ID A8WVP6_CAEBR Unreviewed; 1095 AA.
AC A8WVP6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 123.
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=gcy-17 {ECO:0000313|WormBase:CBG03898};
GN Synonyms=Cbr-gcy-17 {ECO:0000313|EMBL:CAP24709.1};
GN ORFNames=CBG03898 {ECO:0000313|WormBase:CBG03898}, CBG_03898
GN {ECO:0000313|EMBL:CAP24709.1};
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:CAP24709.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP24709.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP24709.1,
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; HE600906; CAP24709.1; -; Genomic_DNA.
DR RefSeq; XP_002639322.1; XM_002639276.1.
DR AlphaFoldDB; A8WVP6; -.
DR EnsemblMetazoa; CBG03898.1; CBG03898.1; WBGene00026663.
DR WormBase; CBG03898; CBP14936; WBGene00026663; Cbr-gcy-17.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; A8WVP6; -.
DR OMA; FRISHMP; -.
DR OrthoDB; 2875278at2759; -.
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; 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; 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:SF363; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-17; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1095
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002732103"
FT TRANSMEM 479..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 642..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 488..823
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 881..1011
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1073..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 123187 MW; 71969C554735E25B CRC64;
MIQRLLIIIF TTFLVLTQCQ VRQTLKVGLI FVQNVTNLQV AIGYRTSASA VLVTKEKIRE
EHLLDNFDFE FIYDFDECNE IQAAGKTVDL LVNKRVDVIF GPTCSRSGMI SSTLAAQYNI
PIFEWGLTSA RQLTDVVRYP TSLPFSVNSY SLAMAIRGTL KQFEWTEFVF MYCNDGDDEK
CESLKDDIQT VASQHSDITL AYTTRIMTGS LSDMRTAIRD IKKRGRIIVA CVASGNGSKR
TLMQAASLEE ANNSEYVYIM AETNSRGFIV DEPGGKWHYL WEGVFNDSAS FTSEDSRQSM
ANLLFLVDNM GMNDEVTPQY LNFSRKVIEM MKDPPFNCIE DCAGEQYSSV AKYAGQLADA
FYAYAVALNR SLTSNPYADI RNGTMILGNI GMTFEGVGGG DVTVDPDSSR TSVITMIGLN
SSKLPETYGR FVINNQSIDF EPLYANEMYD VWNGRERPKV KPICGFTGNQ CPPNFVRDYL
AFVAIIAVFL VFAIGAAIGG VFYAIKQKQR EIERQDELWH VDVGHLQIIP KKSKSEASQR
SFASGPSTST KLTLESRTET NRFSFYLYKN EMVAANKHNA RPSLTEQERY QLRQMRSLDH
DNINKFIGLC LNGPQLMSVY RYCSRGSLAD VIERSSMQMD AFFMFSLIHD IANGLAFIHS
SILHLHGYLS SKNCLIDDRW QVKISSFGIP MIRQSDEVSK KGMLWSAPEV LRNETEERTQ
EGDIYSFGII CSEIITRSSA FDIENRKEKP EEIIYQLKKG GFNAIRPSLL TDESLEINPA
LTHLIRDCWT EKPSERPPID QVKSLLKGMN DGKKVNLMDH VFNMLEAYAS NLEDEVSERT
KELVEEKKKS DLLLYRMLPK TVADKLKSGL SIQPETFELV TIFFSDVVQF TVLAGKCTPL
QVVQLLNDLY TIFDSIIEQH DVYKVETIGD GYLCVSGLPH RNGNEHIRHI ARMSLAFLSS
LAKFRISHMP NERINLRIGI NCGSVVAGVV GLTMPRYCLF GDAVNTASRM ESNGKPGRIH
VSSEANRLLT KVVGGFRTEA RGEVIIKGKG VMETFWLLEE NGSDPMKSLL KKERKNSTTS
SQARSVTPTM DGFSL
//
