ID A0A3Q1FH56_9TELE Unreviewed; 1301 AA.
AC A0A3Q1FH56;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000015222.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000015222.1}
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 STRING; 80966.ENSAPOP00000015222; -.
DR Ensembl; ENSAPOT00000033148.1; ENSAPOP00000015222.1; ENSAPOG00000018180.1.
DR GeneTree; ENSGT00940000159445; -.
DR InParanoid; A0A3Q1FH56; -.
DR OrthoDB; 4175924at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
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; 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; 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:SF6; ADENYLATE CYCLASE TYPE 2; 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 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:UP000257200};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 828..848
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 854..879
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 904..928
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 948..968
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 977..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1020..1037
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 527..654
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1103..1248
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1301 AA; 143364 MW; 10FC496B5A24ABBA CRC64;
MPDKSQGFQD KTRPGGEVSQ ASLVPDIIII SSDEEGQNGG GNILELDDLS HGPDKLKHSA
QSNSIDVLQG NDITGSLTAG DQSGCGVSQL PVEVGVAKTA QAPEPLKTNS LLKGTGVTSQ
STDAPVNSSS DSDYSSTKSS PGYVCTSFST DLCGDDLSEL DGSSFEKTNS ISAVNLSESS
LNTSYSDKTS KNIPDDHRDD SDRDLTDKSK PEVSPCGTSA VLPDFSPQVN QTRDSIDVRW
DEDDGDDDRR STRSRRSVKE GVCCCYQAFH RAFLRCVEET PAMLPGLVLS LLFCVAIIVL
IATTSDVAFH VGALSVVCVV LCLSAVLLVC LPWLATVRRC GGALALFVWG TLYITAIVFI
FTERPVTTWE QVAFFLFLSL SVYTVLPLSL AWALMVGVGT SVSHIIIISV YVPVTSPETP
DLAVQLVANA VLFVCVNCVG IFHLWMTEHD LRISNQKREE FSAIRSQKEI KKYQQEQLLL
SVLPRYIAME LKTEVIKRLS KPTGDKKNGS NFHNFHSLYI RQHKDVSILY ADIVGFTKLA
STCSPEELVA VLNKLFGKFD DLAKKNGCLR IKILGDCYYC VSGLPDPIPT HASNCVQMGL
DMCTNISKLR EATGVEISMR VGVHTGNVLC GVIGLQKWQY DVWSHDVTLA NHMESGGLPG
RVHITEETLQ HLNGAYQVED GDGGSRDPLL KGRKTYLVID PHKPDSISRR PKLAHSLASG
ENRQRASVRM SQYLQSWHSI HPFADLSNPD ATSKKPIVPS NAVMSQLCAE RPPLQSNPKF
LVVDNGVRGS LDTLDTAGRR AKKLNCLTLL FNDVSLEKQF RFSEVKGLHH SMSCIAVVFV
TLFIVQMLVS ERNFVMAVSY GATFPVLVLL LSIAFTGYLE KWRSKMPLSV QWISGLSRGV
STRAALRVFV VTFCVLIVLL MAILNFLFLP GNNCTSIANR TELEALKLYT VPYYLYCCLL
AMLGVIVFTR TCLSVKALLL TLAVVVYLAL FIHVYAPKSR CLINLLHNDT RPGVLQDPQI
MSGVWLVIFY IVCLILARQD ELGCRVDFLL ERCFQSEREE METMENVNRL LLQNVLPLHV
ACVFMGKTIR NQDLYSQSYD CVCVMFASVP QFKEFYSESS ANRDGLECLR FLNEIIADFD
ELLSKPKFCS VVKIKTIGST YMAAAGLTNS PPGDDRKKVD LSYSHVRSMV EFAIALMGKL
ELINTHSFNS FKLRIGINHG PVIAGVIGAH KPQYDIWGNS VNVASRMDST GVLDKIQVTE
ETAQMVQTVG YNVTLRGKVN VKGKGELTTY FVNTDQSSPQ F
//
