GCY4_CAEEL
ID GCY4_CAEEL Reviewed; 1136 AA.
AC Q23681;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 161.
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:ZK970.5};
GN ORFNames=ZK970.5 {ECO:0000312|WormBase:ZK970.5};
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).
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 Br(1-) and I(1-) salt ions in ASE right (ASER) sensory neuron
CC (PubMed:19523832). {ECO:0000250|UniProtKB:Q19187,
CC ECO:0000269|PubMed:19523832}.
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: Expression is biased toward ASE right (ASER)
CC sensory neuron. {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; BX284602; CAA88889.2; -; Genomic_DNA.
DR RefSeq; NP_496218.2; NM_063817.2.
DR AlphaFoldDB; Q23681; -.
DR SMR; Q23681; -.
DR STRING; 6239.ZK970.5; -.
DR PaxDb; Q23681; -.
DR EnsemblMetazoa; ZK970.5.1; ZK970.5.1; WBGene00001531.
DR GeneID; 191642; -.
DR KEGG; cel:CELE_ZK970.5; -.
DR CTD; 191642; -.
DR WormBase; ZK970.5; CE43236; WBGene00001531; gcy-4.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; Q23681; -.
DR OMA; FYMYGMA; -.
DR OrthoDB; 152376at2759; -.
DR PhylomeDB; Q23681; -.
DR PRO; PR:Q23681; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001531; Expressed in material anatomical entity and 2 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: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:0010035; P:response to inorganic substance; IMP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IGI: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; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1136
FT /note="Receptor-type guanylate cyclase gcy-4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433273"
FT TOPO_DOM 22..485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..1136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 533..833
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 891..1021
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 536..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
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 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1136 AA; 128245 MW; 901F8B74296A56FA CRC64;
MRQLNYYIFI STILTYNLTH GQGPRPVIRV GITAALKTEN GSIGWAYTGG AVPLALQYLK
SHGYMLNFDF EFHVEYTECD LANTVRAGLN FMKTNNYDVI IGPPCAPALK MMGTLSTIYK
KPVLGWGFVS ESEISDMNRF PFVASVLPST KTLGVVTSKL LEIYGWDRVA LLYFKNELDY
CSSVVNDVEK SLYNESKSVQ IVMKAEIDGS NSESTSATLQ VVKTRARVIL FCAHAGGEKR
FYLIQAGLLG MNSSEYVHVM LSMRSVGFGV QTSVGKKPLT LSGLPPIWES FTVNPDGMED
LAKSVAAKMI VIDTSSEVRD KTFLQYMTKN IVYAIREPPL SCKVPECLIT NATGMGAYAR
HLFDVFYMYG MAVSSLNSTD PNVYGNLSLL IPKFTTAFEG MTGEVKLNED LARKPLYQVY
GLNSEYDQIS LIDISLINDT VNVVFNYADG NTEVWHFWGG TRPPDTPVCG FLGKSCPLPI
FEQYRALVIV AIAVTILILL AIIICMSSKI RNRRVEQSRL HSEWQIHAIK LRLPMHRRAS
KSSQESETES ASETENFTSK SGDTMTSEFK ETYTIQYLEN DLVLTTAHQV QELSQAEMMK
FVKLRKLDHE NLNKFIGLSI DGSRFVSVWK MCSRGSLQDI ISKGSFSMDY FFMFCMIRDI
AEGLHYIHKS FLRHHGNLRS ATCLVNDSWQ VKLADFGLQF LQDEEEKPFK KNMLWAAPEV
IRGSLSIEQM DSSADIYSFA IVASEILTKR EAWDLSRRKE GYEEIKYAVK KGGQFVLRPD
LHIDIEVNQT LLALVKDCWC ENPEERPSAE NVCKVLFDMT PNTEDNLMDH VFSMLEEYTS
SLEVEVGERT KELTLEKKKS DILLGRMLPK QVAERLKAGQ AVEPESFDLV TVFFSDLVKF
TDLASKCSPF QVVNLLNDVF SNFDSIIEKH DVYKVESIGD GFLCVSGLPN RNGMEHIRQI
VGMSLCFMEF CRNFRIPHLP RERVELRVGI NSGPCVAGVV GLSMPRYCLF GDTVNTASRM
ESNGKPSMIH MSEAAHSLLV NNYPYQFETN SRGEVIIKGK GVMETYWLLG KMSLSNQSTP
PITKVNHKPR KIASFTDSEL TNYSFRSVSP YVENLSDNDD EEIRRVLRRE MMRVEV
