Reviewed, UniProtKB/Swiss-Prot Q63085 (PDE3B_RAT)

Names and origin

Protein names

Recommended name:
    cGMP-inhibited 3',5'-cyclic phosphodiesterase B
    EC=3.1.4.17
Alternative name(s):
    Cyclic GMP-inhibited phosphodiesterase B
      Short name=CGI-PDE B
    CGIPDE1

Gene names

Name:

Pde3b

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1108 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism By similarity.
Catalytic activity	Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 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.
Enzyme regulation	Inhibited by cGMP.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Tissue specificity	Abundant in adipose tissues.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. PDE3 subfamily.

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane
Ligand	Metal-binding cAMP cGMP
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cAMP catabolic process Inferred from direct assay. Source: RGD cellular response to insulin stimulus Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of insulin secretion Inferred from mutant phenotype. Source: RGD signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3',5'-cyclic-AMP phosphodiesterase activity Inferred from direct assay. Source: RGD cAMP binding Inferred from direct assay. Source: RGD cGMP-inhibited cyclic-nucleotide phosphodiesterase activity Inferred from direct assay. Source: RGD drug binding Inferred from direct assay. Source: RGD phosphoprotein binding Inferred from direct assay. Source: RGD protein kinase B binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1108	1108	cGMP-inhibited 3',5'-cyclic phosphodiesterase B		PRO_0000198804
Regions
	Transmembrane	73 – 93	21	Potential
	Transmembrane	114 – 134	21	Potential
	Transmembrane	144 – 164	21	Potential
	Transmembrane	175 – 195	21	Potential
	Transmembrane	204 – 224	21	Potential
	Transmembrane	231 – 251	21	Potential
	Region	695 – 1063	369	Catalytic By similarity
	Compositional bias	16 – 22	7	Poly-Pro
	Compositional bias	99 – 102	4	Poly-Ala
	Compositional bias	175 – 179	5	Poly-Ala
	Compositional bias	1007 – 1021	15	Poly-Asp
	Compositional bias	1068 – 1071	4	Poly-Glu
	Compositional bias	1101 – 1104	4	Poly-Glu
Sites
	Active site	719	1	Proton donor By similarity
	Metal binding	723	1	Divalent metal cation 1 By similarity
	Metal binding	803	1	Divalent metal cation 1 By similarity
	Metal binding	804	1	Divalent metal cation 1 By similarity
	Metal binding	804	1	Divalent metal cation 2 By similarity
	Metal binding	919	1	Divalent metal cation 1 By similarity
Amino acid modifications
	Modified residue	427	1	Phosphoserine By similarity
	Modified residue	610	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63085-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C9B5078C7D3ADD6D	FASTA	1,108	123,107
	10 20 30 40 50 60 MRKDERERDT PAMRSPPPPP PPATATAASP PESLRNGYVK SCVSPLRQDP PRSFFFHLCR 70 80 90 100 110 120 FCNVEPPAAS LRAGARLSLA ALAAFVLAAL LGAGPERWAA AATGLRTLLS ACSLSLSPLF 130 140 150 160 170 180 SIACAFFFLT CFLTRAQRGP DRGAGSWWLL ALPACCYLGD FAAWQWWSWL RGEPAAAAAG 190 200 210 220 230 240 RLCLVLSCVG LLTLAPRVRL RHGVLVLLFA GLVWWVSFSG LGALPPALRP LLSCLVGGAG 250 260 270 280 290 300 CLLALGLDHF FHVRGASPPP RSASTADEKV PVIRPRRRSS CVSLGESAAG YYGSGKMFRR 310 320 330 340 350 360 PSLPCISREQ MILWDWDLKQ WCKPHYQNSG GGNGVDLSVL NEARNMVSDL LIDPSLPPQV 370 380 390 400 410 420 ISSLRSISSL MGAFSGSCRP KINSFTPFPG FYPCSEVEDP VEKGDRKLHK GLSSKPSFPT 430 440 450 460 470 480 AQLRRSSGAS GLLTSEHHSR WDRSGGKRPY QELSVSSHGC HLNGPFSSNL MTIPKQRSSS 490 500 510 520 530 540 VSLTHHAGLR RAGALPSPSL LNSSSHVPVS AGCLTNRSPV GFLDTSDFLT KPSVTLHRSL 550 560 570 580 590 600 GSVSSAADFH QYLRNSDSSL CSSCGHQILK YVSTCEPDGT DHHNEKSGEE DSTVFSKERL 610 620 630 640 650 660 NIVETQEEET VKEDCRELFL EGDDHLMEEA QQPNIDQEVL LDPMLVEDYD SLIEKMSNWN 670 680 690 700 710 720 FQIFELVEKM GEKSGRILSQ VMYTLFQDTG LLETFKIPTQ EFMNYFRALE NGYRDIPYHN 730 740 750 760 770 780 RVHATDVLHA VWYLTTRPIP GLQQLHNNHE TETKADSDAR LSSGQIAYLS SKSCCIPDKS 790 800 810 820 830 840 YGCLSSNIPA LELMALYVAA AMHDYDHPGR TNAFLVATNA PQAVLYNDRS VLENHHAASA 850 860 870 880 890 900 WNLYLSRPEY NFLLNLDHME FKRFRFLVIE AILATDLKKH FDFLAEFNAK ANDVNSNGIE 910 920 930 940 950 960 WSSENDRLLV CQVCIKLADI NGPAKDRDLH LRWTEGIVNE FYEQGDEEAT LGLPISPFMD 970 980 990 1000 1010 1020 RSSPQLAKLQ ESFITHIVGP LCNSYDAAGL LPGQWIEAEE GDDTESDDDD DDDDDDDDDD 1030 1040 1050 1060 1070 1080 DEELDSDDEE TEDNLNPKPQ RRKGRRRIFC QLMHHLTENH KIWKEIIEEE EKCKAEGNKL 1090 1100 QVDNASLPQA DEIQVIEEAD EEEEQMFE

References

[1]	"Molecular cloning of the rat adipocyte hormone-sensitive cyclic GMP-inhibited cyclic nucleotide phosphodiesterase." Taira M., Hockman S.C., Calvo J.C., Taira M., Belfrage P., Manganiello V.C. J. Biol. Chem. 268:18573-18579(1993) [PubMed: 8395509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Adipose tissue.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z22867 mRNA. Translation: CAA80489.1.
IPI	IPI00951591.
PIR	A48508.
RefSeq	NP_058925.1.
UniGene	Rn.10322
3D structure databases
SMR	Q63085. Positions 638-1064.
ModBase	Search...
Protein-protein interaction databases
STRING	Q63085.
PTM databases
PhosphoSite	Q63085.
Proteomic databases
PRIDE	Q63085.
Genome annotation databases
Ensembl	ENSRNOT00000015498; ENSRNOP00000015498; ENSRNOG00000011417; Rattus norvegicus. [Genome view]
GeneID	29516.
KEGG	rno:29516.
Organism-specific databases
CTD	29516.
RGD	61943. Pde3b.
Phylogenomic databases
eggNOG	roNOG10811.
HOVERGEN	Q63085.
InParanoid	Q63085.
Enzyme and pathway databases
BRENDA	3.1.4.17. 248.
Gene expression databases
ArrayExpress	Q63085.
Genevestigator	Q63085.
Family and domain databases
InterPro	IPR003607. Metal-dep_PHydrolase_HD_dom. IPR002073. PDEase. [Graphical view]
Pfam	PF00233. PDEase_I. 1 hit. [Graphical view]
SMART	SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	609453.

Entry information

Entry name

PDE3B_RAT

Accession

Primary (citable) accession number: Q63085

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)