ID A0A3P9PVH9_POERE Unreviewed; 1083 AA.
AC A0A3P9PVH9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Guanylate cyclase {ECO:0000256|RuleBase:RU003431};
DE EC=4.6.1.2 {ECO:0000256|RuleBase:RU003431};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000025912.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000025912.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000025912.1};
RG Ensembl;
RL Submitted (SEP-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|ARBA:ARBA00036920};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC Evidence={ECO:0000256|ARBA:ARBA00036920};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR RefSeq; XP_008413773.1; XM_008415551.2.
DR RefSeq; XP_008413774.1; XM_008415552.2.
DR STRING; 8081.ENSPREP00000025912; -.
DR Ensembl; ENSPRET00000026170.1; ENSPREP00000025912.1; ENSPREG00000017465.1.
DR GeneID; 103468453; -.
DR KEGG; pret:103468453; -.
DR CTD; 572052; -.
DR GeneTree; ENSGT00940000155955; -.
DR OMA; ANYNWFN; -.
DR OrthoDB; 3683909at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma 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; 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; 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; GUANYLYL CYCLASE; 1.
DR PANTHER; PTHR11920:SF347; GUANYLYL CYCLASE C; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1083
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018100115"
FT DOMAIN 473..748
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 823..953
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 410..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 124107 MW; E54B3F1C7618901F CRC64;
MRSWDCLLYL GVLGALGLMA SGHTMLDDCL ASNRKYKMNV VVLEDNNYEW SRPFVQKAVE
QAIEKDRQKN IGNDLDLVLT ANYNGFNTTV YNRQGCGSST CEGVAILKRL VRSNEVGCIM
LGPSCTFATF QLVDEEIGLT LSIPIISAGS FGLSCDYKPK LTRTLPPARK IIDLFLNFKT
EELRFKPEWE KFYVYKKQVN NATEDCFWYI NALEAPSARF ASQTQRVMVR EKXDLQRILK
TSNRHSNIII LCGGPEEISL IKEDVDQIHP DTLFILLDLF NPEYHVNETA HELMEDVLVV
TLPPRNYSYN SNSSYNDTIN DYVAGYHDGA LLFGQVLRDR LMSSEAGRKS EVVNYNPFAN
VTIEGLAGHV VLDEHGDRDV NFSFIYTSVK TGKYETLLVF DSSQNRTIET HPNPALGWKG
QLPDDEPENP EDLGTQDVIV IVLGVSVVVV TAIALIFYRQ NRKERLMQKK WSHMSPHLIG
PLDEKEVSLK IDDDKRKDST YFRQRGCYDK KPVILKELKN AGDFTEEQKI ELNTLLRIDY
YNLTKFYGTV KFEYGVFGVF ELCQRGSLRY ILSDRISYPD ETFMDMEFKI SVMYDIAKGM
SYLHSSSIPV HGRLKSTNCV VDNRMVVKIT DFGCHTILMP GRDLWTAPEH LRKDGVSQKG
DVYSYGIIAH EIVLRQTPFY TRSCFNTTEK LHRIQYPRGN GFFRPDLYFE GISDREIELY
MLIKSCWDED PERRPDFKRI ELTLGKIFSN LHNQATETYM DNLIRRLQMY SRTLECLVEE
RTALYKAERD RADRLNFMLL PGPVVRSLKE TGRVEPELFE EVTIYFSDIV GFTTLCHYST
PMEVVDMLNE IYKNFDSILD HHDVYKVETI GDAYMVASGL PKRNGDRHAV DIAHMALDLL
SFVGTFELQH LPGIPLWIRI GVHSGPCAAG VVGNKMPRYC LFGDTVNTAS RMESTGLPLR
IHASQSTINI LRRTDCQFEF EKRGETYLKG KGKEMTYWLT GVTGRTYNLP TPPTAENFQR
LQQDLADMIV SSLEKHRAGR EGFEKRKTLS TRVRCRDTNN SLRKDSPPEY FHLAVTDNPS
TFL
//
