ID   A0A3Q3XQQ3_MOLML        Unreviewed;       991 AA.
AC   A0A3Q3XQQ3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Guanylate cyclase {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000027721.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000027721.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC         Evidence={ECO:0000256|RuleBase:RU003431};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   AlphaFoldDB; A0A3Q3XQQ3; -.
DR   STRING; 94237.ENSMMOP00000027721; -.
DR   Ensembl; ENSMMOT00000028194.1; ENSMMOP00000027721.1; ENSMMOG00000020959.1.
DR   OMA; LYQGNHV; -.
DR   Proteomes; UP000261620; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 6.10.250.780; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR001170; ANPR/GUC.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920:SF500; GUANYLATE CYCLASE 2G; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00255; NATPEPTIDER.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293,
KW   ECO:0000256|RuleBase:RU003431};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..991
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018766414"
FT   TRANSMEM        459..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          518..809
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          828..957
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   991 AA;  110865 MW;  5FD04F598F3306AB CRC64;
     SHTFVLHLTL VATAATVVNN NGPQTHKLII GFQAPWNMTL PFSALRLGSA IQIAVEKVNT
     SPSFLGNYSL DFVFIDTDCN PKVSLGGFIH QVWKENVSAL FGPACPEEAE VTGLIASTWN
     IPMFGFVGQS SKMDNSDIYD SYIKIVPPLK RSAEVLVKTL EFFGWSHIAI IGGGLESNTW
     DKVDALWTTV ENPLTAKFKL VATVKFDTSN PQLVYQNIRY IATVARIVVL TNKEDSLALL
     QEAERQGLMN GEYVFFLVQH FEVSGNVDNL WKNALNSRID QGATTAFDMA FIIGQKSYEG
     QEYFDFFEQV FERLKGPPFR SNLTSEREAQ APVSPYSAYL HDAVLLYAMG LKEVLKDGKD
     PRNGRLLLQR LKNKNSIQFN ASGLVDFDED GERNLDYYIY DLQHMGDVTK FVPVLHYDSQ
     TKAVPTSMFA SVVWPKGRPP SDKPECGFDN ELCKWLSNIA LFTLLVAFPV IGVLAVLCIG
     VLVLQKLRLQ TRLDDSCWWL ISYGDITIIR ESPGVVGLSL STTVSQGGSG GSQSNFSTNS
     YGLKDKTGRE SVYTTIGLYQ GNQVAIKYIK NPVSSYIQKP SMITEFNMMK EMKHENLVQF
     FGVCIESPNI CLVMQYCRKG SLKDVLRSSD MELDGIFKLS FAYDIVNGMD FIHKSSMRFH
     GNLKPSTCLV DSRLQIKLSG FGLWEFKYGG TNKIISVEKH NYSIIKQLRT PVHGEPVRPL
     LCEQLCDQTI NSLLTACWSE NPNHRLPFET IRRQLRDSSP GHANILDNMV EKLEKYANHL
     EEVVEERTNQ LTAEKTRADK LLSSMLPYIA DQLMAGKSVE PQSYDVVTIF FSDIVGFTSM
     CSISSAMEVV TFLNDLYSLF DDIIKLYDVY KVETIGDAYM VASGVPISNG NKHALEISTM
     ALHFLSSIKV FRIHHMPTES LAIRIGIHSP VVAGVVGTTM PRYCLFGDTV NMASRMESNS
     LLKIHISQHT ANILVQAGSF ELEERGEIEM K
//