ID GCY12_CAEEL Reviewed; 1679 AA.
AC Q19187;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 3.
DT 27-MAR-2024, entry version 185.
DE RecName: Full=Receptor-type guanylate cyclase gcy-12 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000269|PubMed:9096403};
DE Flags: Precursor;
GN Name=gcy-12 {ECO:0000312|WormBase:F08B1.2a};
GN ORFNames=F08B1.2 {ECO:0000312|WormBase:F08B1.2a};
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=9096403; DOI=10.1073/pnas.94.7.3384;
RA Yu S., Avery L., Baude E., Garbers D.L.;
RT "Guanylyl cyclase expression in specific sensory neurons: a new family of
RT chemosensory receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3384-3387(1997).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21124861; DOI=10.1371/journal.pgen.1001211;
RA Fujiwara M., Teramoto T., Ishihara T., Ohshima Y., McIntire S.L.;
RT "A novel zf-MYND protein, CHB-3, mediates guanylyl cyclase localization to
RT sensory cilia and controls body size of Caenorhabditis elegans.";
RL PLoS Genet. 6:E1001211-E1001211(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26434723; DOI=10.1534/genetics.115.177543;
RA Fujiwara M., Hino T., Miyamoto R., Inada H., Mori I., Koga M., Miyahara K.,
RA Ohshima Y., Ishihara T.;
RT "The importance of cGMP signaling in sensory cilia for body size regulation
RT in Caenorhabditis elegans.";
RL Genetics 201:1497-1510(2015).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (PubMed:9096403). Acts upstream of cGMP-dependent
CC protein kinase egl-4, most likely by providing cGMP to the kinase in
CC chemosensory neurons to regulate body size (PubMed:21124861,
CC PubMed:26434723). {ECO:0000269|PubMed:21124861,
CC ECO:0000269|PubMed:26434723, ECO:0000269|PubMed:9096403}.
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:0000269|PubMed:9096403};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 20-25 degrees Celsius. Loses activity at
CC temperatures above 35 degrees Celsius. {ECO:0000269|PubMed:9096403};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell projection, cilium
CC {ECO:0000269|PubMed:21124861, ECO:0000269|PubMed:26434723}. Perikaryon
CC {ECO:0000269|PubMed:26434723}. Cell projection, dendrite
CC {ECO:0000269|PubMed:26434723}. Note=Localization in cilium of sensory
CC neurons is regulated by daf-25 (PubMed:21124861). Cilia localization
CC may be important for regulating body size (PubMed:21124861). Localizes
CC to small puncta around the nucleus in the perikaryon (PubMed:26434723).
CC Enriched at the proximal segment of the cilia or at the distal dendrite
CC tip close to the cilia (PubMed:26434723). {ECO:0000269|PubMed:21124861,
CC ECO:0000269|PubMed:26434723}.
CC -!- TISSUE SPECIFICITY: Expressed in PHA sensory neurons and in head
CC muscles (PubMed:9096403, PubMed:21124861). Expressed in chemosensory
CC neurons AWC, ASE, ASJ, AUA, PHA and PHB, interneuron PVQ, several other
CC unidentified head neurons, an excretory gland cell and head muscles
CC (PubMed:26434723). Highly expressed in the sensory cila at the nose tip
CC (PubMed:26434723). {ECO:0000269|PubMed:21124861,
CC ECO:0000269|PubMed:26434723, ECO:0000269|PubMed:9096403}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Increased body size and increased formation of
CC dauer larvae. Double knockout with che-2 rescues the locomotion defect
CC in the single che-2 mutant. {ECO:0000269|PubMed:26434723}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; FO081082; CCD68976.2; -; Genomic_DNA.
DR RefSeq; NP_494995.2; NM_062594.2.
DR AlphaFoldDB; Q19187; -.
DR SMR; Q19187; -.
DR STRING; 6239.F08B1.2a.1; -.
DR GlyCosmos; Q19187; 7 sites, No reported glycans.
DR EPD; Q19187; -.
DR PaxDb; 6239-F08B1-2; -.
DR EnsemblMetazoa; F08B1.2a.1; F08B1.2a.1; WBGene00001538.
DR GeneID; 173902; -.
DR KEGG; cel:CELE_F08B1.2; -.
DR UCSC; F08B1.2; c. elegans.
DR AGR; WB:WBGene00001538; -.
DR WormBase; F08B1.2a; CE01900; WBGene00001538; gcy-12.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000168507; -.
DR HOGENOM; CLU_001072_0_0_1; -.
DR InParanoid; Q19187; -.
DR OMA; SIQGFDM; -.
DR OrthoDB; 2877804at2759; -.
DR PhylomeDB; Q19187; -.
DR PRO; PR:Q19187; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001538; Expressed in larva and 3 other cell types or tissues.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004016; F:adenylate cyclase activity; 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; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0061067; P:negative regulation of dauer larval development; IMP:UniProtKB.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IGI:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IGI:UniProtKB.
DR CDD; cd07302; CHD; 1.
DR CDD; cd14042; PK_GC-A_B; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
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; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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;
KW Coiled coil; Glycoprotein; GTP-binding; Lyase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..1679
FT /note="Receptor-type guanylate cyclase gcy-12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433281"
FT TOPO_DOM 45..592
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..1679
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 639..955
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1027..1158
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1412..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1534..1580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1623..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 961..997
FT /evidence="ECO:0000255"
FT COMPBIAS 1412..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 645..653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 696
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1032
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1032
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1033
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1076
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1076
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1679 AA; 189973 MW; 35828FA6A77EAB2E CRC64;
MWPTSVEALR FYHTFAFSPG RRRRLFGLSI VFVIAALCVT SCDADAVPAP SPEAEPSLGA
GANPYLLDSL VKRLPKKGDK KEILISYLAA VPTLMGEIDQ YLLNLSASNS AQNSSKDRES
FSKKLNQIVH CLTTDAYVSV VSGALVAAIV EINQDKDLIP AYQLKYVFGN TCGNDSHSTR
LFMEHWQAGA RVFIGPEKNC KTEAAMAASQ NLPIISYRCN DQDISRDDYH YRTFARTVPP
AGEIFKAFMS LMKQYNWRKF SVVYDVKKGQ VKNELFETLK RMVETENKFE EHKFEIMNVS
KLEFSKMDIS SQQDIQSIEN AIKSTMQTTR IYLTFDNVRL FRTMLSIMGE MGLTQQDYML
IYVDTNYDWL NVYHSMNNHF LRNTMTYLHH SWDANNSSDR KMLDYARSAL SIIPTPVKLN
SQRFYNFWKK AGDYMHHFGV QKADNLKGNR IACYLYDAVY LYAKAIHELV EEYGNDDSYD
PTADGKAIID RIVNKKYRSI QGFDMRIDER GNSKGNFSLL SWQKVAPIMN KSDPSYYPLD
HALDLTAIFV EAPDKDRLPN LQFKSSRIQW LKGEPPPDEP VCGFHGENCR KKGIFSYLTV
VVMILIAVFS LVLTGFTLNY IRSRRFEKEL SMIWKIDPYE VRRVVGGVNN ESTASLMQSD
VMQFAKTKTP WWSKAPVQGT GMRGLASYKG TLVGLKDLMY GRKPKDLTRE AKKELRAMRQ
LAHPNVNNFL GIIVCQYSVT VVREYCSKGS LHDILRNENL KLDHMYVASF VDDLVKGMVY
IHDSELKMHG NLKSTNCLIT SRWTLQIADF GLRELREGIM YDSSYNIWEN FLWTAPEAMT
INGSLAISNP PTPKADAYSF GIIFHEIFTR EGPYKIYVQR GDVNGEAAPK KDSVECRALV
EKTVRRVYSD PYFRPDTSDL EVQNYVKEVM AACWHHDPYQ RPEFKTIKNK LKPLFHQIYK
QNIMDHMVLM MEKYQTQLED LVDERTIELK DEQRRSQHLL QRMLPSSVAE QLLAGQDVIP
EAFPPVTIYF SDIVGFTTIS GESTPMEVVT FLNKLYTLFD SIIRRYDVYK VETIGDAYMV
VSGVPQYKTM EYHAEQIAMM AIHILSAVRS FSIPHRSCEP LMIRIGMHTG PCVAGVVGKT
MPRYTLFGDT VNTASRMESN GEALRIHCSS STQKVLTSID QGFLLEERGS LAIKGKGQMT
TYWLNGRAGY EFTETIEDKM VVPDIFPRPN LKNRGSSWGV NRESSLSLAT EKSSQIMKRQ
SAAMNRNNQD VIYYNQPLNS GGFTSRGTSN REMPKLYEED RESLLNQSAS LLGSRTSGRK
KSTASKYNGF SASRMFSSTI SNASSSRPSR PSTFDHDTLA LRKRSTSLPD GEKLNLEFIE
TTNLANNSVP AIPNNISSLE PVFRKASIID GYSSQSESPS QSQYPSYRDL TTGPHQRKRG
IATVFPVRKR SLSCGDAVPL KINENGASGS ITTAVSPRSS CRALDPTMKL AARASSPDEI
IFQEDDEDAL IDNDSLLTSN GNSKSEDVLR TCPQPRRKNK HSFLRDPSPL AKRFRDASPF
GKKKPFWNSN KSNEHTSSPA DSISRLFRRF RGGSVNEYAD LNHYCDDEDE SGRANGYEMQ
EMGKMTGRQR EQRNGSRTNR SVSCSPDECG TLTDSSDPHL TIPSSSIGDS SASTSLSCS
//
