GCY7_CAEEL
ID GCY7_CAEEL Reviewed; 1111 AA.
AC H2L002; Q7JP50;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Receptor-type guanylate cyclase gcy-7 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-7 {ECO:0000312|WormBase:F52E1.4b};
GN ORFNames=F52E1.4 {ECO:0000312|WormBase:F52E1.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16099833; DOI=10.1073/pnas.0505530102;
RA Johnston R.J. Jr., Chang S., Etchberger J.F., Ortiz C.O., Hobert O.;
RT "MicroRNAs acting in a double-negative feedback loop to control a neuronal
RT cell fate decision.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12449-12454(2005).
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=16547101; DOI=10.1534/genetics.106.055749;
RA Ortiz C.O., Etchberger J.F., Posy S.L., Frokjaer-Jensen C., Lockery S.,
RA Honig B., Hobert O.;
RT "Searching for neuronal left/right asymmetry: genomewide analysis of
RT nematode receptor-type guanylyl cyclases.";
RL Genetics 173:131-149(2006).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=19523832; DOI=10.1016/j.cub.2009.05.043;
RA Ortiz C.O., Faumont S., Takayama J., Ahmed H.K., Goldsmith A.D., Pocock R.,
RA McCormick K.E., Kunimoto H., Iino Y., Lockery S., Hobert O.;
RT "Lateralized gustatory behavior of C. elegans is controlled by specific
RT receptor-type guanylyl cyclases.";
RL Curr. Biol. 19:996-1004(2009).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (By similarity). Unlike other guanylate cyclases
CC expressed in ASE neurons, may not play a role in chemotaxis responses
CC toward salt ions in ASEL (ASE left) sensory neurons (PubMed:19523832).
CC {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:19523832}.
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:0000250|UniProtKB:Q19187};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F52E1.4a};
CC IsoId=H2L002-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F52E1.4b};
CC IsoId=H2L002-2; Sequence=VSP_057700, VSP_057701;
CC -!- TISSUE SPECIFICITY: Expressed asymmetrically in ASE left (ASEL) sensory
CC neuron (PubMed:16099833, PubMed:16547101). Expressed in excretory canal
CC cell (PubMed:16547101). {ECO:0000269|PubMed:16099833,
CC ECO:0000269|PubMed:16547101}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both ASEL and ASER neurons throughout
CC late embryonic and early larval stages. {ECO:0000269|PubMed:16099833}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; BX284605; CCD70805.1; -; Genomic_DNA.
DR EMBL; BX284605; CCD70806.1; -; Genomic_DNA.
DR RefSeq; NP_001023954.1; NM_001028783.1. [H2L002-2]
DR RefSeq; NP_001023955.1; NM_001028784.1. [H2L002-1]
DR AlphaFoldDB; H2L002; -.
DR SMR; H2L002; -.
DR STRING; 6239.F52E1.4b; -.
DR PaxDb; H2L002; -.
DR EnsemblMetazoa; F52E1.4a.1; F52E1.4a.1; WBGene00001534. [H2L002-2]
DR EnsemblMetazoa; F52E1.4b.1; F52E1.4b.1; WBGene00001534. [H2L002-1]
DR GeneID; 179222; -.
DR UCSC; F52E1.4a; c. elegans.
DR CTD; 179222; -.
DR WormBase; F52E1.4a; CE35321; WBGene00001534; gcy-7. [H2L002-2]
DR WormBase; F52E1.4b; CE35322; WBGene00001534; gcy-7. [H2L002-1]
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; H2L002; -.
DR OMA; YVENMSA; -.
DR OrthoDB; 94238at2759; -.
DR PhylomeDB; H2L002; -.
DR SignaLink; H2L002; -.
DR PRO; PR:H2L002; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001534; Expressed in larva.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0007635; P:chemosensory behavior; IGI:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IGI:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0032026; P:response to magnesium ion; IGI:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 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 Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07701; HNOBA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell membrane; cGMP biosynthesis;
KW Glycoprotein; Lyase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1111
FT /note="Receptor-type guanylate cyclase gcy-7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433276"
FT TOPO_DOM 25..488
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..1111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 536..838
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 896..1026
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 542..550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 568
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1031..1045
FT /note="PGKIHVSAEANRMLH -> RMDFGFPPFSDKLNI (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057700"
FT VAR_SEQ 1046..1111
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057701"
SQ SEQUENCE 1111 AA; 124914 MW; 2B9C35C6C76F758E CRC64;
MKPFYSMSLV LFLVITLLPK PMFPQVATGT TGNVIRVGFI HCRDFQSAPI TVGYRTSAAA
ASIAVDRLKR ENLMSGWEFN FTIEFDDCVE SEAAGMTVDL IEKHNVDVII GPTMNQPTLA
AFIVSNYFNR PIIAWGLVNA AQLDDFERFP NAGILSAGQR SLGVAIRAVL KRYEWSQFVY
AYFTEEDTEK CVTMRNDLQQ VVSYFGDIIL AYSIQVADIS NDGMIEALKK IQSRGRIIVT
CMKDGIGLRR KWLLAAEEAG MIGDEYVYVF SDIKSKGYVV PLLGGGERPS WILSTGSDEN
DTRALKAFKQ SIFICDMMGQ GSIATNYTIF GQEIIARMKE APYFCTKDCE GENFTVAATY
AGQLHDAVYA YGVALDKMLK AGQIAQYRNA TAFMRYFPQS FIGMSGNVTI NEKGTRNPTL
FLLALDENNN NTRMATIYVE NMSATFNALY SDEGVMWASR KNNARPVDVP LCGFTGNLCP
KSFVDEYLIW VIVAIVVLFL AITAAACGIY FSIQARRQEI ERLNRLWQIP FIHLHQINSK
QKGKGEHSVR SLQSGTSTLS SRTTVSFKTE SRNFLFFSLQ RESDYEPVVA KKHAYRPRLD
DDKCTFMRSL RNLDQDNLNR FIGLCLDGPQ MLSVWRFCSR GSIADVILKA TIQMDNFFIY
SLIKDMVHGL VFLHGSMVGY HGMLTSKCCL IDDRWQVKIS NYGLQDLRSP EMYEKKDLLW
SAPELLRAED IKGSKEGDVY SLGIICAELI TRKGVFNMED RKEDPEEIIY LLKKGGLKSP
RPDLEYDHTI EINPALLHLV RDCFTERPSE RPSIETVRSQ LRGMNSSRND NLMDHVFNML
ESYASSLEEE VSERTKELVE EKKKSDVLLY RMLPKTVADK LKLGQTVEPE TFEQVTIFFS
DVVQFTTLAS KCTPLQVVNL LNDLYTIFDG IIEKHDVYKV ETIGDGYLCV SGLPHRNGNE
HVRQIALMSL AFLSSLQFFR VPHLPSERIN LRIGMNCGSV VAGVVGLTMP RFCLFGDAVN
TASRMESNGK PGKIHVSAEA NRMLHLVGGF DTESRGEVII KGKGVMETFW LTGQGTGAVS
GARHVSAKKV SKKMDEIHRQ ETLKSDEQLS D
