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Database: UniProt
Entry: A8X8R7_CAEBR
LinkDB: A8X8R7_CAEBR
Original site: A8X8R7_CAEBR 
ID   A8X8R7_CAEBR            Unreviewed;      1104 AA.
AC   A8X8R7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 118.
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};
GN   Name=Cbr-gcy-6 {ECO:0000313|EMBL:CAP29028.2};
GN   ORFNames=CBG09580 {ECO:0000313|WormBase:CBG09580}, CBG_09580
GN   {ECO:0000313|EMBL:CAP29028.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP29028.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP29028.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP29028.2,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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:ARBA00001436,
CC         ECO:0000256|RuleBase:RU003431};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; HE600998; CAP29028.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8X8R7; -.
DR   STRING; 6238.A8X8R7; -.
DR   WormBase; CBG09580; CBP40393; WBGene00031141; -.
DR   eggNOG; KOG1023; Eukaryota.
DR   HOGENOM; CLU_001072_1_3_1; -.
DR   InParanoid; A8X8R7; -.
DR   OMA; GFLHCDV; -.
DR   OrthoDB; 2877804at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
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:0001653; F:peptide receptor activity; 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; IPR011645; HNOB_dom_associated.
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:SF76; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-6; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07701; HNOBA; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549};
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..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1104
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002730219"
FT   TRANSMEM        484..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          558..850
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          908..1038
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   1104 AA;  124715 MW;  6422F4DFB598367A CRC64;
     MHPTTAVLLF LATVDCQPPG NIFHLGFLHC DVLQKNVEGS SPYISYRTSA SAASIAIDRI
     KRENRLTGYD FKFTILYDQC DENLAAGNAI KLFRDYNYCF ISAAIPVFTL ATYYNTPIVT
     WGMTSSATLD DASRYPTAGI ISIGSRRHRY FSLAVTFREV MLEYGWDQFV YAYSLEGDDE
     KCETMRDDFQ NMIAYYGDIV LSYTIQIMDH SEAGLLAVLK DVSTRGRIIV PCFHEGNTRG
     LHRRWMLVAA RNGFVTDEYV YIIPSLRSKG YAIQQDDGSY RYPWVDSTGP QPSDHEAIPG
     FQRSIFIVDM QGQGKIGSNY SVFEDEVIRR MKQPPYNCTE ACSAQEYQHA ATYAGQLHDA
     VYLYGLAMER VLITAPTQYR NGTQFGFLEN IFSGHHNLGV GGPIVIDDSG GRSPTLFVLT
     LDANNTSSII MTVDVDQQSA EVTKLYSNEA TAVWYHRKGI RPPDEPVCGY TGSKCPANVF
     YENMGWFIAA IIVILLTILG AILAFVYLFY AKRQEVERQN ALWQIPYKSM MTVAKKGKGE
     HSMRSISSVP STISSTRSST LSEVGETRNY LFFQIQNEVE IEKVAARKYT IRTLFDNKIC
     ANMRQMRLID HSNLNKFIGM SLDAPQLLSV WRFCSRGSLA DVIRKASLQM DGFFIYSLMK
     DIVNGLTWIH DSSHEYHGML TSKNCLLNDR WQLKITDFGL RNFRTHDQYT KMGELLEILY
     FSEVFKFSDR LWTAPELLRN DDIMGSREGD VYSLGIISAE LITRSSVFDL ENRKEDAEEI
     VYMLKKGGLQ SPRPHLDHDE SIEINPGLLH LVRDCWTERP SERPDIKQVA SQLRSMNTNR
     NDNLMDHVFN VLESYASTLE DEVAERMKEL VEEKKKSDVL LYRMLPKQVA DKLKLGQTVE
     PETFDVVTLF FSDVVSFTTL AGKCTPLQVV NLLNGLYTIF DGIIEQHDVY KVETIGDGYF
     VASGVPRRNG NEHTRNIASM SLCFVKSLAD FNIPHLPGEK INIRVGFHCG SVVAGVVGLT
     MPRYCLFGDA VNTASRMESN SKPSCSNFSA GHVHISDEAN RMLMTLGGFT TETRGEVIIK
     GKGVMTTYWL LKMDESAAPK NLKK
//
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