ID A0A2T7PMH3_POMCA Unreviewed; 617 AA.
AC A0A2T7PMH3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Guanylate cyclase soluble subunit beta-1 {ECO:0000256|ARBA:ARBA00039698};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
DE AltName: Full=Guanylate cyclase soluble subunit beta-3 {ECO:0000256|ARBA:ARBA00041698};
DE AltName: Full=Soluble guanylate cyclase small subunit {ECO:0000256|ARBA:ARBA00043208};
GN ORFNames=C0Q70_05878 {ECO:0000313|EMBL:PVD34602.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD34602.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD34602.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD34602.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD34602.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the
CC biosynthesis of the signaling molecule cGMP.
CC {ECO:0000256|ARBA:ARBA00037442}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD34602.1}.
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DR EMBL; PZQS01000003; PVD34602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7PMH3; -.
DR STRING; 400727.A0A2T7PMH3; -.
DR EnsemblMetazoa; XM_025231922.1; XP_025087707.1; LOC112560236.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 6.10.250.780; -; 1.
DR Gene3D; 3.90.1520.10; H-NOX domain; 1.
DR Gene3D; 3.30.450.260; Haem NO binding associated domain; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR038158; H-NOX_domain_sf.
DR InterPro; IPR011644; Heme_NO-bd.
DR InterPro; IPR011645; HNOB_dom_associated.
DR InterPro; IPR042463; HNOB_dom_associated_sf.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45655:SF2; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-1; 1.
DR PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07700; HNOB; 1.
DR Pfam; PF07701; HNOBA; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT DOMAIN 462..596
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 407..434
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 617 AA; 69867 MW; 047DDE149AC9D074 CRC64;
MQKGTYNQES FVEEVCIDIR GDRLTNYSEN SGGFFLKPRD LYKNIRYEEG TAMMHHIQEE
AALEMEGHFL VRLVYDDALS YDLVGAASKI LKVPASDILE LFGQMFFDYC KESGYDKILQ
VLGSTTRDFL QNLDALHDHL SSIYPGMRAP SFRCSEREED GATILHYYSD RPGLEHIVIG
IVKAVAKELH SAEVHVEVIQ SKTDDCDHVQ FAITENGKDA YRRKADMEIC HEFLSDEPKI
SPATFCRAFP FHLMFGTDLR IHQAGTAITR VIPRVAQGCR ITDLFDMIRP HMDFEFSHIL
SHINTVFVLA TKPNVLGSTN TRKEVPEGEG VTSPRHQADR DASVMRLKGQ MIHVVEADSI
LFLCSPSVMN LDDLCRRGLF LSDIPLHDAT RDLVLLSEHF EAEYKLAQNL EILTEELQRT
YRELEDEKRK TDRLMYSILP PSVANELRHR RQVPAMKFKM VTILFSGIVG FSQFCAKNSE
THSAMKIVQL LNTVYTEFDK LLTPEKNANI YKVETVGDKY MVVSGLPVPC DDHARCIALL
ALDLMDFSAK LRDPNGEQII ITIGIHSGEV VTGVIGKKMP RYCLFGNTVN LTSRTETTGV
KGKINVSEYA YKLSKII
//
