GCY13_CAEEL
ID GCY13_CAEEL Reviewed; 1028 AA.
AC Q19768;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Receptor-type guanylate cyclase gcy-13 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-13 {ECO:0000312|WormBase:F23H12.6};
GN ORFNames=F23H12.6 {ECO:0000312|WormBase:F23H12.6};
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 RIM interneurons.
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; BX284605; CAA98947.3; -; Genomic_DNA.
DR RefSeq; NP_506097.3; NM_073696.3.
DR AlphaFoldDB; Q19768; -.
DR SMR; Q19768; -.
DR STRING; 6239.F23H12.6; -.
DR PaxDb; Q19768; -.
DR PRIDE; Q19768; -.
DR EnsemblMetazoa; F23H12.6.1; F23H12.6.1; WBGene00001539.
DR GeneID; 191646; -.
DR KEGG; cel:CELE_F23H12.6; -.
DR UCSC; F23H12.6; c. elegans.
DR CTD; 191646; -.
DR WormBase; F23H12.6; CE45651; WBGene00001539; gcy-13.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; Q19768; -.
DR OMA; LYQGNHV; -.
DR OrthoDB; 181838at2759; -.
DR PhylomeDB; Q19768; -.
DR PRO; PR:Q19768; -.
DR Proteomes; UP000001940; Chromosome V.
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; IPR001170; ANPR/GUC.
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 PRINTS; PR00255; NATPEPTIDER.
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; Coiled coil; Glycoprotein; GTP-binding;
KW Lyase; Membrane; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000305"
FT CHAIN ?..1028
FT /note="Receptor-type guanylate cyclase gcy-13"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433282"
FT TOPO_DOM ?..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..1028
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 499..770
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 844..974
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 491..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 786..817
FT /evidence="ECO:0000255"
FT COMPBIAS 497..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1028 AA; 115325 MW; ED0F5EF30E7877ED CRC64;
MASSVGWQTS ASAIEIAMDR IKSEHLIDNI GINFIYVFDD CNEAKAAGLS SKLLMDANVS
AIVGPTCNAA GLAVVNLAGY YNTPVLTWGL TISSSFIDTS KYPTTVTIVP VAKSIAAAIH
EVMIQFEWTE FVYVFVEDEK CGYFRDDLEQ ITSDSNYTSL SRTIQIYDQS YTNLVRQLEK
LKTVSRIFTV CLPEAGDIKR RFMLAAYDLD MTTDEYVYLF AGPKSTAYQQ TSSTGDVVGI
WVDWSENPDG RDEEAKLAFM RTMVIVATPV QGEQYAAFKK EVIERMKLPP YNCVDECKEK
EYQEAAEYAD QLHDTIYLYA LILNKTIEEQ GIEQIANGSN IVTRGAGIEF EGMSGVVRMN
GIGYRLPNMN LANLDSNATQ RTVAYMDIDS TSVNWTFAII DQALIWDAYN GKLPQTRPEC
GYSGKSCPVN FFVDYLYIVV IVAVIIVLCC AAAAIAAFLV IKARRDEELR LDDQWIVPHG
MLQSIIKGRK ESHHSSRSLQ SNSTTTTGTT GISSRSVFFP ETETQGYFVY MNEPVLARKY
QLRVPIFKQD RSELRMLRSI EHDNVNRFIG LSIDGPVYMS FWRYCSRGSI KDVIAKSSIN
MDGFFIYCLI KDIASGLQYI HHSPIKQHGS LTSECCYIND RWQVKIGSYG LSFMQGVEKR
TEDGLLHTAP EVLREGLTSG TQAGDVYSFS IVCSELVGHS SAWNLENRKE EADEIIFMVK
RGGRTPFRPS LDDVDDDINP AMLHLIRDCW DEDPKQRPNI DMVNKLMKNM NSGRSGSANL
MDHVFSVLEK HASSLEDEVQ ERMKELVEEK KKSDILLYRM LPQQVAERLK LGQSVEPEAF
ESVTIFFSDV VGFTVLANKS TPLQVVNLLN DLYTTFDAII EKNDSYKVET IGDAYLVVSG
LPRRNGTEHV ANIANMSLEL MDSLQAFKIP HLPQEKVQIR IGMHSGSCVA GVVGLTMPRY
CLFGDTVNTA SRMESNGKPG FIHLSSDCYD LLTSLYKEYN TESRGEVIIK GKGVMQTYWL
LGMKEESA
