P23440 (PDE6B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
Short name=GMP-PDE beta
EC=3.1.4.35

Gene names

Name:	Pde6b
Synonyms:	Mpb, Pdeb, rd

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	856 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	This protein participates in processes of transmission and amplification of the visual signal. Necessary for the formation of a functional phosphodiesterase holoenzyme.
Catalytic activity	Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.
Cofactor	Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions By similarity.
Subunit structure	Oligomer composed of two catalytic chains (alpha and beta), an inhibitory chain (gamma) and the delta chain.
Subcellular location	Membrane; Lipid-anchor.
Involvement in disease	Note=Defects in Pde6b are the cause of retinal degeneration.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. Contains 2 GAF domains.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Metal-binding cGMP
Molecular function	Hydrolase
PTM	Lipoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	detection of light stimulus Inferred from mutant phenotype. Source: MGI retina development in camera-type eye Inferred from mutant phenotype. Source: MGI signal transduction Inferred from electronic annotation. Source: InterPro visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3',5'-cyclic-GMP phosphodiesterase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P23440-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P23440-2)

Also known as: Beta';

The sequence of this isoform differs from the canonical sequence as follows:
     801-856: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 853	853	Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta		PRO_0000023350
	Propeptide	854 – 856	3	Removed in mature form By similarity		PRO_0000023351
Regions
	Domain	71 – 220	150	GAF 1
	Domain	252 – 429	178	GAF 2
Sites
	Active site	557	1	Proton donor By similarity
	Metal binding	561	1	Divalent metal cation 1 By similarity
	Metal binding	597	1	Divalent metal cation 1 By similarity
	Metal binding	598	1	Divalent metal cation 1 By similarity
	Metal binding	598	1	Divalent metal cation 2 By similarity
	Metal binding	718	1	Divalent metal cation 1 By similarity
Amino acid modifications
	Lipidation	853	1	S-geranylgeranyl cysteine By similarity
Natural variations
	Alternative sequence	801 – 856	56	Missing in isoform 2.		VSP_004592
Experimental info
	Sequence conflict	5	1	E → G in CAA39439. Ref.1
	Sequence conflict	19	1	A → S in CAA39439. Ref.1
	Sequence conflict	49 – 50	2	EL → DV in CAA39439. Ref.1
	Sequence conflict	158	1	P → T in CAA39439. Ref.1
	Sequence conflict	176	1	L → C in CAA39439. Ref.1
	Sequence conflict	232	1	E → R in CAA39439. Ref.1
	Sequence conflict	236	1	G → S in CAA39439. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 209F3A936DD16D46	FASTA	856	98,535
	10 20 30 40 50 60 MSLSEEQVRS FLDGNPTFAH QYFGKKLSPE NVAGACEDGW LADCGSLREL CQVEESAALF 70 80 90 100 110 120 ELVQDMQESV NMERVVFKIL RRLCTILHAD RCSLFMYRQR NGIAELATRL FSVQPDSLLE 130 140 150 160 170 180 DCLVPPDSEI VFPLDIGIVG HVAQTKKMIN VQDVAECPHF SSFADELTDY VTKNILSTPI 190 200 210 220 230 240 MNGKDVVAVI MAVNKLDGPC FTSEDEDVFT KYLNFATLNL KIYHLSYLHN CETRRGQVLL 250 260 270 280 290 300 WSANKVFEEL TDIERQFHKA FYTVRAYLNC ERYSVGLLDM TKEKEFFDVW PVLMGEAQPY 310 320 330 340 350 360 SGPRTPDGRE IVFYKVIDYI LHGKEDIKVI PTPPADHWAL ASGLPTYVAE SGFICNIMNA 370 380 390 400 410 420 SADEMFNFQE GPLDDSGWVI KNVLSMPIVN KKEEIVGVAT FYNRKDGKPF DDQDEVLMES 430 440 450 460 470 480 LTQFLGWSVL NTDTYDKMNK LENRKDIAQD MVLYHVRCDK DEIQEILPTR DRLGKEPADC 490 500 510 520 530 540 EEDELGKILK EELPGPTKFD IYEFHFSDLE CTELELVKCG IQMYYELGVV RKFQIPQEVL 550 560 570 580 590 600 VRFLFSVSKA YRRITYHNWR HGFNVAQTMF TLLMTGKLKS YYTDLEAFAM VTAGLCHDID 610 620 630 640 650 660 HRGTNNLYQM KSQNPLAKLH GSSILERHHL EFGKFLLAEE SLNIYQNLNR RQHEHVIHLM 670 680 690 700 710 720 DIAIIATDLA LYFKKRTMFQ KIVDESKNYE DKKSWVEYLS LETTRKEIVM AMMMTACDLS 730 740 750 760 770 780 AITKPWEVQS KVALLVAAEF WEQGDLERTV LDQQPIPMMD RNKAAELPKL QVGFIDFVCT 790 800 810 820 830 840 FVYKEFSRFH EEILPMFDRL QNNRKEWKAL ADEYEAKVKA LEEEKKKEED RVAAKKVGTE 850 VCNGGPAPKS STCCIL
	Isoform 2 (Beta') [UniParc]. Checksum: 23F1AC68F7CC7AF7	FASTA	800	92,331
	10 20 30 40 50 60 MSLSEEQVRS FLDGNPTFAH QYFGKKLSPE NVAGACEDGW LADCGSLREL CQVEESAALF 70 80 90 100 110 120 ELVQDMQESV NMERVVFKIL RRLCTILHAD RCSLFMYRQR NGIAELATRL FSVQPDSLLE 130 140 150 160 170 180 DCLVPPDSEI VFPLDIGIVG HVAQTKKMIN VQDVAECPHF SSFADELTDY VTKNILSTPI 190 200 210 220 230 240 MNGKDVVAVI MAVNKLDGPC FTSEDEDVFT KYLNFATLNL KIYHLSYLHN CETRRGQVLL 250 260 270 280 290 300 WSANKVFEEL TDIERQFHKA FYTVRAYLNC ERYSVGLLDM TKEKEFFDVW PVLMGEAQPY 310 320 330 340 350 360 SGPRTPDGRE IVFYKVIDYI LHGKEDIKVI PTPPADHWAL ASGLPTYVAE SGFICNIMNA 370 380 390 400 410 420 SADEMFNFQE GPLDDSGWVI KNVLSMPIVN KKEEIVGVAT FYNRKDGKPF DDQDEVLMES 430 440 450 460 470 480 LTQFLGWSVL NTDTYDKMNK LENRKDIAQD MVLYHVRCDK DEIQEILPTR DRLGKEPADC 490 500 510 520 530 540 EEDELGKILK EELPGPTKFD IYEFHFSDLE CTELELVKCG IQMYYELGVV RKFQIPQEVL 550 560 570 580 590 600 VRFLFSVSKA YRRITYHNWR HGFNVAQTMF TLLMTGKLKS YYTDLEAFAM VTAGLCHDID 610 620 630 640 650 660 HRGTNNLYQM KSQNPLAKLH GSSILERHHL EFGKFLLAEE SLNIYQNLNR RQHEHVIHLM 670 680 690 700 710 720 DIAIIATDLA LYFKKRTMFQ KIVDESKNYE DKKSWVEYLS LETTRKEIVM AMMMTACDLS 730 740 750 760 770 780 AITKPWEVQS KVALLVAAEF WEQGDLERTV LDQQPIPMMD RNKAAELPKL QVGFIDFVCT 790 800 FVYKEFSRFH EEILPMFDRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Retinal degeneration in the rd mouse is caused by a defect in the beta subunit of rod cGMP-phosphodiesterase." Bowes C., Li T., Danciger M., Baxter L.C., Applebury M.L., Farber D.B. Nature 347:677-680(1990) [PubMed: 1977087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Retina.
[2]	"Complete cDNA sequences of mouse rod photoreceptor cGMP phosphodiesterase alpha- and beta-subunits, and identification of beta'-, a putative beta-subunit isozyme produced by alternative splicing of the beta-subunit gene." Baehr W., Champagne M.S., Lee A.K., Pittler S.J. FEBS Lett. 278:107-114(1991) [PubMed: 1847109] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2). Tissue: Retina.
[3]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Retina.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X55968 mRNA. Translation: CAA39439.1. X60133 mRNA. Translation: CAA42719.1. AK044364 mRNA. Translation: BAC31885.1. CH466529 Genomic DNA. Translation: EDL20122.1.
IPI	IPI00132326. IPI00227887.
PIR	S30762.
RefSeq	NP_032832.2. NM_008806.2.
UniGene	Mm.1372.
3D structure databases
ProteinModelPortal	P23440.
SMR	P23440. Positions 52-813.
ModBase	Search...
Protein-protein interaction databases
STRING	P23440.
PTM databases
PhosphoSite	P23440.
Proteomic databases
PRIDE	P23440.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031456; ENSMUSP00000031456; ENSMUSG00000029491.
GeneID	18587.
KEGG	mmu:18587.
Organism-specific databases
CTD	5158.
MGI	MGI:97525. Pde6b.
Phylogenomic databases
HOGENOM	HBG445272.
HOVERGEN	HBG053539.
InParanoid	P23440.
OrthoDB	EOG44TP77.
Gene expression databases
ArrayExpress	P23440.
Bgee	P23440.
Genevestigator	P23440.
GermOnline	ENSMUSG00000029491. Mus musculus.
Family and domain databases
InterPro	IPR003018. GAF. IPR003607. Metal-dep_PHydrolase_HD_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [Graphical view]
Gene3D	G3DSA:1.10.1300.10. PDEase_catalytic_dom. 1 hit.
KO	K13756.
Pfam	PF01590. GAF. 2 hits. PF00233. PDEase_I. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00065. GAF. 2 hits. SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

PDE6B_MOUSE

Accession

Primary (citable) accession number: P23440
Secondary accession number(s): Q80UF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	July 27, 2011
Last modified:	November 16, 2011
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program