Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Head-specific guanylate cyclase

Gene

Gycalpha99B

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

May have a role in phototransduction. A second subunit may be required for enzyme activity.1 Publication

Catalytic activityi

GTP = 3',5'-cyclic GMP + diphosphate.

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • guanylate cyclase activity Source: FlyBase
  • heme binding Source: InterPro

GO - Biological processi

  • intracellular signal transduction Source: InterPro
  • positive phototaxis Source: FlyBase
  • rhodopsin mediated signaling pathway Source: FlyBase
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cGMP biosynthesis, Sensory transduction, Vision

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Head-specific guanylate cyclase (EC:4.6.1.2)
Alternative name(s):
Gycalpha99B
Gene namesi
Name:Gycalpha99B
Synonyms:dgc1, GYC, GYC-ALPHA-63A, Gyc99B
ORF Names:CG1912
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0013972. Gycalpha99B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • guanylate cyclase complex, soluble Source: FlyBase
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 676676Head-specific guanylate cyclasePRO_0000074121Add
BLAST

Proteomic databases

PaxDbiQ07093.

Expressioni

Tissue specificityi

Head, where it is preferentially expressed in the CNS and the retina. Not found in bodies.1 Publication

Gene expression databases

BgeeiQ07093.
ExpressionAtlasiQ07093. differential.
GenevisibleiQ07093. DM.

Interactioni

Subunit structurei

Dimer.Curated

Protein-protein interaction databases

STRINGi7227.FBpp0084819.

Structurei

3D structure databases

ProteinModelPortaliQ07093.
SMRiQ07093. Positions 264-379, 457-649.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini466 – 593128Guanylate cyclasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4171. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
InParanoidiQ07093.
KOiK12318.
OMAiHWALEDE.
OrthoDBiEOG7SFHW6.
PhylomeDBiQ07093.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011644. Heme_NO-bd.
IPR011645. HNOB_dom_associated.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF00211. Guanylate_cyc. 1 hit.
PF07700. HNOB. 1 hit.
PF07701. HNOBA. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF111126. SSF111126. 1 hit.
SSF55073. SSF55073. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07093-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACPFFRRAD SLTRQPSVIA EPGGHWALED EELSDDALTL THLQMAIQLL
60 70 80 90 100
TAPSNEDLNT AVTSLVAKYR QNWPNIHKLK LDPQTFKSCA NYDYLADIQE
110 120 130 140 150
LLLKMDEASA SEILVLLGEE LITCCCTGII ERAFRCLGTD LQEFLGSLDG
160 170 180 190 200
VYDVLKLQEE DVTDTGFVCA GEGELIFTSE RPVIAWLLLG SLKALTRMLY
210 220 230 240 250
KVDVNIKIEP VEGDARRYRY LFSLVKDNSQ TMLMGRPTSV SKTIPETVQR
260 270 280 290 300
SNSSNASDLQ MNSSSFCKMF PWHFIMNEQL ELVQLGRGFS KLYKPYMADF
310 320 330 340 350
GCQATTYFDF KRPKGLTMKF RDIVRRTYTP FLIGLNNPPG AVDFPAIGLE
360 370 380 390 400
IKGQMVHCPE SNSLLFIGSP FLDGLDGLTC NGLFISDIPL HDATREVILV
410 420 430 440 450
GEQARAQDGL RRRMDKIKNS IEEANSAVTK ERKKNVSLLH LIFPAEIAEK
460 470 480 490 500
LWLGSSIDAK TYPDVTILFS DIVGFTSICS RATPFMVISM LEGLYKDFDE
510 520 530 540 550
FCDFFDVYKV ETIGDAYCVA SGLHRASIYD AHKVAWMALK MIDACSKHIT
560 570 580 590 600
HDGEQIKMRI GLHTGTVLAG VVGRKMPRYC LFGHSVTIAN KFESGSEALK
610 620 630 640 650
INVSPTTKDW LTKHEGFEFE LQPRDPSFLP KEFPNPGGTE TCYFLESFRN
660 670
PALDSELPLV EHINVSMKTI SEGGDA
Length:676
Mass (Da):75,663
Last modified:June 21, 2005 - v2
Checksum:iCE8097E1EC3787F8
GO

Sequence cautioni

The sequence AAB25820.1 differs from that shown. Reason: Frameshift at several positions. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S57126 mRNA. Translation: AAB25820.1. Frameshift.
U27117 mRNA. Translation: AAA87940.1.
AE014297 Genomic DNA. Translation: AAF56917.1.
AY060654 mRNA. Translation: AAL28202.1.
PIRiJH0810.
RefSeqiNP_477088.2. NM_057740.4.
UniGeneiDm.3968.

Genome annotation databases

EnsemblMetazoaiFBtr0085453; FBpp0084819; FBgn0013972.
GeneIDi43493.
KEGGidme:Dmel_CG1912.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S57126 mRNA. Translation: AAB25820.1. Frameshift.
U27117 mRNA. Translation: AAA87940.1.
AE014297 Genomic DNA. Translation: AAF56917.1.
AY060654 mRNA. Translation: AAL28202.1.
PIRiJH0810.
RefSeqiNP_477088.2. NM_057740.4.
UniGeneiDm.3968.

3D structure databases

ProteinModelPortaliQ07093.
SMRiQ07093. Positions 264-379, 457-649.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0084819.

Proteomic databases

PaxDbiQ07093.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085453; FBpp0084819; FBgn0013972.
GeneIDi43493.
KEGGidme:Dmel_CG1912.

Organism-specific databases

CTDi43493.
FlyBaseiFBgn0013972. Gycalpha99B.

Phylogenomic databases

eggNOGiKOG4171. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
InParanoidiQ07093.
KOiK12318.
OMAiHWALEDE.
OrthoDBiEOG7SFHW6.
PhylomeDBiQ07093.

Miscellaneous databases

GenomeRNAii43493.
PROiQ07093.

Gene expression databases

BgeeiQ07093.
ExpressionAtlasiQ07093. differential.
GenevisibleiQ07093. DM.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011644. Heme_NO-bd.
IPR011645. HNOB_dom_associated.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF00211. Guanylate_cyc. 1 hit.
PF07700. HNOB. 1 hit.
PF07701. HNOBA. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF111126. SSF111126. 1 hit.
SSF55073. SSF55073. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a Drosophila gene encoding a head-specific guanylyl cyclase."
    Yoshikawa S., Miyamoto I., Aruga J., Furuichi T., Okano H., Mikoshiba K.
    J. Neurochem. 60:1570-1573(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: Canton-S.
    Tissue: Head.
  2. "Two Drosophila genes that encode the alph and beta subunits of the brain soluble guanylyl cyclase."
    Shah S., Hyde D.R.
    J. Biol. Chem. 270:15368-15376(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiGCYH_DROME
AccessioniPrimary (citable) accession number: Q07093
Secondary accession number(s): Q24085, Q95SQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 21, 2005
Last modified: July 6, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.