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Database: UniProt
Entry: A0A2K6E0U1_MACNE
LinkDB: A0A2K6E0U1_MACNE
Original site: A0A2K6E0U1_MACNE 
ID   A0A2K6E0U1_MACNE        Unreviewed;       901 AA.
AC   A0A2K6E0U1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Adenylate cyclase type 5 {ECO:0000256|ARBA:ARBA00040910};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE   AltName: Full=ATP pyrophosphate-lyase 5 {ECO:0000256|ARBA:ARBA00042065};
DE   AltName: Full=Adenylate cyclase type V {ECO:0000256|ARBA:ARBA00042046};
DE   AltName: Full=Adenylyl cyclase 5 {ECO:0000256|ARBA:ARBA00041988};
GN   Name=ADCY5 {ECO:0000313|Ensembl:ENSMNEP00000041784.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000041784.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000041784.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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: 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|RuleBase:RU000405}.
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DR   AlphaFoldDB; A0A2K6E0U1; -.
DR   Ensembl; ENSMNET00000066283.1; ENSMNEP00000041784.1; ENSMNEG00000043685.1.
DR   GeneTree; ENSGT00940000158054; -.
DR   OMA; GSLWPNC; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000043685; Expressed in heart and 8 other cell types or tissues.
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-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; 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; 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   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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
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   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        384..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        411..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        457..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        528..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        553..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        624..643
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          92..219
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          711..850
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   901 AA;  101378 MW;  4D2CDAE3341F8A5D CRC64;
     LLVSNVLIFS CTNIVGVCTH YPAEVSQRQA FQETRECIQA RLHSQRENQQ QERLLLSVLP
     RHVAMEMKAD INAKQEDMMF HKIYIQKHDN VSILFADIEG FTSLASQCTA QELVMTLNEL
     FARFDKLAAE NHCLRIKILG DCYYCVSGLP EARADHAHCC VEMGMDMIEA ISLVREVTGV
     NVNMRVGIHS GRVHCGVLGL RKWQFDVWSN DVTLANHMEA GGKAGRIHIT KATLNYLNGD
     YEVEPGCGGE RNAYLKEHSI ETFLILRCTQ KRKEEKAMIA KMNRQRTNSI GHNPPHWGAE
     RPFYNHLGGN QVSKEMKRMG FEDPKDKNAQ ESANPEDEVD EFLGRAIDAR SIDRLRSEHV
     RKFLLTFREP DLEKKYSKQV DDRFGAYVAC ASLVFLFICF VQITIVPHSV FMLSFYLTCS
     LLLTLVVFVS VIYSCVKLFP PCDSLQEDRE RSKMNSTLVG CSPITLVFLA AFFTCNSKDL
     LGCLAQEHNI SASQVNACHV VESAVNYSLG DEQGFCGSPW PNCNFPEYFT YSVLLSLLAC
     SVFLQINCIG KLALMLAIEL IYVLIVEVPG VTLFDNADLL VTANAIPSPG SCENPRPRRM
     EAGTHFPSGA CPPPTRSPEH ATKVALKVVT PIIISVFVLA LYLHAQQVES TARLDFLWKL
     QATEEKEEME ELQAYNRRLL HNILPKDVAA HFLARERRND ELYYQSCECV AVMFASIANF
     SEFYVELEAN NEGVECLRLL NEIIADFDEI ISEDRFRQLE KIKTIGSTYM AASGLNDSTY
     DKVGKTHIKA LADFAMKLMD QMKYINEHSF NNFQMKIGLN IGPVVAGVIG ARKPQYDIWG
     NTVNVASRMD STGVPDRIQV TTDMYQVLAA NTYQLECRGV VKVKGKGEMM TYFLNGGPPL
     S
//
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