GCY4_CAEBR
ID GCY4_CAEBR Reviewed; 1135 AA.
AC A8WPG9;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Receptor-type guanylate cyclase gcy-4 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-4 {ECO:0000312|WormBase:CBG00851};
GN ORFNames=CBG00851 {ECO:0000312|WormBase:CBG00851};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000312|Proteomes:UP000008549};
RN [1] {ECO:0000312|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP22376.2,
RC ECO:0000312|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.A., 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.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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. Regulates chemotaxis responses toward salt ions in ASE
CC sensory neurons (By similarity). {ECO:0000250|UniProtKB:Q19187,
CC ECO:0000250|UniProtKB:Q23681}.
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 ASE 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; HE600951; CAP22376.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WPG9; -.
DR SMR; A8WPG9; -.
DR STRING; 6238.CBG00851; -.
DR EnsemblMetazoa; CBG00851b.1; CBG00851b.1; WBGene00024180.
DR WormBase; CBG00851; CBP43164; WBGene00024180; Cbr-gcy-4.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; A8WPG9; -.
DR OMA; FYMYGMA; -.
DR OrthoDB; 152376at2759; -.
DR Proteomes; UP000008549; Chromosome II.
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:EnsemblMetazoa.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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:0010035; P:response to inorganic substance; IEA:EnsemblMetazoa.
DR GO; GO:1902074; P:response to salt; IEA:EnsemblMetazoa.
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; 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 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; Chemotaxis; Glycoprotein; GTP-binding;
KW Lyase; Membrane; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1135
FT /note="Receptor-type guanylate cyclase gcy-4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433272"
FT TOPO_DOM 21..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..1135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 545..837
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 895..1025
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 535..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1135 AA; 128272 MW; 0F6D8E516D3ADBA3 CRC64;
MTQLLRFLLI LSIFCDFSHS QRPTIRVGIA AALKTQNGSI GWAYAGGAVP LALQYLKSHG
FVKDFDFEFH VEYTECDLTE TVRAGLDFMK TKNYDVIIGP PCATPLIAMG TLSTVYKKPV
LGWGFVSESE FSDMERFPYL TSVLPSSMTL GTVTSALLEL YGWDRIALVY FKNELNYCSG
VIEDVETSLY DENYSQMVQV VIKEEVDQNN TENFVATLQM IKARARIIIF CAQTGAEKRF
YMIQAGKQGM NTSEYVHVML SMRSVGFGVQ SAVGKKPLNS GLAPIWEAFQ VAPDGLEDLA
KSVASKMLVI DLSSDIRDKE FLQYMTKNIV YAIREPPLSC MAPECLAANA TGMGAYARHL
FDVFYMYGMA LTNLNSTDPN IYGNVDLLVS KFTTPFEGMT GQVQLNSELS RLPLYQVYAL
NKEYDQISIM NISLINGTAK VSLAYQNESS DVWHFWGSTR PLDTPICGFL GKSCPIPFFD
QYRLLIFVFV IVAGLLILAI FTCLTSMVRN QRAEQSRLNS EWQIHAIKLR IPEKKGRRLS
TDSENSTVTK SSKGSSSKNF ETSEFNENYE IQFLENDLVL TTAHQVQELS NLDKMRLVKL
RKLDHENLNK FIGLSIDGSR YLAVWKMCTR GSIQDIMSRG NFSMDYFFMF CMIRDIAEGL
NFLHKSFLRL HGNLRSATCL VNDSWQVKLA EFGLEFLQDD EERPTQKRLL WAAPEVLRGS
LTVSQMDPSA DVYSFAIVAS EILTKKEAWD LHKRKEGYEG KRGNSKIEII YNVKKGGPHP
FRPTLLTDSD VNKSLLALVK DCWSENPEAR PNTENICKII LDMTPRTKDN LMDHVFSMLE
EYTQTLEVEV DERTKELVLE KKKSDILLGR MLPKQVAERL KAGQAVEPES FDLVTVFFSD
LVKFTELANK CSPFQVVNLL NEVFSNFDAI IEKHDVYKVE SIGDGFLCVS GLPNRNGVEH
IRQIVEMALG FLEFCDKFRI PHLPRERVEL RVGVNSGSCV AGVVGLSMPR YCLFGDTVNT
ASRMESNGKA SLIHMSEIAH AFLVDHFPYQ YETNSRGEVI IKGKGVMETF WLLGRISMSN
RSTPPVAQLK QLPQKCSSFT DTGTIRSVSP YIENASDSED EELRRVMRRE MMRVS
