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P51841 (GUC2F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinal guanylyl cyclase 2

Short name=RETGC-2
EC=4.6.1.2
Alternative name(s):
Guanylate cyclase 2F, retinal
Guanylate cyclase F
Short name=GC-F
Rod outer segment membrane guanylate cyclase 2
Short name=ROS-GC2
Gene names
Name:GUCY2F
Synonyms:GUC2F, RETGC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1108 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Enzyme regulation

Activated by GCAP-1; inhibited by calcium.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Retina. Localized exclusively in the outer nuclear layer and inner segments of the rod and cone photoreceptor cells.

Domain

The protein kinase domain is predicted to be catalytically inactive.

Post-translational modification

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.

Sequence similarities

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.

Contains 1 guanylate cyclase domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processcGMP biosynthesis
Sensory transduction
Vision
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   LigandGTP-binding
Nucleotide-binding
   Molecular functionLyase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular signal transduction

Inferred from electronic annotation. Source: InterPro

phototransduction, visible light

Traceable author statement. Source: Reactome

receptor guanylyl cyclase signaling pathway

Traceable author statement Ref.1. Source: ProtInc

regulation of rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

visual perception

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentintegral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

nuclear outer membrane

Traceable author statement Ref.1. Source: ProtInc

photoreceptor disc membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

guanylate cyclase activity

Traceable author statement Ref.1. Source: ProtInc

protein kinase activity

Inferred from electronic annotation. Source: InterPro

receptor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5050 Potential
Chain51 – 11081058Retinal guanylyl cyclase 2
PRO_0000012386

Regions

Topological domain51 – 467417Extracellular Potential
Transmembrane468 – 49023Helical; Potential
Topological domain491 – 1108618Cytoplasmic Potential
Domain532 – 812281Protein kinase
Domain884 – 1014131Guanylate cyclase

Amino acid modifications

Disulfide bond104 ↔ 132 By similarity
Disulfide bond452Interchain By similarity
Disulfide bond460Interchain By similarity

Natural variations

Natural variant101R → P in a breast cancer sample; somatic mutation. Ref.3
VAR_036419
Natural variant401S → C. Ref.4
Corresponds to variant rs34228145 [ dbSNP | Ensembl ].
VAR_042233
Natural variant1601I → N. Ref.4
Corresponds to variant rs33971675 [ dbSNP | Ensembl ].
VAR_042234
Natural variant2301R → W. Ref.4
Corresponds to variant rs33973457 [ dbSNP | Ensembl ].
VAR_042235
Natural variant2841L → P. Ref.4
Corresponds to variant rs12008095 [ dbSNP | Ensembl ].
VAR_009136
Natural variant2961R → Q. Ref.1
Corresponds to variant rs502209 [ dbSNP | Ensembl ].
VAR_009137
Natural variant3051R → Q. Ref.4
Corresponds to variant rs55966326 [ dbSNP | Ensembl ].
VAR_042236
Natural variant3081Y → C. Ref.4
Corresponds to variant rs16985750 [ dbSNP | Ensembl ].
VAR_030633
Natural variant3801Q → H. Ref.4
Corresponds to variant rs2272925 [ dbSNP | Ensembl ].
VAR_030634
Natural variant4341G → R. Ref.4
Corresponds to variant rs56293008 [ dbSNP | Ensembl ].
VAR_042237
Natural variant5681G → D in a glioblastoma multiforme sample; somatic mutation. Ref.4
VAR_042238
Natural variant6281R → Q. Ref.4
Corresponds to variant rs7883913 [ dbSNP | Ensembl ].
VAR_030635
Natural variant6771V → L. Ref.4
Corresponds to variant rs35474112 [ dbSNP | Ensembl ].
VAR_042239
Natural variant7941E → K. Ref.4
Corresponds to variant rs35726803 [ dbSNP | Ensembl ].
VAR_042240
Natural variant8721G → D. Ref.5
VAR_069424
Natural variant10101A → V. Ref.4
Corresponds to variant rs55735218 [ dbSNP | Ensembl ].
VAR_042241
Natural variant10521K → R in a lung adenocarcinoma sample; somatic mutation. Ref.4
VAR_042242
Natural variant10551E → D in a lung squamous cell carcinoma sample; somatic mutation. Ref.4
VAR_042243

Sequences

Sequence LengthMass (Da)Tools
P51841 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: B047BBF1A3C009F9

FASTA1,108124,850
        10         20         30         40         50         60 
MFLGLGRFSR LVLWFAAFRK LLGHHGLASA KFLWCLCLLS VMSLPQQVWT LPYKIGVVGP 

        70         80         90        100        110        120 
WACDSLFSKA LPEVAARLAI ERINRDPSFD LSYSFEYVIL NEDCQTSRAL SSFISHHQMA 

       130        140        150        160        170        180 
SGFIGPTNPG YCEAASLLGN SWDKGIFSWA CVNYELDNKI SYPTFSRTLP SPIRVLVTVM 

       190        200        210        220        230        240 
KYFQWAHAGV ISSDEDIWVH TANRVASALR SHGLPVGVVL TTGQDSQSMR KALQRIHQAD 

       250        260        270        280        290        300 
RIRIIIMCMH SALIGGETQM HLLECAHDLK MTDGTYVFVP YDALLYSLPY KHTPYRVLRN 

       310        320        330        340        350        360 
NPKLREAYDA VLTITVESQE KTFYQAFTEA AARGEIPEKL EFDQVSPLFG TIYNSIYFIA 

       370        380        390        400        410        420 
QAMNNAMKEN GQAGAASLVQ HSRNMQFHGF NQLMRTDSNG NGISEYVILD TNLKEWELHS 

       430        440        450        460        470        480 
TYTVDMEMEL LRFGGTPIHF PGGRPPRADA KCWFAEGKIC HGGIDPAFAM MVCLTLLIAL 

       490        500        510        520        530        540 
LSINGFAYFI RRRINKIQLI KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQITSEVQS 

       550        560        570        580        590        600 
GRSPRLSFSS GSLTPATYEN SNIAIYEGDW VWLKKFSLGD FGDLKSIKSR ASDVFEMMKD 

       610        620        630        640        650        660 
LRHENINPLL GFFYDSGMFA IVTEFCSRGS LEDILTNQDV KLDWMFKSSL LLDLIKGMKY 

       670        680        690        700        710        720 
LHHREFVHGR LKSRNCVVDG RFVLKVTDYG FNDILEMLRL SEEESSMEEL LWTAPELLRA 

       730        740        750        760        770        780 
PRGSRLGSFA GDVYSFAIIM QEVMVRGTPF CMMDLPAQEI INRLKKPPPV YRPVVPPEHA 

       790        800        810        820        830        840 
PPECLQLMKQ CWAEAAEQRP TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIR 

       850        860        870        880        890        900 
ERTEELEIEK QKTEKLLTQM LPPSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS 

       910        920        930        940        950        960 
EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGSRHA AEIANMSLDI 

       970        980        990       1000       1010       1020 
LSSVGTFKMR HMPEVPVRIR IGLHSGPVVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY 

      1030       1040       1050       1060       1070       1080 
RIHVSLSTVT ILQNLSEGYE VELRGRTELK GKGTEETFWL IGKKGFMKPL PVPPPVDKDG 

      1090       1100 
QVGHGLQPVE IAAFQRRKAE RQLVRNKP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a second photoreceptor-specific membrane retina guanylyl cyclase (RetGC), RetGC-2."
Lowe D.G., Dizhoor A.M., Liu K., Gu Q., Spencer M., Laura R., Lu L., Hurley J.B.
Proc. Natl. Acad. Sci. U.S.A. 92:5535-5539(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-296.
Tissue: Retina.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-10.
[4]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-40; ASN-160; TRP-230; PRO-284; GLN-305; CYS-308; HIS-380; ARG-434; ASP-568; GLN-628; LEU-677; LYS-794; VAL-1010; ARG-1052 AND ASP-1055.
[5]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-872.
+Additional computationally mapped references.

Web resources

Mutations of the GUCY2F gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L37378 mRNA. Translation: AAA74451.1.
AL031387 Genomic DNA. Translation: CAB41303.1.
CCDSCCDS14545.1.
PIRI59385.
RefSeqNP_001513.2. NM_001522.2.
UniGeneHs.123074.

3D structure databases

ProteinModelPortalP51841.
SMRP51841. Positions 584-855, 883-1083.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109241. 3 interactions.
IntActP51841. 2 interactions.
MINTMINT-7970335.
STRING9606.ENSP00000218006.

PTM databases

PhosphoSiteP51841.

Polymorphism databases

DMDM311033391.

Proteomic databases

PaxDbP51841.
PRIDEP51841.

Protocols and materials databases

DNASU2986.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000218006; ENSP00000218006; ENSG00000101890.
GeneID2986.
KEGGhsa:2986.
UCSCuc004eod.4. human.

Organism-specific databases

CTD2986.
GeneCardsGC0XM108616.
H-InvDBHIX0056276.
HGNCHGNC:4691. GUCY2F.
HPAHPA000734.
HPA027473.
MIM300041. gene.
neXtProtNX_P51841.
PharmGKBPA29071.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000293307.
HOVERGENHBG098487.
InParanoidP51841.
KOK12321.
OMANSIYFIA.
OrthoDBEOG7QVM1V.
PhylomeDBP51841.
TreeFamTF106338.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

BgeeP51841.
CleanExHS_GUCY2F.
GenevestigatorP51841.

Family and domain databases

Gene3D3.30.70.1230. 1 hit.
InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011645. Haem_no_assoc-bd.
IPR011009. Kinase-like_dom.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07701. HNOBA. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi2986.
NextBio11840.
PROP51841.
SOURCESearch...

Entry information

Entry nameGUC2F_HUMAN
AccessionPrimary (citable) accession number: P51841
Secondary accession number(s): Q9UJF1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM