GC76C_DROME
ID GC76C_DROME Reviewed; 1525 AA.
AC Q7JQ32; Q24051;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Receptor-type guanylate cyclase Gyc76C {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000255, ECO:0000255|RuleBase:RU003431, ECO:0000269|PubMed:24284209};
DE AltName: Full=DrGC-1 {ECO:0000303|PubMed:7706258};
DE Flags: Precursor;
GN Name=Gyc76C {ECO:0000312|FlyBase:FBgn0266136};
GN ORFNames=CG42636 {ECO:0000312|FlyBase:FBgn0266136};
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 {ECO:0000312|EMBL:AAA74408.1};
RN [1] {ECO:0000312|EMBL:AAA74408.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=7706258; DOI=10.1074/jbc.270.13.7189;
RA McNeil L., Chinkers M., Forte M.;
RT "Identification, characterization, and developmental regulation of a
RT receptor guanylyl cyclase expressed during early stages of Drosophila
RT development.";
RL J. Biol. Chem. 270:7189-7196(1995).
RN [2] {ECO:0000312|EMBL:AAA85858.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7759483; DOI=10.1074/jbc.270.21.12418;
RA Liu W., Yoon J., Burg M., Chen L., Pak W.L.;
RT "Molecular characterization of two Drosophila guanylate cyclases expressed
RT in the nervous system.";
RL J. Biol. Chem. 270:12418-12427(1995).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAR31133.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAR31133.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAR31133.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=15282266; DOI=10.1523/jneurosci.1104-04.2004;
RA Ayoob J.C., Yu H.H., Terman J.R., Kolodkin A.L.;
RT "The Drosophila receptor guanylyl cyclase Gyc76C is required for
RT semaphorin-1a-plexin A-mediated axonal repulsion.";
RL J. Neurosci. 24:6639-6649(2004).
RN [7] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23213443; DOI=10.1242/bio.2012943;
RA Patel U., Davies S.A., Myat M.M.;
RT "Receptor-type guanylyl cyclase Gyc76C is required for development of the
RT Drosophila embryonic somatic muscle.";
RL Biol. Open 1:507-515(2012).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21893139; DOI=10.1016/j.peptides.2011.08.019;
RA Overend G., Cabrero P., Guo A.X., Sebastian S., Cundall M., Armstrong H.,
RA Mertens I., Schoofs L., Dow J.A., Davies S.A.;
RT "The receptor guanylate cyclase Gyc76C and a peptide ligand, NPLP1-VQQ,
RT modulate the innate immune IMD pathway in response to salt stress.";
RL Peptides 34:209-218(2012).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23862019; DOI=10.1242/bio.20134887;
RA Patel U., Myat M.M.;
RT "Receptor guanylyl cyclase Gyc76C is required for invagination, collective
RT migration and lumen shape in the Drosophila embryonic salivary gland.";
RL Biol. Open 2:711-717(2013).
RN [10] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH KERMIT
RP AND PLEXA, AND MUTAGENESIS OF ASP-945.
RX PubMed=24284209; DOI=10.1242/dev.095968;
RA Chak K., Kolodkin A.L.;
RT "Function of the Drosophila receptor guanylyl cyclase Gyc76C in PlexA-
RT mediated motor axon guidance.";
RL Development 141:136-147(2014).
RN [11] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-635.
RX PubMed=26440503; DOI=10.1371/journal.pgen.1005576;
RA Schleede J., Blair S.S.;
RT "The Gyc76C receptor guanylyl cyclase and the foraging cGMP-dependent
RT kinase regulate extracellular matrix organization and BMP signaling in the
RT developing wing of Drosophila melanogaster.";
RL PLoS Genet. 11:E1005576-E1005576(2015).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (PubMed:24284209). Acts as a receptor for the NPLP1-4
CC peptide and modulates the innate immune IMD pathway in response to salt
CC stress by inducing nuclear translocation of NF-kappa-B protein Rel
CC which leads to increased expression of the antimicrobial peptide
CC diptericin (PubMed:21893139). Plays a role in Sema-1a-mediated axon
CC repulsion which is required for the correct establishment of
CC neuromuscular connectivity (PubMed:15282266, PubMed:24284209). Required
CC in developing embryonic somatic muscle for correct patterning of
CC ventral and lateral muscles and for localization of integrin beta-ps at
CC developing dorsal muscle myotendinous junctions (PubMed:23213443).
CC Required for invagination, migration and lumen shape of the embryonic
CC salivary gland by regulating the localization of the integrin-binding
CC protein rhea/Talin to the visceral mesoderm surrounding the gland and
CC maintaining the laminin matrix (PubMed:23862019). Required in the
CC developing wing to regulate extracellular matrix (ECM) organization by
CC activating the cGMP-dependent protein kinase For which represses the
CC activity of matrix metalloproteases such as Mmp2 and decreases ECM
CC matrix reorganization (PubMed:26440503). {ECO:0000269|PubMed:15282266,
CC ECO:0000269|PubMed:21893139, ECO:0000269|PubMed:23213443,
CC ECO:0000269|PubMed:23862019, ECO:0000269|PubMed:24284209,
CC ECO:0000269|PubMed:26440503}.
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:0000255, ECO:0000255|RuleBase:RU003431,
CC ECO:0000269|PubMed:24284209};
CC -!- SUBUNIT: Interacts with the semaphorin 1A receptor PlexA; PlexA
CC enhances Gyc76C catalytic activity. Interacts with the PDZ domain-
CC containing protein kermit; kermit increases cell surface expression of
CC Gyc76C. {ECO:0000269|PubMed:24284209}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24284209};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In the adult, widely distributed in the head and
CC thorax with highest levels in the optic lobe and central brain and
CC expression also detected in the retina (PubMed:7759483). Expressed at
CC similar levels in adult head and body (PubMed:7759483). In females,
CC highly expressed in oocytes with lower levels in the digestive tract
CC (PubMed:7759483). In mid-embryogenesis, enriched in the circular
CC visceral mesoderm that overlies the migrating salivary gland and in the
CC fat body that underlies the gland but at background levels in the gland
CC itself (PubMed:23213443). In late embryogenesis, detected in the mature
CC salivary gland, in the somatic body wall muscles and the tendon cells
CC to which the muscles attach, and in the constricting midgut
CC (PubMed:23213443). Also expressed in migrating tracheal cells at mid-
CC embryogenesis and in the developed trachea at the end of embryogenesis
CC with enrichment in the apical domains (PubMed:23213443).
CC {ECO:0000269|PubMed:23213443, ECO:0000269|PubMed:7759483}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo, larva, pupa and adult
CC (PubMed:7706258, PubMed:7759483). Expressed at very high levels in
CC early cleavage stage embryos at 0-2 hours followed by lower expression
CC at 2-6 and 6-10 hours of embryogenesis (PubMed:7706258). During later
CC stages of embryogenesis at 10-14 and 14-18 hours, expressed again at
CC high levels, particularly in muscle fibers (PubMed:7706258). Very low
CC levels in larval and pupal stages (PubMed:7706258).
CC {ECO:0000269|PubMed:7706258, ECO:0000269|PubMed:7759483}.
CC -!- DOMAIN: The guanylate cyclase domain is required for Sema-1a-mediated
CC axon repulsion. {ECO:0000269|PubMed:15282266}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: Abnormal patterning of the somatic body wall
CC muscles with numerous ventral and lateral muscles that fail to extend
CC or are missing and reduced levels of integrin beta-ps at dorsal muscle
CC myotendinous junctions (PubMed:23213443). Defects in salivary gland
CC invagination, migration and lumen shape and mislocalization of the
CC integrin-binding protein rhea/Talin (PubMed:23862019). Defects in motor
CC axon guidance with failure of motor axons to defasciculate from one
CC another and innervate their proper muscle targets (PubMed:15282266).
CC Wings display disrupted posterior crossveins (PubMed:26440503). RNAi-
CC mediated knockdown in malpighian tubule principal cells inhibits NPLP1-
CC 4-mediated increases in fluid transport rates and cGMP levels, inhibits
CC NPLP1-4-mediated nuclear translocation of NF-kappa-B protein Rel and
CC abolishes expression of the antimicrobial peptide diptericin
CC (PubMed:21893139). {ECO:0000269|PubMed:15282266,
CC ECO:0000269|PubMed:21893139, ECO:0000269|PubMed:23213443,
CC ECO:0000269|PubMed:23862019, ECO:0000269|PubMed:26440503}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255, ECO:0000255|RuleBase:RU000405}.
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DR EMBL; L35598; AAA74408.1; -; mRNA.
DR EMBL; U23485; AAA85858.1; -; mRNA.
DR EMBL; AE014296; ACZ94744.1; -; Genomic_DNA.
DR EMBL; AE014296; ACZ94745.1; -; Genomic_DNA.
DR EMBL; AE014296; ACZ94746.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94756.1; -; Genomic_DNA.
DR EMBL; BT011062; AAR31133.1; -; mRNA.
DR PIR; A56699; A56699.
DR RefSeq; NP_001007096.1; NM_001007095.3.
DR RefSeq; NP_001007097.1; NM_001007096.3.
DR RefSeq; NP_001163473.1; NM_001170002.1.
DR RefSeq; NP_001163474.1; NM_001170003.2.
DR RefSeq; NP_001163475.1; NM_001170004.2.
DR RefSeq; NP_001262063.1; NM_001275134.1.
DR RefSeq; NP_524165.2; NM_079441.4.
DR AlphaFoldDB; Q7JQ32; -.
DR IntAct; Q7JQ32; 8.
DR STRING; 7227.FBpp0291484; -.
DR GlyGen; Q7JQ32; 9 sites.
DR PaxDb; Q7JQ32; -.
DR PRIDE; Q7JQ32; -.
DR EnsemblMetazoa; FBtr0302277; FBpp0291483; FBgn0261360.
DR EnsemblMetazoa; FBtr0302278; FBpp0291484; FBgn0261360.
DR EnsemblMetazoa; FBtr0302279; FBpp0291485; FBgn0261360.
DR EnsemblMetazoa; FBtr0302280; FBpp0291486; FBgn0266136.
DR EnsemblMetazoa; FBtr0302281; FBpp0291487; FBgn0266136.
DR EnsemblMetazoa; FBtr0302282; FBpp0291488; FBgn0266136.
DR EnsemblMetazoa; FBtr0333879; FBpp0306011; FBgn0266136.
DR GeneID; 40153; -.
DR GeneID; 8674026; -.
DR KEGG; dme:Dmel_CG42636; -.
DR KEGG; dme:Dmel_CG42637; -.
DR CTD; 8674026; -.
DR FlyBase; FBgn0266136; Gyc76C.
DR VEuPathDB; VectorBase:FBgn0261360; -.
DR VEuPathDB; VectorBase:FBgn0266136; -.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000168507; -.
DR HOGENOM; CLU_001072_1_1_1; -.
DR InParanoid; Q7JQ32; -.
DR OMA; PTDEPMC; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; Q7JQ32; -.
DR SignaLink; Q7JQ32; -.
DR ChiTaRS; Gyc76C; fly.
DR PRO; PR:Q7JQ32; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0261360; Expressed in midgut and 12 other tissues.
DR ExpressionAtlas; Q7JQ32; baseline.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; 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:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001653; F:peptide receptor activity; IPI:FlyBase.
DR GO; GO:0030215; F:semaphorin receptor binding; IPI:FlyBase.
DR GO; GO:0038023; F:signaling receptor activity; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IGI:FlyBase.
DR GO; GO:0016199; P:axon midline choice point recognition; IGI:FlyBase.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0007428; P:primary branching, open tracheal system; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IDA:FlyBase.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; cGMP biosynthesis; Glycoprotein; GTP-binding;
KW Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1525
FT /note="Receptor-type guanylate cyclase Gyc76C"
FT /id="PRO_5007213161"
FT TOPO_DOM 20..493
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..1525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 547..824
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 896..1026
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1122..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 553..561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 581
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 901
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 901
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 902
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 945
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 945
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 635
FT /note="L->H: In 3L043; complete loss of the posterior
FT crossvein in adult wings."
FT /evidence="ECO:0000269|PubMed:26440503"
FT MUTAGEN 945
FT /note="D->A: Abolishes guanylate cyclase activity but does
FT not affect cell surface location."
FT /evidence="ECO:0000269|PubMed:24284209"
FT CONFLICT 381
FT /note="A -> S (in Ref. 2; AAA85858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1525 AA; 170503 MW; 5055D253FD398D30 CRC64;
MTRWPFNLLL LLSVAVRDCS NHRTVLTVGY LTALTGDLKT RQGLAISGAL TMALDEVNKD
PNLLPNVYLD LRWNDTKGDT VLATKAITEM ICDGIATIFG PEGPCYVEAI VSQSRNIPMI
SYKCAEYRAS AIPTFARTEP PDTQVVKSLL ALLRYYAWNK FSILYEDVWS PVADLLKDQA
TKRNMTINHK QSFIDNRVKC CEQMLDCCRS GYWYQLVQNT MNRTRIYVFL GAANSLVDFM
SSMETAGLFA RGEYMVIFVD MMVYSEREAE KYLRRVDQIT FMSNCHSTEN FNQMARSLLV
VASTPPTKDY IQFTKQVQKY SSKPPFNLEI PRLFVESNFS KFISIYAAYL YDSVKLYAWA
VDKMLREETR VLTDDVIFEV ASNGTRVIDT IIKNRTYMSI TGSKIKIDQY GDSEGNFSVL
AYKPHKWNNS NNMPCNYHMV PVAYFHQGEE HPEYKLINGS IDWPSGGEKP ADEPMCGFAN
ELCKKDDTHY TSTVAAVVLG VLLFCSGVIT MSIYRKWKIE LEIEGLLWKI DPNEIKGYSG
NEIVSSPSKV SLMSAQSYGS RWTNQFVTST GRLRGAVVRI KELKFPRKRD ISREIMKEMR
LLRELRHDNI NSFIGASVEP TRILLVTDYC AKGSLYDIIE NEDIKLDDLF IASLIHDLIK
GMIYIHNSQL VYHGNLKSSN CVVTSRWMLQ VTDFGLHELR QCAENESIGE HQHYRNQLWR
APELLRNHIH GSQKGDVYAF AIIMYEIFSR KGPFGQINFE PKEIVDYVKK LPLKGEDPFR
PEVESIIEAE SCPDYVLACI RDCWAEDPEE RPEFSVIRNR LKKMRGGKTK NIMDQMMEMM
EKYANNLEDI VTERTRLLCE EKMKTEDLLH RMLPQSVAEK LTMGQGVEPV SYDLVTIYFS
DIVGFTAMSA ESTPLQVVNF LNDLYTVFDR IIRGYDVYKV ETIGDAYMVV SGLPIKNGDR
HAGEIASMAL ELLHAVKQHR IAHRPNETLK LRIGMHTGPV VAGVVGLTMP RYCLFGDTVN
TASRMESNGE ALKIHISNKC KLALDKLGGG YITEKRGLVN MKGKGDVVTW WLTGANENAI
QKKLVDMMDM PPPLFSRPRK SPKLNPDSRQ PSIQAMHFCG TGSRRQSTVP RAMDGESTYS
LQGSVRESPR MVSKRDRDRE RPPINGLGAG HFVGGALLES AQASLSTLNH SETNETNCDM
DGGSGGVSGS GSGLVRQPNA LHKPLAMVRP HRIISAAQLP QLGDNDDDSA DTLLRESRSL
DPMPMQQLRK RHDRVKLPPS KLSKNNSRSL DTGVSLISGN PNGEVHSSQL DLDNEMTANP
VDATDGYDDE LGLLMRHDNG QLPALRYSGS FPNAQISIVP TGRSAGGGGG GREGGGSNCA
KHLNNNCNGG VNVEDDLESP LLQRQASLSV PPEEMLAHNK RWHSLEHMDG PGGHGGNSVS
YAADIDNRHP GDLDFFSGSS NQHHRSKAAG GSKLTNWMTN IFKGNGVRSG EARRVGILPS
GVHGARTGFT DMAASAAARD RESIV
