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Database: UniProt
Entry: G1KKR2_ANOCA
LinkDB: G1KKR2_ANOCA
Original site: G1KKR2_ANOCA 
ID   G1KKR2_ANOCA            Unreviewed;       789 AA.
AC   G1KKR2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 74.
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:ENSACAP00000010795.3};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000010795.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000010795.3, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000010795.3,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000010795.3}
RP   IDENTIFICATION.
RG   Ensembl;
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: 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; G1KKR2; -.
DR   STRING; 28377.ENSACAP00000010795; -.
DR   Ensembl; ENSACAT00000011018.3; ENSACAP00000010795.3; ENSACAG00000010774.3.
DR   eggNOG; KOG3619; Eukaryota.
DR   GeneTree; ENSGT00940000158054; -.
DR   HOGENOM; CLU_001072_2_5_1; -.
DR   TreeFam; TF313845; -.
DR   Proteomes; UP000001646; Chromosome 1.
DR   Bgee; ENSACAG00000010774; 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; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IBA:GO_Central.
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; 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; 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:UP000001646};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        293..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        441..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        512..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..128
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          599..738
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   789 AA;  88543 MW;  513250E8790E53FB CRC64;
     SILFADIEGF TSLASQCTAQ ELVMTLNELF ARFDKLAAEN HCLRIKILGD CYYCVSGLPE
     ARADHAHCCV EMGMDMIEAI SLVREVTGVN VNMRVGIHSG RVHCGVLGLR KWQFDVWSND
     VTLANHMEAG GKAGRIHITK ATLNYLNGDY EVELGFGGER NAYLKEHSIE TFLIVRCSQK
     RKEEKATIAK MNRQRTNSIG HNAPHWGVDR SFYNHLGSNQ VSKEMKRMGF EDPNNKNIQE
     NMNPEDEVDE FLGRAIDARS IDRLRSEHVR KFLLTFRELD LEKKYSKQVD DRFGAYVACA
     SLVFLFICFV QITIVPHSVF MLAFYLTCFV ILTTVVFVSV IYSCVKLFPA PLQTLSRKIV
     QSRTNNTIVG VFTIVLVFFS AFANMFTCST VDLLHCVAEE YNITPHEVDM CHINDFASNY
     SLGTAQGLCA GSQPSCNLND VLLSLLACSV FLQISCIGKL ILMLIIEFIY VLIVEVPGLT
     LFDNADLLVT ANAVIEEGNS GTGAIPPSVS RVALKIVTPV VITVFVLAVY LHAQQVESTA
     RLDFLWKLQA TEEKEEMEEL QAYNRRLLHN ILPKDVAAHF LAQERRNDEL YYQSCECVAV
     MFASICNFSE FYVELEANNE GVECLRLLNE IIADFDEIIS EDQFRQLEKI KTIGSTYMAA
     SGLNDTTYDK VGKTHIKALA DFAMKLMDQM KYINEHSFNN FQMKIGLNAG PVVAGVIGAR
     KPQYDIWGNT VNVASRMDST GVPDRIQVTT DMYQVLIVNN YQLECRGVVK VKGKGEMTTY
     FLNEGPSAS
//
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