ID C3ZFB1_BRAFL Unreviewed; 938 AA.
AC C3ZFB1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 99.
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};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_206552 {ECO:0000313|EMBL:EEN49417.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN49417.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN49417.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN49417.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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 EMBL; GG666612; EEN49417.1; -; Genomic_DNA.
DR RefSeq; XP_002593406.1; XM_002593360.1.
DR AlphaFoldDB; C3ZFB1; -.
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; C3ZFB1; -.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0016941; F:natriuretic peptide receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR CDD; cd07302; CHD; 1.
DR CDD; cd06352; PBP1_NPR_GC-like; 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; 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:SF335; GUANYLATE CYCLASE 32E; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 348..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 398..677
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 751..880
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 686..724
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN49417.1"
SQ SEQUENCE 938 AA; 106314 MW; 29E1E5CD87E12B78 CRC64;
FIGPTCSQVC RPVANLAAYW NLPVFTPLCN AIDMHDKQHF STLVRFFGPA ITWGSFYVGI
CRRFGWNRFA VVSHWDIGWT IPAYGIVEYA EELNMTVPSY HVLSPDDSLE KVLTQATRRA
RIILLSGPGY LIRRLMLTAH DLGLTGGDHV FFCLRYFRHD EIFGNFSWKT GDSRDADARE
AYKSLFVLSL YRPENDVSRA FSRDVRRRSR ETFSYEFHPD EEVSVMAAIA YDTVHIYAHA
LNETLAFGED PYDGRRLAER VRNRTFEGVQ GWVTLDNNGD RETNYMMYSF QDGKMKAVGY
YFGHSGEYED VPGTMITWPA GGLTPPPDAP YCGFDEEKYL RHSRYGPIYT LGLALILPII
FLLVGYTIYH RHTVEKKVAF KTCQLRSQDI MPIRTRSATP RNSISTGQEN SSCKLAEYKV
GQIMCTMSVL VFYVIKELRV DGNRATMKRG IQKELTQLCE LNHPNLARIV GACLEAPNCC
VLIDHCSKGS LQDILKNESI KLDWTFRWSL IMDIVKGLEY LHNSFLKCHG SLKSTNCVVD
SRFVVKITDF GLWMLRKKKR ISMEEPKFLI CSDQLWTAPE ILRGGTERSQ KADVYSFALI
LHEIAFRKGV FYQEGSQLSP KDIITRVALS LSGVPFRPTI LEKDCPAGLS GLIKQCWAET
PEDRPDCKVI GAAVRRISGM KSENILDNLL ARMEHYADNL ESLVQEKTAQ VLDEKKRAED
LLERLLPRSD SILFSCCDGG TVHPESFDSV TVFFSDIVGF TAMSADSSPM EVVDMLNDLY
TCFDDIIGNY DVYKVETIGD AYVVVSGLPE RNSTHAAEIA RMALEMLRAV QTFRIRHRTS
EQLKLRIGIH TGPCAAGVVG RKMPRYCLFG DTVNTASRME TYGMALRIHV SETTYQALCL
TERFLLEARG ELEIKGKGPQ RTYWLLGEKG GIAKESFV
//
