GCY25_CAEEL
ID GCY25_CAEEL Reviewed; 1034 AA.
AC A0A078BQP2; A0A078BTN7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Receptor-type guanylate cyclase gcy-25 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-25 {ECO:0000312|WormBase:Y105C5B.2a};
GN ORFNames=Y105C5B.2 {ECO:0000312|WormBase:Y105C5B.2a};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y105C5B.2a};
CC IsoId=A0A078BQP2-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y105C5B.2b};
CC IsoId=A0A078BQP2-2; Sequence=VSP_057708;
CC -!- TISSUE SPECIFICITY: Expressed in AQR, PQR and URX sensory neurons.
CC {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; BX284604; CDX47497.1; -; Genomic_DNA.
DR EMBL; BX284604; CDX47498.1; -; Genomic_DNA.
DR RefSeq; NP_001294116.1; NM_001307187.1. [A0A078BQP2-1]
DR RefSeq; NP_001294117.1; NM_001307188.1. [A0A078BQP2-2]
DR AlphaFoldDB; A0A078BQP2; -.
DR SMR; A0A078BQP2; -.
DR STRING; 6239.Y105C5B.2; -.
DR PaxDb; A0A078BQP2; -.
DR EnsemblMetazoa; Y105C5B.2a.1; Y105C5B.2a.1; WBGene00001549. [A0A078BQP2-1]
DR EnsemblMetazoa; Y105C5B.2b.1; Y105C5B.2b.1; WBGene00001549. [A0A078BQP2-2]
DR GeneID; 191653; -.
DR KEGG; cel:CELE_Y105C5B.2; -.
DR CTD; 191653; -.
DR WormBase; Y105C5B.2a; CE50061; WBGene00001549; gcy-25. [A0A078BQP2-1]
DR WormBase; Y105C5B.2b; CE50104; WBGene00001549; gcy-25. [A0A078BQP2-2]
DR eggNOG; KOG1023; Eukaryota.
DR OMA; LALRWHK; -.
DR OrthoDB; 143875at2759; -.
DR PRO; PR:A0A078BQP2; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001549; Expressed in larva.
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: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: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: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; IPR001828; ANF_lig-bd_rcpt.
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; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 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 Coiled coil; Glycoprotein; GTP-binding; Lyase; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1034
FT /note="Receptor-type guanylate cyclase gcy-25"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433293"
FT TOPO_DOM 17..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..1034
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 464..749
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 821..951
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 758..785
FT /evidence="ECO:0000255"
FT BINDING 470..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 641..693
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057708"
SQ SEQUENCE 1034 AA; 117322 MW; 4BEC8B67F2426C4C CRC64;
MLLLLLLLKI STFVDSFQIG HLEFENSNET RILEICMKNA GSWRDHRLIS LPSCHNFNGL
ENAANLNYQY SVDLLIGAAC DEETQTVSRL ALRWHKLYLS SAPLSTKEKE STTIALKPHS
LAGTAEVILA MCKSMKWKEI GIIYSEETKY TAHAIYDMLA EQEDDLKINV FLETDGLSNT
YTILHSARAL ISFLTTLDLS KFFKTLKENA FRPLEFSIVH VDCNKSEISN FYTYLDNNAG
EEPNPISAAR LRKLYRHVAL LKNSHDDMEK TEEFAKKYGL VPSYTLYKAL ILCDGLQLLN
NYTAPRGNLS IVQQLPYLWN HVTNTETQGY SGPVFIGNDG VRLPYYEMHM WRDGKAVHVA
NVKPRESDYC GGNMTKNCYE FLPSSPLLED LPPYTSDCGY DNNLCSDFHV FMIAAIVFSI
LLIPMAIAFY LQRKEHLIQQ MPWRVPLDSI SFDDNGGSLS ASRRVSTIST ARASYSSIFS
GNVAEHAIVN KQKVSVKRHV QRRAITFSRQ EMEMLNQLKY MSHTNINPFT GICFNQGSEL
IVMWQFTTRY SLEDLIFVKE QKFGRNFQST FIKHIVHGIN YIHNSSIKVH GALYLSNCVV
DSYWVVKLTD FGIKGILKER TNHKELAPSS AFDVDAIHYK YLQLAPEHIS AILEKLEEPR
GTVEGDIYQL AMCIYQILFY MRPFAERQES IKELAHLLSS QSTAPLHPKV PEGNSFTMRL
LSIIQQCWLY KPAARPALIK ITDAVNREFG QDVKGTLIDQ MIEMIDEYSA NLEQIVAERT
RELEQDMSVT ENLLYQLLPK SVADSIRSGK TVVPEQHSSV TLLVVDVCQF TKFCEAFIPV
HILETLQELY SSFDNIVQKN KAFKVENVGD AYLICSGIPE MSGFRHLREI CKISLKLQAF
MKTFKVRHRP SHTLQIKMGI TSGAVAAGIL GSTAPRFCIF GDTVNMACRM ASTGNPGSIQ
LSELTANTLM EKFPSFMLEE RGMIDVKGKG ACLTFWLTGE KDIMRRQSSR SSCISQIKFE
LDEADNSKKM FLNV
