ID W5M433_LEPOC Unreviewed; 1302 AA.
AC W5M433;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:ENSLOCP00000003141.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000003141.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000003141.1}
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: 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; AHAT01031917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01031918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000003148.1; ENSLOCP00000003141.1; ENSLOCG00000002667.1.
DR GeneTree; ENSGT00940000155577; -.
DR HOGENOM; CLU_001072_12_0_1; -.
DR Proteomes; UP000018468; Linkage group LG13.
DR Bgee; ENSLOCG00000002667; Expressed in zone of skin and 10 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016849; F:phosphorus-oxygen lyase activity; IEA:InterPro.
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; 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:UP000018468};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 129..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 805..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 834..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 883..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 907..927
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 934..956
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 995..1014
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 410..537
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1076..1216
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 143200 MW; 9195EDE6AA3A5CC2 CRC64;
MASPRHQPLL LRHTEVSCDA GGGGVAVKVN SSGGGKPPPP HPPPQHRGPA SGSAGGGGGS
KHIKYSISSS CSSGESGVRR AMVPGLRGQR KVPQLFERSA AQWWDPGFDS PILEDACRER
CFPQTQRRFR YVLSYLAAAG LLWGVYFGVN HDRCDPFAFL LPTAGFLAFC LALFLFTFTR
LYARLYPQVS LLLIVVTFAV TLAPQVQTAA FSQSQGREED PSGNRSNSSG GPPRPGKLCI
SPVGTFSLCM EVLLLLYSVL HLRLYASVLL GLGYSVLFEA LGCVYIAEDH PTLYWLAPGK
GLLHLCAHAI GIHLFIMSEV RSRSTFLKVG QAIMHGKDLE VEKALKERMI HSVMPRRVAD
ELMKQGDDES ETSVKRYSTS SPKSKKKKTS IPRGQIIFRP FNMKRMEPVS ILFADIVGFT
KMSANKSAHA LVGLLNDLFG RFDRLCEVTK CEKISTLGDC YYCVAGCPEP RADHAYCCIE
MGLGMIEAIE QFCQEKKEMV NMRVGVHTGT VLCGILGMKR FKFDVWSNDV NLANLMEQLG
VAGKVHISEV TAGFLDDRYE REDGRVLERV GQNVVADQLK GLKTYLISGQ RVEHSQCSCS
QLGLTGPDPG DGPAAAPRAQ SPDATPAAGP DSGLAHCQAD RAKVPCPSCS VVLIPSSELA
VEDGTVQNGC QEEHKNNAKV PSGRGPKAQN GLLSPPADDK MTNSQTSLCE MLQEKEKKWG
GVSMDHSALI PLRSKNFRER SDAHFVDVIK EDSLMKDYFF KPPINKLSLN FLEKPLESAY
RASYQEEVQT KAPVQTFASP TFSSFLDVLL SSAVFAALAV ACFLRPWVTG SPPPAAAIAV
CVLAVLLEGI SLVLSVRMAF YLDNVMSCTR QLLQVISGWI PRHLIGAVLI SLPALSVFTH
ITCQFHLSLQ FTMFICCAVI ITIIQYCNFC QLSFWMRSSF ATAVGAVLLA VLYTPLCARG
VGKPGKFQVA SKNSSDVVRV YFGGSPSDSL SAPAVALQDV SLAFFLLLLL VWFLNREFEV
SYRLHYHGNV EADQHRIKIQ NMRDQADWLL RNIIPIHVAE QLKVTQSYSK NHDNVGVIFA
SIVNFSEFYE ENYEGGKECY RVLNELIGDF DELLRKPAFG NIEKIKTIGA TYMAASGLNT
SQCQDSAHPH GHLRTLFDFA MEMMRVVDDF NKDMLWFNFK LRIGFNHGPL TAGVIGTTKL
LYDIWGDTVN IASRMDTTGV ECRVQVSEES YRVLKEMGYE FDYRGTVNVK GKGQMKTFLF
PKSVDSGMVP QHQLSVSPDI RVQVDGSIGR SPTDEIAGVV PS
//
