ID M3ZGP0_XIPMA Unreviewed; 1297 AA.
AC M3ZGP0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000001382.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000001382.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000001382.2};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014328051.1; XM_014472565.1.
DR STRING; 8083.ENSXMAP00000001382; -.
DR Ensembl; ENSXMAT00000001385.2; ENSXMAP00000001382.2; ENSXMAG00000001325.2.
DR GeneID; 102225745; -.
DR KEGG; xma:102225745; -.
DR eggNOG; KOG3619; Eukaryota.
DR GeneTree; ENSGT00940000159445; -.
DR HOGENOM; CLU_001072_2_5_1; -.
DR InParanoid; M3ZGP0; -.
DR OMA; KWRTKMP; -.
DR OrthoDB; 4175924at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; 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; 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; 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:UP000002852};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 269..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..872
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 899..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 945..965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 972..989
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1016..1033
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 524..651
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1099..1244
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 156..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1297 AA; 144797 MW; F40A453BFB3FE93D CRC64;
MPDESRTFPD EFRPRQEAAQ VALVPNIVVI SSDGKGKAST LELKRDGLKQ QDVPGGSLSG
LGASPVSVEL GEVKTAHVPE PLKAISLLRG REVSMDQESP VDPSGIKLQN DMNLPLQANS
CTDSDYSSTK SSPGYTCNGF GTDLYNGERL ELETRKLEKM SSVSPVNLSG TSLDSDKARK
SNLDFNRGDS MLDLTGKSKA ENSTNGSSPR SSVVRQNRDS MDVGSERYLE DDYVDRQSIR
SRRSVKEGVF CCYQATNRAF LRCVEETPAM LSGLLLSIIF CVVIIIVIAA TGRTEEPYLG
DHVGALSVVC VVLCLNVILL VCLPWVATVR RCGGALALFV WEMLYVTAMV FIFTGGEVNA
WEQVAFFLFL SLSVYTVLPL SLTWALIVGI GSSVSHIIII SVYVPVKNAN TRPNIPQLAE
QLVANAVLFV CVNCFGVFHL WMTENDLRAS NKKREEFSAV RSQKEVKKYQ QEGLLLSVLP
RYIAVELKSE VIRRLSKPKG DEAKETSNHP NFHSLYVRQH RDVSILYADI VGFTKLASTC
TPEELVAVLN KLFGKFDDIA KKNGCLRIKI LGDCYYCVSG LPDPIPTHAI NCVQMGLDMC
TAINELRRAT EVDINMRVGV HTGNVLSGVI GSQKWQYDVW SNDVTLANQM ESGGLPGRVH
ITEETLQHLN GAYEVEDGDG ESRNTHLNGR KTFLVIDPNK PSSVPRRPNL AAGENKQRAS
VRMSQYLKSW KNVHPFADLS NPQKKKPFKP LKGVIPRPRL TSTEETHFHN NPNRLSIDSS
IKGSLDTVDI AGRKVKKLNW LTLLFNDLCV EKQFRLSKVT NLHYSVSCIV IIFVTLFTVQ
MLVSEKNFQM AVSYGVTFPV MVALLVISFV AYMKKLHSKL PLNVQWVVKL SRNLLARAVL
RLFLVTLCIL ITLLMAILNL IVLPGRNCTS VTNTTYLGGQ RLYNLPYYLY CCLLAMLGVM
VFVRICFSVK GFLLTLAVVV YLALFLKVYE NESNCLVDVF YDTNHTHVGV LKDPQIMSGI
WLVIFYFVCL ILARRDELTC RVDFLLECCF QTEREEMETM ENVNKLLLQN VMPLHVASFF
MGKAVRNQDL YSESYECVCV LFASMPQFKE FYNESSANGD GLECLRFLNE IIVDFDDLLS
KPKFSSVEKI KTIGSTYMAA AGLRHSPVGE DNKKIDMTYT TVRTMVEFAI AMMRKLEKLN
QHSFNNFKLR IGANHGPVIA GVIGAHKPQY DIWGNSVNVA SRMESTGELD KLQVTEETSQ
IIQSVGYDVT LRGKVNVKGK GELTTYYVKT DHSTPQF
//
