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Receptor-type guanylate cyclase gcy-14 (EC 4.6.1.2)

 GCY14_CAEEL             Reviewed;        1111 AA.
Q23310; G1UJJ4;
24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
26-JUN-2013, sequence version 2.
22-NOV-2017, entry version 154.
RecName: Full=Receptor-type guanylate cyclase gcy-14 {ECO:0000305};
EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
Flags: Precursor;
Name=gcy-14 {ECO:0000312|WormBase:ZC412.2};
ORFNames=ZC412.2 {ECO:0000312|WormBase:ZC412.2};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:BAK69482.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF HIS-57; HIS-88; HIS-145
AND HIS-273.
PubMed=23664973; DOI=10.1016/j.cub.2013.04.052;
Murayama T., Takayama J., Fujiwara M., Maruyama I.N.;
"Environmental alkalinity sensing mediated by the transmembrane
guanylyl cyclase GCY-14 in C. elegans.";
Curr. Biol. 23:1007-1012(2013).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION.
PubMed=19523832; DOI=10.1016/j.cub.2009.05.043;
Ortiz C.O., Faumont S., Takayama J., Ahmed H.K., Goldsmith A.D.,
Pocock R., McCormick K.E., Kunimoto H., Iino Y., Lockery S.,
Hobert O.;
"Lateralized gustatory behavior of C. elegans is controlled by
specific receptor-type guanylyl cyclases.";
Curr. Biol. 19:996-1004(2009).
-!- FUNCTION: Guanylate cyclase involved in the production of the
second messenger cGMP (By similarity). Regulates chemotaxis
responses toward Na(1+) and Li(1+) salt ions and alkaline pH in
ASE left (ASEL) sensory neuron. Directly senses environmental
alkalinity in ASEL neuron which probably leads to the activation
of cGMP-gated cation channel tax2/tax4 (PubMed:23664973,
PubMed:19523832). {ECO:0000250|UniProtKB:Q19187,
ECO:0000269|PubMed:19523832, ECO:0000269|PubMed:23664973}.
-!- CATALYTIC ACTIVITY: GTP = 3',5'-cyclic GMP + diphosphate.
{ECO:0000250|UniProtKB:Q19187}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23664973}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}. Cell projection, cilium
{ECO:0000269|PubMed:23664973}. Note=Localizes in cilium of ASEL
sensory neurons. {ECO:0000269|PubMed:23664973}.
-!- TISSUE SPECIFICITY: Expressed asymmetrically in ASEL sensory
neuron. {ECO:0000269|PubMed:23664973}.
-!- DOMAIN: The extracellular domain is required for the direct
sensing of alkaline pH. {ECO:0000269|PubMed:23664973}.
-!- DOMAIN: The protein kinase domain is predicted to be catalytically
inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
-!- SEQUENCE CAUTION:
Sequence=BAK69482.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB668394; BAK69482.1; ALT_INIT; mRNA.
EMBL; BX284605; CAB01533.2; -; Genomic_DNA.
PIR; T27564; T27564.
RefSeq; NP_506660.2; NM_074259.2.
EnsemblMetazoa; ZC412.2; ZC412.2; WBGene00001540.
GeneID; 191647; -.
KEGG; cel:CELE_ZC412.2; -.
UCSC; ZC412.2; c. elegans.
CTD; 191647; -.
WormBase; ZC412.2; CE48405; WBGene00001540; gcy-14.
GeneTree; ENSGT00760000118959; -.
HOGENOM; HOG000016255; -.
InParanoid; Q23310; -.
KO; K01769; -.
OMA; SKAEASM; -.
OrthoDB; EOG091G02QS; -.
PRO; PR:Q23310; -.
Proteomes; UP000001940; Chromosome V.
Bgee; WBGene00001540; -.
GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
GO; GO:0006935; P:chemotaxis; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0010446; P:response to alkaline pH; IMP:UniProtKB.
GO; GO:0010035; P:response to inorganic substance; IMP:UniProtKB.
GO; GO:0010226; P:response to lithium ion; IMP:UniProtKB.
GO; GO:1902074; P:response to salt; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
Gene3D; 3.30.70.1230; -; 1.
InterPro; IPR001054; A/G_cyclase.
InterPro; IPR018297; A/G_cyclase_CS.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR011645; HNOB_dom_associated.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR029787; Nucleotide_cyclase.
InterPro; IPR028082; Peripla_BP_I.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00211; Guanylate_cyc; 1.
Pfam; PF07701; HNOBA; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00044; CYCc; 1.
SUPFAM; SSF53822; SSF53822; 1.
SUPFAM; SSF55073; SSF55073; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Cell projection; cGMP biosynthesis;
Chemotaxis; Complete proteome; Glycoprotein; GTP-binding; Lyase;
Membrane; Nucleotide-binding; Receptor; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 14 {ECO:0000255}.
CHAIN 15 1111 Receptor-type guanylate cyclase gcy-14.
{ECO:0000255}.
/FTId=PRO_0000433283.
TOPO_DOM 15 473 Extracellular. {ECO:0000255}.
TRANSMEM 474 494 Helical. {ECO:0000255}.
TOPO_DOM 495 1111 Cytoplasmic. {ECO:0000255}.
DOMAIN 482 817 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 875 1005 Guanylate cyclase. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
NP_BIND 488 496 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 545 545 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 145 145 Involved in sensing alkaline pH.
{ECO:0000269|PubMed:23664973}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 57 57 H->Q: No effect on chemotaxis to alkaline
pH. No effect on chemotaxis toward Na+.
Normal cilium localization.
{ECO:0000269|PubMed:23664973}.
MUTAGEN 88 88 H->Q: No effect on chemotaxis to alkaline
pH. No effect on chemotaxis toward Na+.
Normal cilium localization.
{ECO:0000269|PubMed:23664973}.
MUTAGEN 145 145 H->Q: Loss of chemotaxis to alkaline pH.
No effect on chemotaxis toward Na+.
Normal cilium localization.
{ECO:0000269|PubMed:23664973}.
MUTAGEN 273 273 H->Q: No effect on chemotaxis to alkaline
pH. No effect on chemotaxis toward Na+.
Normal cilium localization.
{ECO:0000269|PubMed:23664973}.
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


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