GCY14_CAEEL
ID GCY14_CAEEL Reviewed; 1111 AA.
AC Q23310; G1UJJ4;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Receptor-type guanylate cyclase gcy-14 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-14 {ECO:0000312|WormBase:ZC412.2};
GN ORFNames=ZC412.2 {ECO:0000312|WormBase:ZC412.2};
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|EMBL:BAK69482.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DOMAIN, AND MUTAGENESIS OF HIS-57; HIS-88; HIS-145 AND
RP HIS-273.
RX PubMed=23664973; DOI=10.1016/j.cub.2013.04.052;
RA Murayama T., Takayama J., Fujiwara M., Maruyama I.N.;
RT "Environmental alkalinity sensing mediated by the transmembrane guanylyl
RT cyclase GCY-14 in C. elegans.";
RL Curr. Biol. 23:1007-1012(2013).
RN [2] {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 [3] {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). Regulates chemotaxis responses toward
CC Na(1+) and Li(1+) salt ions and alkaline pH in ASE left (ASEL) sensory
CC neuron. Directly senses environmental alkalinity in ASEL neuron which
CC probably leads to the activation of cGMP-gated cation channel tax2/tax4
CC (PubMed:23664973, PubMed:19523832). {ECO:0000250|UniProtKB:Q19187,
CC ECO:0000269|PubMed:19523832, ECO:0000269|PubMed:23664973}.
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23664973}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell projection, cilium
CC {ECO:0000269|PubMed:23664973}. Note=Localizes in cilium of ASEL sensory
CC neurons. {ECO:0000269|PubMed:23664973}.
CC -!- TISSUE SPECIFICITY: Expressed asymmetrically in ASEL sensory neuron.
CC {ECO:0000269|PubMed:23664973}.
CC -!- DOMAIN: The extracellular domain is required for the direct sensing of
CC alkaline pH. {ECO:0000269|PubMed:23664973}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAK69482.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB668394; BAK69482.1; ALT_INIT; mRNA.
DR EMBL; BX284605; CAB01533.2; -; Genomic_DNA.
DR PIR; T27564; T27564.
DR RefSeq; NP_506660.2; NM_074259.2.
DR AlphaFoldDB; Q23310; -.
DR SMR; Q23310; -.
DR STRING; 6239.ZC412.2; -.
DR PRIDE; Q23310; -.
DR EnsemblMetazoa; ZC412.2.1; ZC412.2.1; WBGene00001540.
DR GeneID; 191647; -.
DR KEGG; cel:CELE_ZC412.2; -.
DR UCSC; ZC412.2; c. elegans.
DR CTD; 191647; -.
DR WormBase; ZC412.2; CE48405; WBGene00001540; gcy-14.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00970000196659; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; Q23310; -.
DR OMA; CPPDFVK; -.
DR OrthoDB; 109593at2759; -.
DR PRO; PR:Q23310; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001540; Expressed in larva.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
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:0042802; F:identical protein binding; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IMP: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:0010446; P:response to alkaline pH; IMP:UniProtKB.
DR GO; GO:0010035; P:response to inorganic substance; IMP:UniProtKB.
DR GO; GO:0010226; P:response to lithium ion; IMP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IMP: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 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cell projection; cGMP biosynthesis; Chemotaxis;
KW Glycoprotein; GTP-binding; Lyase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..1111
FT /note="Receptor-type guanylate cyclase gcy-14"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433283"
FT TOPO_DOM 15..473
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..1111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 482..817
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 875..1005
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1061..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 488..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 145
FT /note="Involved in sensing alkaline pH"
FT /evidence="ECO:0000269|PubMed:23664973"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 57
FT /note="H->Q: No effect on chemotaxis to alkaline pH. No
FT effect on chemotaxis toward Na+. Normal cilium
FT localization."
FT /evidence="ECO:0000269|PubMed:23664973"
FT MUTAGEN 88
FT /note="H->Q: No effect on chemotaxis to alkaline pH. No
FT effect on chemotaxis toward Na+. Normal cilium
FT localization."
FT /evidence="ECO:0000269|PubMed:23664973"
FT MUTAGEN 145
FT /note="H->Q: Loss of chemotaxis to alkaline pH. No effect
FT on chemotaxis toward Na+. Normal cilium localization."
FT /evidence="ECO:0000269|PubMed:23664973"
FT MUTAGEN 273
FT /note="H->Q: No effect on chemotaxis to alkaline pH. No
FT effect on chemotaxis toward Na+. Normal cilium
FT localization."
FT /evidence="ECO:0000269|PubMed:23664973"
SQ SEQUENCE 1111 AA; 124706 MW; BE288FE4FF07CABC CRC64;
MCLFLLLFPY LASGQFLQTV KVGLLFSKDT ASVMRAVGYR TSAAAVLVAR DRIRAEHLLD
QYDFNFTVKF DECTEGLAGG KTVELINHDN VDVIIGPTCN RAGIAVASLA AYYNVPVFQW
GLTTAADIGN VSRYPTTVTL SLDTHSMALG VREVLRRFEW DEFVFIYSND GDEEKCASMK
DDLEKMGIEN SDVTLAYMVQ IQTVTLDALQ KALTEVSKRG RIIIACFANG RGFKKAFVAS
TVLAGMSTDE YMYMFAEPQS RGFYVDEING GEHYSWDDTD GNFVTGLTPE QIRDAYGKVL
YICDNMGLPT TITPEFANFS SQLISRMTEQ PFNCVQDCSN STYKVPATYA GQLFDAFYAY
GVALNRSLTQ DPTRANLKNG SFVLSDIGMS FQGVGGGTVT LDDTGTRIVQ VYMFALNTSL
LPYLAASLVI NGSEVEYTPF YKSEADLWSV RPLARPICGF SGLECPPDFV KEYLVYTIIA
AVIVVLALLA GCAGLLYTMQ MKRKEMERQD LLWQVPFIEL QQVQSKSKAE ASMHSFASGP
STSTKITVES RSETINFIFY YYQQDILAAM KHDLILQFDA EQKAEFRQMR NFDNDNLNKF
IGLCLDGPQL FSLWRFCSRG SLSDVISKSS MQMDSFFMFS LIRDISNGLL FIHNSFLKCH
GHLTSRCCLI DDRWQIKISG YGLKSVRTFE NPKKEDLLWT PPENLRNENE ERLPEGDIYS
FGIICSEILT RSSAFDLENR KEKPDVIIYQ VKKGGHNPMR PSLDTGETVE INPALLHLIR
DCWTERPSER PSIEQVRGHL NGMRDGRKSN LMDHVFNMLE TYASTLEEEV SDRTKELVEE
KKKSDVLLYR MLPKMVADKL KLGQTVEPET FEQVTIFFSD VVQFTTLAGK CTPLQVVTLL
NDLYTIFDGI IEQNDVYKVE TIGDGYLCVS GLPHRNGNEH IRHIARMSLG FLSSLEFFRV
QHLPSERINL RIGINCGSVV AGVVGLTMPR YCLFGDAVNT ASRMESNGKP GKIHVTAEAN
QMLTQVVGGF RTESRGEVII KGKGVMETYW LLGEQSRISV SAQAPREKTP EPPRRQSVRS
ISPIIEKMSE ETQKGLYSAY KDFNNGNECV S
