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Protein

Retinal guanylyl cyclase 2

Gene

Gucy2f

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Activated by GCAP-1; inhibited by calcium.By similarity

GO - Molecular functioni

GO - Biological processi

  • detection of light stimulus involved in visual perception Source: CACAO
  • intracellular signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cGMP biosynthesis, Sensory transduction, Vision

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_311545. Inactivation, recovery and regulation of the phototransduction cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinal guanylyl cyclase 2 (EC:4.6.1.2)
Gene namesi
Name:Gucy2f
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:105119. Gucy2f.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini51 – 469419ExtracellularSequence AnalysisAdd
BLAST
Transmembranei470 – 49021HelicalSequence AnalysisAdd
BLAST
Topological domaini491 – 1108618CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5050Sequence AnalysisAdd
BLAST
Chaini51 – 11081058Retinal guanylyl cyclase 2PRO_0000280445Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi104 ↔ 132By similarity
Disulfide bondi452 – 452InterchainBy similarity
Disulfide bondi460 – 460InterchainBy similarity

Post-translational modificationi

There are 9 conserved cysteine residues in sensory guanylate cyclases, 6 in the extracellular domain, which may be involved in intra- or interchain disulfide bonds.By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ5SDA5.

PTM databases

PhosphoSiteiQ5SDA5.

Expressioni

Gene expression databases

BgeeiQ5SDA5.
CleanExiMM_GUCY2F.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000044521.

Structurei

3D structure databases

ProteinModelPortaliQ5SDA5.
SMRiQ5SDA5. Positions 571-803, 884-1060.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini532 – 812281Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini884 – 1014131Guanylate cyclasePROSITE-ProRule annotationAdd
BLAST

Domaini

The protein kinase domain is predicted to be catalytically inactive.

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000293307.
HOVERGENiHBG098487.
InParanoidiQ5SDA5.
KOiK12321.
OMAiNSIYFIA.
OrthoDBiEOG7QVM1V.
PhylomeDBiQ5SDA5.
TreeFamiTF106338.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5SDA5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLGPWPFSR LLSWFAISSR LSGQHGLPSS KFLRCLCLLA LLPLLRWGQA
60 70 80 90 100
LPYKIGVIGP WTCDPFFSKA LPEVAAALAI ERISRDKTFD RSYSFEYVIL
110 120 130 140 150
NEDCQTSKAL ASFISHQQMA SGFVGPANPG FCEAASLLGT SWDKGIFSWA
160 170 180 190 200
CVNHELDNKH SFPTFSRTLP SPIRVLVTVM KYFQWAHAGV ISSDEDIWMH
210 220 230 240 250
TANRVSSALR SQGLPVGVVL TSGRDSQSIQ KALQQIRQAD RIRIIIMCMH
260 270 280 290 300
SALIGGETQT HFLELAHDLK MTDGTYVFVP YDVLLYSLPY KHSPYQVLRN
310 320 330 340 350
NPKLREAYDA VLTITVESHE KTFYEAYAEA AARGEIPEKP DSNQVSPLFG
360 370 380 390 400
TIYNSIYFIA QAMNNAMKKN GRASAASLVQ HSRNMQFYGF NQLIKTDSNG
410 420 430 440 450
NGISEYVILD TNGKEWELRG TYTVDMETEL LRFRGTPIHF PGGRPTSADA
460 470 480 490 500
KCWFAERKIC QGGIDPALAM MVCFALLIAL LSINGFAYFI RRRINKIQLI
510 520 530 540 550
KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQIISEVQS GRSPRLSFSS
560 570 580 590 600
GSLTPATYEN SNIAIYEGDW VWLKKFPPGD FGDIKSIKSS ASDVFEMMKD
610 620 630 640 650
LRHENVNPLL GFFYDSGMFA IVSEFCSRRS LEDILTNDDV KLDWMFKSSL
660 670 680 690 700
LLDLIKGMKY LHHREFIHGR LKSRNCVVDG RFVLKVTDYG FNDILEMLRL
710 720 730 740 750
SEEEPSEEEL LWTAPELLRA PGGIRLGSFA GDVYSFAIIM QEVMVRGAPF
760 770 780 790 800
CMMDLPAKEI IDRLKMPPPV YRPVVSPEYA PAECLQLMKQ CWAEASEQRP
810 820 830 840 850
TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIR ERTEELEIEK
860 870 880 890 900
QKTEKLLTQM LPLSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS
910 920 930 940 950
EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGSRHA
960 970 980 990 1000
AEIANMSLDI LSSVGTFKMR HMPEVPVRIR IGLHSGPVVA GVVGLTMPRY
1010 1020 1030 1040 1050
CLFGDTVNTA SRMESTGLPY RIHVSLSTVT ILQTLSEGYE VELRGRTELK
1060 1070 1080 1090 1100
GKGTEETFWL VGKKGFTKPL PVPPPVGKDG QVGHGLQPAE IAAFQRRKAE

RQLVRNKP
Length:1,108
Mass (Da):124,425
Last modified:December 21, 2004 - v1
Checksum:i8A1456FCB384FA90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY651761 mRNA. Translation: AAV54098.1.
AL671916, BX324191 Genomic DNA. Translation: CAM19986.1.
BX324191, AL671916 Genomic DNA. Translation: CAM24899.1.
BC115714 mRNA. Translation: AAI15715.1.
AK044234 mRNA. Translation: BAC31833.1.
CCDSiCCDS30446.1.
RefSeqiNP_001007577.1. NM_001007576.2.
XP_006528904.1. XM_006528841.2.
UniGeneiMm.208511.

Genome annotation databases

EnsembliENSMUST00000042530; ENSMUSP00000044521; ENSMUSG00000042282.
GeneIDi245650.
KEGGimmu:245650.
UCSCiuc009ulq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY651761 mRNA. Translation: AAV54098.1.
AL671916, BX324191 Genomic DNA. Translation: CAM19986.1.
BX324191, AL671916 Genomic DNA. Translation: CAM24899.1.
BC115714 mRNA. Translation: AAI15715.1.
AK044234 mRNA. Translation: BAC31833.1.
CCDSiCCDS30446.1.
RefSeqiNP_001007577.1. NM_001007576.2.
XP_006528904.1. XM_006528841.2.
UniGeneiMm.208511.

3D structure databases

ProteinModelPortaliQ5SDA5.
SMRiQ5SDA5. Positions 571-803, 884-1060.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000044521.

PTM databases

PhosphoSiteiQ5SDA5.

Proteomic databases

PRIDEiQ5SDA5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042530; ENSMUSP00000044521; ENSMUSG00000042282.
GeneIDi245650.
KEGGimmu:245650.
UCSCiuc009ulq.2. mouse.

Organism-specific databases

CTDi2986.
MGIiMGI:105119. Gucy2f.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000293307.
HOVERGENiHBG098487.
InParanoidiQ5SDA5.
KOiK12321.
OMAiNSIYFIA.
OrthoDBiEOG7QVM1V.
PhylomeDBiQ5SDA5.
TreeFamiTF106338.

Enzyme and pathway databases

ReactomeiREACT_311545. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

NextBioi386884.
PROiQ5SDA5.
SOURCEiSearch...

Gene expression databases

BgeeiQ5SDA5.
CleanExiMM_GUCY2F.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Application of functional genomic technologies in a mouse model of retinal degeneration."
    Shearstone J.R., Wang Y.E., Clement A., Allaire N.E., Yang C., Worley D.S., Carulli J.P., Perrin S.
    Genomics 85:309-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Retina.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-846.
    Strain: C57BL/6J.
    Tissue: Retina.

Entry informationi

Entry nameiGUC2F_MOUSE
AccessioniPrimary (citable) accession number: Q5SDA5
Secondary accession number(s): Q8BLL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: December 21, 2004
Last modified: June 24, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.