P51842 (GUC2F_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1108 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed only in the eye.
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 process	Sensory transduction Vision cGMP biosynthesis
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	GTP-binding Nucleotide-binding
Molecular function	Lyase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from direct assay Ref.1. Source: RGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro GTP binding Inferred from electronic annotation. Source: UniProtKB-KW guanylate cyclase activity Inferred from direct assay Ref.1. Source: RGD protein homodimerization activity Inferred from direct assay PubMed 9153227. Source: RGD protein kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 50	50	Potential
	Chain	51 – 1108	1058	Retinal guanylyl cyclase 2		PRO_0000012387
Regions
	Topological domain	51 – 465	415	Extracellular Potential
	Transmembrane	466 – 490	25	Helical; Potential
	Topological domain	491 – 1108	618	Cytoplasmic Potential
	Domain	532 – 812	281	Protein kinase
	Domain	884 – 1014	131	Guanylate cyclase
Amino acid modifications
	Disulfide bond	104 ↔ 132		By similarity
	Disulfide bond	452		Interchain By similarity
	Disulfide bond	460		Interchain By similarity

Sequences

	Sequence		Length	Mass (Da)
	P51842 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 2A9147AF2202E4E3	FASTA	1,108	124,411
	10 20 30 40 50 60 MFLGPWPFSR LLSWFAISSR LSGQHGLTSS KFLRYLCLLA LLPLIWWGQA LPYKIGVIGP 70 80 90 100 110 120 WTCDPFFSKA LPEVAAALAI ERISRDMSFD RSYSFEYVIL NEDCQTSKAL TSFISHQQMA 130 140 150 160 170 180 SGFVGPANPG YCEAASLLGN SWDKGIFSWA CVNHELDNKH SYPTFSRTLP SPIRVLVTVM 190 200 210 220 230 240 KYFQWAHAGV ISSDEDIWVH TANQVSSALR SHGLPVGVVL TSGQDSRSIQ KALQQIRQAD 250 260 270 280 290 300 RIRIIIMCMH SALIGGETQT HFLELAHDLK MTDGTYVFVP YDVLLYSLPY KHSPYQVLRN 310 320 330 340 350 360 NQKLREAYDA VLTITVESHE KTFYEAFTEA AAGGEIPEKL DSHQVSPLFG TIYNSIYFIA 370 380 390 400 410 420 QAMSNALKEN GQASAASLTR HSRNMQFYGF NQLIRTDSNG NGISEYVILD TNGKEWELRG 430 440 450 460 470 480 TYTVDMETEL LRFRGTPIHF PGGRPTSADA KCWFAQGKIC QGGIDPALAM MVCFALLLAL 490 500 510 520 530 540 LSINGFAYFI RRRINKIQLI KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQIISEVQS 550 560 570 580 590 600 GRSPRLSFSS GSLTPATYEN SNIAIYQGDW VWLKKFPPGD FGDIKSIKSS ASDVFEMMKD 610 620 630 640 650 660 LRHENVNPLL GFFYDSGMFA IVSEFCSRRS LEDILTQDDV KLDWMFKSSL LLDLIKGMKY 670 680 690 700 710 720 LHHREFIHGR LKSRNCVVDG RFVLKVTDYG FNNILEMLRL SEEEPSEEEL LWTAPELLRA 730 740 750 760 770 780 PGGIRLGSFA GDVYSFAIIM QEVMVRGAPF CMMDLSAKEV IDRLKMPPPV YRPVVSPEFA 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 IGLHTGPVVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY 1030 1040 1050 1060 1070 1080 RIHVSLSTVT ILRTLSEGYE VELRGRTELK GKGTEETFWL VGKKGFTKPL PVPPPVGKDG 1090 1100 QVGHGLQPAE IAAFQRRKAE RQLVRNKP

References

[1]	"Two membrane forms of guanylyl cyclase found in the eye." Yang R.-B., Foster D.C., Garbers D.L., Fuelle H.-J. Proc. Natl. Acad. Sci. U.S.A. 92:602-606(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Eye.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L36030 mRNA. Translation: AAA65511.1.
IPI	IPI00206274.
PIR	B55915.
RefSeq	NP_446283.1. NM_053831.1.
UniGene	Rn.10061.
3D structure databases
ProteinModelPortal	P51842.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000049500.
PTM databases
PhosphoSite	P51842.
Proteomic databases
PaxDb	P51842.
PRIDE	P51842.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000046804; ENSRNOP00000049500; ENSRNOG00000019086.
GeneID	116556.
KEGG	rno:116556.
Organism-specific databases
CTD	2986.
RGD	620439. Gucy2f.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00560000076744.
HOGENOM	HOG000293307.
HOVERGEN	HBG098487.
InParanoid	P51842.
KO	K12321.
OMA	NSIYFIA.
OrthoDB	EOG4XD3QC.
Gene expression databases
Genevestigator	P51842.
GermOnline	ENSRNOG00000019086. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.70.1230. 1 hit.
InterPro	IPR001054. A/G_cyclase. IPR018297. A/G_cyclase_CS. IPR001828. ANF_lig-bd_rcpt. IPR011645. Haem_no_assoc-bd. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. [Graphical view]
Pfam	PF01094. ANF_receptor. 1 hit. PF00211. Guanylate_cyc. 1 hit. PF07701. HNOBA. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
SMART	SM00044. CYCc. 1 hit. [Graphical view]
SUPFAM	SSF55073. A/G_cyclase. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	PS00452. GUANYLATE_CYCLASE_1. 1 hit. PS50125. GUANYLATE_CYCLASE_2. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	619209.

Entry information

Entry name

GUC2F_RAT

Accession

Primary (citable) accession number: P51842

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program