GCYH_DROME
ID GCYH_DROME Reviewed; 676 AA.
AC Q07093; Q24085; Q95SQ4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Head-specific guanylate cyclase;
DE EC=4.6.1.2 {ECO:0000269|PubMed:7797526};
DE AltName: Full=Guanylyl cyclase alpha 1 subunit {ECO:0000303|PubMed:7797526};
DE Short=Dgcalpha1 {ECO:0000303|PubMed:7797526};
DE AltName: Full=Gycalpha99B;
GN Name=Gycalpha99B; Synonyms=dgc1, GYC, GYC-ALPHA-63A, Gyc99B;
GN ORFNames=CG1912;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=8095978; DOI=10.1111/j.1471-4159.1993.tb03324.x;
RA Yoshikawa S., Miyamoto I., Aruga J., Furuichi T., Okano H., Mikoshiba K.;
RT "Isolation of a Drosophila gene encoding a head-specific guanylyl
RT cyclase.";
RL J. Neurochem. 60:1570-1573(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP SUBUNIT.
RC STRAIN=Oregon-R;
RX PubMed=7797526; DOI=10.1074/jbc.270.25.15368;
RA Shah S., Hyde D.R.;
RT "Two Drosophila genes that encode the alph and beta subunits of the brain
RT soluble guanylyl cyclase.";
RL J. Biol. Chem. 270:15368-15376(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: May have a role in phototransduction (PubMed:8095978).
CC Catalyzes the conversion of GTP to cGMP, a common second messenger that
CC is utilized in a wide variety of cells and signal transduction pathways
CC (PubMed:7797526). A second subunit is required for enzyme activity
CC (PubMed:7797526). {ECO:0000269|PubMed:7797526,
CC ECO:0000269|PubMed:8095978}.
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:7797526};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC Evidence={ECO:0000305|PubMed:7797526};
CC -!- SUBUNIT: Heterodimer. {ECO:0000305|PubMed:7797526}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Head, where it is preferentially expressed in the
CC CNS and the retina (PubMed:8095978, PubMed:7797526). Not found in
CC bodies (PubMed:8095978). {ECO:0000269|PubMed:7797526,
CC ECO:0000269|PubMed:8095978}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB25820.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S57126; AAB25820.1; ALT_FRAME; mRNA.
DR EMBL; U27117; AAA87940.1; -; mRNA.
DR EMBL; AE014297; AAF56917.1; -; Genomic_DNA.
DR EMBL; AY060654; AAL28202.1; -; mRNA.
DR PIR; JH0810; JH0810.
DR RefSeq; NP_477088.2; NM_057740.4.
DR AlphaFoldDB; Q07093; -.
DR SMR; Q07093; -.
DR BioGRID; 68357; 1.
DR STRING; 7227.FBpp0084819; -.
DR PaxDb; Q07093; -.
DR EnsemblMetazoa; FBtr0085453; FBpp0084819; FBgn0013972.
DR GeneID; 43493; -.
DR KEGG; dme:Dmel_CG1912; -.
DR CTD; 43493; -.
DR FlyBase; FBgn0013972; Gycalpha99B.
DR VEuPathDB; VectorBase:FBgn0013972; -.
DR eggNOG; KOG4171; Eukaryota.
DR GeneTree; ENSGT00940000169967; -.
DR HOGENOM; CLU_011614_5_0_1; -.
DR InParanoid; Q07093; -.
DR OMA; PLVEHIN; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; Q07093; -.
DR BioGRID-ORCS; 43493; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43493; -.
DR PRO; PR:Q07093; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0013972; Expressed in brain and 7 other tissues.
DR ExpressionAtlas; Q07093; baseline and differential.
DR Genevisible; Q07093; DM.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IDA:FlyBase.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0046956; P:positive phototaxis; IMP:FlyBase.
DR GO; GO:0070482; P:response to oxygen levels; IBA:GO_Central.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.450.260; -; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR Gene3D; 3.90.1520.10; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR038158; H-NOX_domain_sf.
DR InterPro; IPR011644; Heme_NO-bd.
DR InterPro; IPR011645; HNOB_dom_associated.
DR InterPro; IPR042463; HNOB_dom_associated_sf.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07700; HNOB; 1.
DR Pfam; PF07701; HNOBA; 2.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF111126; SSF111126; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 1: Evidence at protein level;
KW cGMP biosynthesis; Cytoplasm; GTP-binding; Lyase; Nucleotide-binding;
KW Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..676
FT /note="Head-specific guanylate cyclase"
FT /id="PRO_0000074121"
FT DOMAIN 466..593
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
SQ SEQUENCE 676 AA; 75663 MW; CE8097E1EC3787F8 CRC64;
MACPFFRRAD SLTRQPSVIA EPGGHWALED EELSDDALTL THLQMAIQLL TAPSNEDLNT
AVTSLVAKYR QNWPNIHKLK LDPQTFKSCA NYDYLADIQE LLLKMDEASA SEILVLLGEE
LITCCCTGII ERAFRCLGTD LQEFLGSLDG VYDVLKLQEE DVTDTGFVCA GEGELIFTSE
RPVIAWLLLG SLKALTRMLY KVDVNIKIEP VEGDARRYRY LFSLVKDNSQ TMLMGRPTSV
SKTIPETVQR SNSSNASDLQ MNSSSFCKMF PWHFIMNEQL ELVQLGRGFS KLYKPYMADF
GCQATTYFDF KRPKGLTMKF RDIVRRTYTP FLIGLNNPPG AVDFPAIGLE IKGQMVHCPE
SNSLLFIGSP FLDGLDGLTC NGLFISDIPL HDATREVILV GEQARAQDGL RRRMDKIKNS
IEEANSAVTK ERKKNVSLLH LIFPAEIAEK LWLGSSIDAK TYPDVTILFS DIVGFTSICS
RATPFMVISM LEGLYKDFDE FCDFFDVYKV ETIGDAYCVA SGLHRASIYD AHKVAWMALK
MIDACSKHIT HDGEQIKMRI GLHTGTVLAG VVGRKMPRYC LFGHSVTIAN KFESGSEALK
INVSPTTKDW LTKHEGFEFE LQPRDPSFLP KEFPNPGGTE TCYFLESFRN PALDSELPLV
EHINVSMKTI SEGGDA
