ID M3YUB1_MUSPF Unreviewed; 1352 AA.
AC M3YUB1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN Name=ADCY9 {ECO:0000313|Ensembl:ENSMPUP00000014921.1,
GN ECO:0000313|RefSeq:XP_004750592.1, ECO:0000313|RefSeq:XP_012910485.1,
GN ECO:0000313|RefSeq:XP_044928082.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000014921.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000014921.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004750592.1, ECO:0000313|RefSeq:XP_012910485.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004750592.1,
RC ECO:0000313|RefSeq:XP_012910485.1};
RG RefSeq;
RL Submitted (NOV-2023) 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=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; AEYP01027760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01027761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01027762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01027763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004750592.1; XM_004750535.3.
DR RefSeq; XP_012910485.1; XM_013055031.2.
DR RefSeq; XP_012910486.1; XM_013055032.1.
DR RefSeq; XP_044928082.1; XM_045072147.1.
DR STRING; 9669.ENSMPUP00000014921; -.
DR Ensembl; ENSMPUT00000015158.1; ENSMPUP00000014921.1; ENSMPUG00000015032.1.
DR GeneID; 101680942; -.
DR KEGG; mpuf:101680942; -.
DR CTD; 115; -.
DR eggNOG; KOG3618; Eukaryota.
DR GeneTree; ENSGT00940000155577; -.
DR HOGENOM; CLU_001072_12_0_1; -.
DR OMA; FTAMPPG; -.
DR OrthoDB; 3686360at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; 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; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF8; ADENYLATE CYCLASE TYPE 9; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
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};
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 Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 788..809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 821..845
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 866..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 890..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 976..995
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 394..521
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1057..1197
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1333..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1352 AA; 150469 MW; 0E6E4EA24984BF5D CRC64;
MASPPHQQLL PHHSTEVSCD SSGDSNSVRV KINPKQLSSN SHPKHCKYSI SSSCSSSGDS
GGVPRRVGAG GRLRRQKKLP QLFERASSRW WDPKFDSVNL EEACMERCFP QTQRRFRYAL
FYIGFACLLW SIYFGVHMRS KLMVMVAPAL CFLVVCVGFF LFTFTKLYAR HYVWTSLVLT
LLVFALTLAA QFQVLTPLSG RADSFNRTLA AKPTDTCLSQ VGSFSMCIEV LFLLYTVMHL
PLYLSLFLGV VYSVLFETFG YHFRDKDCFP PPGAWAPHWE LLSRALLHVC IHAIGVHLFI
MSQVRSRSTF LKVGQSIMHG KDLEVEKALK ERMIHSVMPR IIADDLMKQG DEESENSVKR
HATSSPKNRK KKSSIQKAPI AFRPFKMQQI EEVSILFADI VGFTKMSANK SAHALVGLLN
DLFGRFDRLC EETKCEKIST LGDCYYCVAG CPEPRADHAY CCIEMGLGMI RAIEQFCQEK
KEMVNMRVGV HTGTVLCGIL GMRRFKFDVW SNDVNLANLM EQLGVAGKVH ISEATAKYLD
DRYEMEDGKV TERLGQSVVA DQLKGLKTYL IAGQRAKESH CSCSEALLSG FEVIDGSRVS
SGPRGQGTAS PGSVSDLAQT VKTFDNVKTC PSCGITFAPK SEAGAEGGAV QNGCQEEHKN
STKAPGAPNS KTQNGLLSPP QEEKLTNSQT SLCEILQEKG RWAGVSLDQS ALLPLRFKNI
REKTDAHFVD VIKEDSLMKD YFFKPPINQF SLNFLDQELE RSYRTSYQEE VIKNSPVKTF
ASATFSSLLD VFLSTTVFLI LSITCFLKYG AASMSPPPAA LAVFGAALLL EVLSLVVSIR
MVFFLEDVMA CTKRLLEWIA GWLPRHFIGA ILVSLPALAV YSHVTSEFET NIHVTVFMGS
AVLITVVHYC NFCQLSSWMR SSLATVVGAG PLLLLCISLC PDSSIVISHL DAGQNFSSEG
NPCNSSLPHG GGTASLIGQE VVLVFFLLLL LVWFLNREFE VSYRLHYHGD VEADLHRTKI
QSMRDQADWL LRNIIPYHVA EQLKVSQTYS KNHDSGGVIF ASIVNFSEFY EENYEGGKEC
YRVLNELIGD FDELLSRPGY SSIEKIKTIG ATYMAASGLN GAQCQDGGHP QEHLQVLFEF
AKEMMRVVDD FNSNMLWFNF KLRVGFNHGP LTAGVIGTTK LLYDIWGDTV NIASRMDSTG
VECRIQVSEE SYRVLSKMGY DFDYRGTVNV KGKGQMKTYL YPKCMDSGAV PQHQLSISPD
IRVQVDGSIG RSPTDEIANL VPSVQNADKT SLGSENNMQA KDTHLSSKRP WKEPVKPEER
SRFGKAIEKS DCEEVGMEEA SELTRLNVSK SV
//
