GCY22_CAEEL
ID GCY22_CAEEL Reviewed; 1058 AA.
AC Q9XTY1; J7SA55; J7SF90;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Receptor-type guanylate cyclase gcy-22 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-22 {ECO:0000312|WormBase:T03D8.5a};
GN ORFNames=T03D8.5 {ECO:0000312|WormBase:T03D8.5a};
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=16099833; DOI=10.1073/pnas.0505530102;
RA Johnston R.J. Jr., Chang S., Etchberger J.F., Ortiz C.O., Hobert O.;
RT "MicroRNAs acting in a double-negative feedback loop to control a neuronal
RT cell fate decision.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12449-12454(2005).
RN [3] {ECO:0000305}
RP FUNCTION, AND DOMAIN.
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).
RN [4] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-596; MET-710 AND GLU-912.
RX PubMed=20837997; DOI=10.1534/genetics.110.119768;
RA Adachi T., Kunitomo H., Tomioka M., Ohno H., Okochi Y., Mori I., Iino Y.;
RT "Reversal of salt preference is directed by the insulin/PI3K and Gq/PKC
RT signaling in Caenorhabditis elegans.";
RL Genetics 186:1309-1319(2010).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (By similarity). Regulates chemotaxis responses toward
CC Li(1-), Mg(2+), Cl(1-), Br(1)- and I(1-) salt ions and methionine in
CC ASE right (ASER) sensory neuron (PubMed:19523832, PubMed:20837997). May
CC regulate ASER neuronal activity such as axon sprouting and calcium
CC responses to changes in salt concentrations (PubMed:19523832).
CC {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:19523832,
CC ECO:0000269|PubMed:20837997}.
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=3;
CC Name=a {ECO:0000312|WormBase:T03D8.5a};
CC IsoId=Q9XTY1-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T03D8.5b};
CC IsoId=Q9XTY1-2; Sequence=VSP_057707;
CC Name=c {ECO:0000312|WormBase:T03D8.5c};
CC IsoId=Q9XTY1-3; Sequence=VSP_057706;
CC -!- TISSUE SPECIFICITY: Expression in ASER neuron begins at an early larval
CC stage and is maintained in the adult. {ECO:0000269|PubMed:16099833}.
CC -!- DOMAIN: The extracellular and guanylate cyclase domains are essential
CC for chemosensory responses. {ECO:0000269|PubMed:19523832}.
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; Z92838; CAB07410.2; -; Genomic_DNA.
DR EMBL; Z92838; CCM09401.1; -; Genomic_DNA.
DR EMBL; Z92838; CCM09402.1; -; Genomic_DNA.
DR RefSeq; NP_001263951.1; NM_001277022.1. [Q9XTY1-3]
DR RefSeq; NP_001263952.1; NM_001277023.1. [Q9XTY1-2]
DR RefSeq; NP_508018.2; NM_075617.3. [Q9XTY1-1]
DR AlphaFoldDB; Q9XTY1; -.
DR SMR; Q9XTY1; -.
DR STRING; 6239.T03D8.5a; -.
DR PaxDb; Q9XTY1; -.
DR PRIDE; Q9XTY1; -.
DR EnsemblMetazoa; T03D8.5a.1; T03D8.5a.1; WBGene00001547. [Q9XTY1-1]
DR EnsemblMetazoa; T03D8.5b.1; T03D8.5b.1; WBGene00001547. [Q9XTY1-2]
DR EnsemblMetazoa; T03D8.5c.1; T03D8.5c.1; WBGene00001547. [Q9XTY1-3]
DR GeneID; 180365; -.
DR KEGG; cel:CELE_T03D8.5; -.
DR UCSC; T03D8.5; c. elegans. [Q9XTY1-1]
DR CTD; 180365; -.
DR WormBase; T03D8.5a; CE43349; WBGene00001547; gcy-22. [Q9XTY1-1]
DR WormBase; T03D8.5b; CE47774; WBGene00001547; gcy-22. [Q9XTY1-2]
DR WormBase; T03D8.5c; CE47796; WBGene00001547; gcy-22. [Q9XTY1-3]
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000169004; -.
DR InParanoid; Q9XTY1; -.
DR OMA; IYYLHHS; -.
DR OrthoDB; 111503at2759; -.
DR PhylomeDB; Q9XTY1; -.
DR PRO; PR:Q9XTY1; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001547; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
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:0008306; P:associative learning; IMP:UniProtKB.
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:0050850; P:positive regulation of calcium-mediated signaling; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0010226; P:response to lithium ion; IMP:UniProtKB.
DR GO; GO:0032026; P:response to magnesium ion; IMP:UniProtKB.
DR GO; GO:1904640; P:response to methionine; 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; 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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; cGMP biosynthesis; Chemotaxis;
KW Coiled coil; Glycoprotein; GTP-binding; Lyase; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1058
FT /note="Receptor-type guanylate cyclase gcy-22"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433291"
FT TOPO_DOM 25..470
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..1058
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 501..809
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 867..997
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 811..840
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 302
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 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 421..428
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057706"
FT VAR_SEQ 425..428
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057707"
FT MUTAGEN 596
FT /note="G->E: In pe905; moderate loss of chemotaxis in
FT response to Cl-."
FT /evidence="ECO:0000269|PubMed:20837997"
FT MUTAGEN 710
FT /note="M->I: In pe922; moderate loss of chemotaxis in
FT response to Cl-."
FT /evidence="ECO:0000269|PubMed:20837997"
FT MUTAGEN 912
FT /note="E->K: In pe902; severe loss of chemotaxis in
FT response to Cl-."
FT /evidence="ECO:0000269|PubMed:20837997"
SQ SEQUENCE 1058 AA; 118887 MW; 54699D8C14290AA7 CRC64;
MSFISKCFIC LLFSTYFLPP VNSAVLQVGF LAANDNTTEL APFIGWGQVA GALGVAWSRI
VEYGLLPGYE TMNLTWVLTN CREADAVGSV INYAEGHAHV VLGPPCVRPA QVAGSVAKYL
DFPLILWGPP FDSSLLNQFE YPTIASTTSS TLYQATSLIR LLEYYKWTEI ALIYYVARSD
LIPRCTPLIS DFEGLVNNND NLTITYRRQM SVITNTSYAT ALRNLKELAR VVIVCLESDE
ARRNLMISIS ENGMDGDEYV YIMAESRRAG FASSFWNGTD GKNDLALRAA RKFLVMDNQK
YNDTTTFVQE VRAAFSRPPF SCPNCTNIDP TVSQVGPLGD ALLLYAYALN RSIATGNPNP
TGTEFCEVAK GMEFLGFTGK VIINQNSTRT PLFVVYNLDS TDKEMIVMQI TEDLDDSKDP
VASSVNYYIT LVATPAQIWD TWGGTVPLST PICGFTGTDC PKSFTDQYLA IILGCTAAAL
VLIIAVISTI VFLVRSKRQE EERLNQLWQV HFSSLVKPPQ KNTMHSSRSL QSTVTTSTKV
TINSKKDTER HSFYFLNNDS VVARKHNFRA TFTKNDRAMF RKMRNVDNDN LCKFIGLSLD
SPTLISIWRY CSRGSLQDVI AKGSLQMDWF FKYSLMRDVA DAIYYLHHSP IGPHGWLSSS
TCLVDERWQV KVSFFGLSAI KQYEVKEQRD FLHTAPEHIR DTNLPITKEM DIYSFAIICS
ELITKKSAWD LENETFDIEE LVYKIKKGGR SPPRPSLETE DEHNGSMSLL VRDCWNENPD
QRPTSEQIKT LMKSMNHNRS SNLMDHVFNV LEQYASNLED EVQARMKELT EEKKRSDVLL
YRMLPKQVAE KLKLGQSVEP ETFDCVTIFF SDVVSFTTLA SRCTPLQVVN LLNDLYTTFD
AIIEQHDVYK VETIGDGYLC VSGLPHRNGN EHAKEISSMS FSLLKAIKTF RVPHLPKERI
NIRVGLHTGP VVTGVVGMTM PRYCLFGDSV NTASRMESNG KPGRVHISTE CMKFLTEVIG
GYQTEPRGEV IVKGKGAVQT HWLLTDDEIE AKENGESI
