGRVHI TEATLNHLDK AYEVEDGHGE
QRDPYLKEMN IRTYLVIDPR SQQPPPPSHH LSKPKGDATL KMRASVRVTR YLESWGAARP
FAHLNHRESV SSSETPISNG RRQKAIPLRR HRAPDRSASP KGRLEDDCDD EMLSAIEGLS
STRPCCSKSD DFHTFGPIFL EKGFEREYRL VPIPRARYDF ACASLVFVCI LLVHLLVMPR
MATLGVSFGL VACLLGLVLS FCFATEFSRC FPSRSTLQAI SESVETQPLV RLVLVVLTVG
SLLTVAIINM PLTLNPGPEQ PGDNKTSPLA AQNRVGTPYE LLPYYTCSCI LGFIACSVFL
RMSLELKAML LTVALVAYLL LFNLSPCWHV SGNSTETNGT QRTRLLLSDA QSMPSHTLAP
GAQETAPSPS YLERDLKIMV NFYLILFYAT LILLSRQIDY YCRLDCLWKK KFKKEHEEFE
TMENVNRLLL ENVLPAHVAA HFIGDKAAED WYHQSYDCVC VMFASVPDFK VFYTECDVNK
EGLECLRLLN EIIADFDELL LKPKFSGVEK IKTIGSTYMA AAGLSAPSGH ENQDLERKHV
HIGVLVEFSM ALMSKLDGIN RHSFNSFRLR VGINHGPVIA GVIGARKPQY DIWGNTVNVA
SRMESTGELG KIQVTEETCT ILQGLGYSCE CRGLINVKGK GELRTYFVCT DTAKFQGLGL
N
//
