GCY2_CAEEL
ID GCY2_CAEEL Reviewed; 1118 AA.
AC Q10029;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Receptor-type guanylate cyclase gcy-2 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-2 {ECO:0000312|WormBase:R134.2};
GN ORFNames=R134.2 {ECO:0000312|WormBase:R134.2};
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.
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).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (By similarity). {ECO:0000250|UniProtKB:Q19187}.
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 -!- TISSUE SPECIFICITY: Expressed bilaterally in AWA and ASI sensory
CC neurons and in RIA and PVT interneurons. {ECO:0000269|PubMed:16547101}.
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; BX284602; CAA88053.2; -; Genomic_DNA.
DR PIR; T24214; T24214.
DR RefSeq; NP_496038.1; NM_063637.1.
DR AlphaFoldDB; Q10029; -.
DR SMR; Q10029; -.
DR STRING; 6239.R134.2; -.
DR PaxDb; Q10029; -.
DR WormBase; R134.2; CE25080; WBGene00001529; gcy-2.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; Q10029; -.
DR OMA; TVANERW; -.
DR OrthoDB; 1491884at2759; -.
DR PhylomeDB; Q10029; -.
DR PRO; PR:Q10029; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001529; Expressed in adult organism.
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:InterPro.
DR GO; GO:0005525; F:GTP 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; IEA:UniProt.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
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:0010038; P:response to metal ion; IEA:UniProt.
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 InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
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; 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 Cell membrane; cGMP biosynthesis; Glycoprotein; GTP-binding; Lyase;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1118
FT /note="Receptor-type guanylate cyclase gcy-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433270"
FT TOPO_DOM 22..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..1118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 558..875
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 872..1002
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1076..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1118 AA; 126056 MW; D0C91AE94C905FB1 CRC64;
MVSSILKFVI LIHSTFHSTF AQNLPDTTVA PKTKRTIKIG IAAAQRTQTS SIGWSVCGGA
VPMAIERLRE FGYVKDFDFE FIVDYTECDQ GSVVRAGIEF IKTHKVDVII GPPCAQALRV
MSFLAENYKK PVLGWGFVSD TDLSDVIRFP YLTTVIPNSL MLGYAASKML TVYNWGRVAM
LYYYSDIKYC SGVMNDVEAT FNNPSTPNVN IVIKAEIYLN DNETTDIVFQ SVKSRARIIF
WCTQTAIEKR DYLIKIATHD MIGDEYVHIM LSMRNIAFGA QTSLGKPTFS QSGLTPIWES
FTEGTDDFEK MVKQAATRMF VLDVNSEVAD KKYLDYLQKN IMKAVQSPPM NCSTVECMTA
NTTIMGGYAR QLFDVVYLYG VALTNTNSTD PAVYDDVDVI VPQFVTSFQG MTGKVVISPN
LTRMPIFQLY GLNSDYEQVA LAEFTYIDPI MNVTLSYKEE GGAVWYFYGN SRPLDIPICG
FLGKFCPISF WEQYMILAIV SISVIVLMVI IMIIGCLCVI SAKHAEQART NAEWQVPFVN
LMESEKQIRS NATSRRSLQS APSISTGHSG VTTVSDFCEN YTMMMYEKEM VLTAKYQYTH
LTKADKERFV KMRKLDHENI NRFIGLSIDS AHFIAVTKLC SRGSLQDILS RGNFSMDYFF
MFCIIRDVAK GLEYLHKTFL RLHGNLRSAT CLVNDSWQVK LAEYGMDNLV EEQTPPKKRL
LWVAPEVLRG SLSVSQMEPS ADIYSFAIIA SEILTKKEAW DILDRKEDCE ALIALVKDCW
AEVPEDRPTA ENICSQMKGL VSKQKTNLMD HVFNMLEEYT STLEEEIEER TKELTLEKKK
ADILLSRMLP KQVAERLKAG QTVEPEGFDS VTVFFSDVVK FTILASKCSP FQTVNLLNDL
YSNFDTIIEQ HGVYKVESIG DGYLCVSGLP TRNGYAHIKQ IVDMSLKFME YCRSFKIPHL
PRENVELRIG VNSGPCVAGV VGLSMPRYCL FGDTVNTASR MESNGKPSLI HLTSDAHLLL
LTHYPNHYDT SSRGEVIIKG KGVMETFWVH GRIDDIAEPT ELRSICKPST VANERWITPP
APKPEIRSVS SHGSRPPSVY DPLQDHRKFK MDTLKVAN
