Reviewed, UniProtKB/Swiss-Prot Q01064 (PDE1B_HUMAN)

Names and origin

Protein names

Recommended name:
    Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
      Short name=Cam-PDE 1B
    EC=3.1.4.17
Alternative name(s):
    63 kDa Cam-PDE

Gene names

Name:	PDE1B
Synonyms:	PDE1B1, PDES1B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	536 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has a preference for cGMP as a substrate.
Catalytic activity	Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.
Enzyme regulation	Type I PDE are activated by the binding of calmodulin in the presence of Ca2+.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Calmodulin-binding cAMP cGMP
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	apoptosis Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent cyclic-nucleotide phosphodiesterase activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 536

536

Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B

PRO_0000198789

Regions

Region

27 – 47

21

Calmodulin-binding Potential

Region

197 – 496

300

Catalytic By similarity

Amino acid modifications

Modified residue

466

1

Phosphoserine By similarity

Experimental info

Sequence conflict

225 – 226

2

QI → SM in AAA58405. Ref.2

Sequence conflict

337

1

S → A in AAA58405. Ref.2

Secondary structure

1

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536

Helix Strand Turn

Details...

Helix

152 – 158

7

Turn

159 – 162

4

Helix

168 – 174

7

Helix

179 – 190

12

Helix

193 – 196

4

Helix

201 – 215

15

Turn

216 – 218

3

Beta strand

221 – 224

4

Helix

225 – 242

18

Helix

244 – 247

4

Helix

250 – 262

13

Turn

263 – 266

4

Helix

272 – 278

7

Helix

281 – 286

6

Helix

291 – 303

13

Helix

307 – 309

3

Turn

311 – 314

4

Helix

317 – 332

16

Helix

336 – 338

3

Helix

339 – 351

13

Helix

358 – 370

13

Helix

373 – 375

3

Helix

378 – 402

25

Helix

414 – 427

14

Helix

429 – 444

16

Helix

476 – 501

26

Sequences

	Sequence		Length	Mass (Da)
	Q01064-1 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: D15211AC32C756A4	FASTA	536	61,380
	10 20 30 40 50 60 MELSPRSPPE MLEESDCPSP LELKSAPSKK MWIKLRSLLR YMVKQLENGE INIEELKKNL 70 80 90 100 110 120 EYTASLLEAV YIDETRQILD TEDELQELRS DAVPSEVRDW LASTFTQQAR AKGRRAEEKP 130 140 150 160 170 180 KFRSIVHAVQ AGIFVERMFR RTYTSVGPTY STAVLNCLKN LDLWCFDVFS LNQAADDHAL 190 200 210 220 230 240 RTIVFELLTR HNLISRFKIP TVFLMSFLDA LETGYGKYKN PYHNQIHAAD VTQTVHCFLL 250 260 270 280 290 300 RTGMVHCLSE IELLAIIFAA AIHDYEHTGT TNSFHIQTKS ECAIVYNDRS VLENHHISSV 310 320 330 340 350 360 FRLMQDDEMN IFINLTKDEF VELRALVIEM VLATDMSCHF QQVKTMKTAL QQLERIDKPK 370 380 390 400 410 420 ALSLLLHAAD ISHPTKQWLV HSRWTKALME EFFRQGDKEA ELGLPFSPLC DRTSTLVAQS 430 440 450 460 470 480 QIGFIDFIVE PTFSVLTDVA EKSVQPLADE DSKSKNQPSF QWRQPSLDVE VGDPNPDVVS 490 500 510 520 530 FRSTWVKRIQ ENKQKWKERA ASGITNQMSI DELSPCEEEA PPSPAEDEHN QNGNLD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Inhibition of calmodulin-dependent phosphodiesterase induces apoptosis in human leukemic cells." Jiang X., Li J., Paskind M., Epstein P.M. Proc. Natl. Acad. Sci. U.S.A. 93:11236-11241(1996) [PubMed: 8855339] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Identification and characterisation of a human calmodulin-stimulated phosphodiesterase PDE1B1." Yu J., Frazier A.L.B., Wolda S.L., Florio V.A., Martins T.J., Snyder P.B., Harris E.A.S., McCaw K.N., Farrell C.A., Steiner B., Bentley J.K., Beavo J.A., Ferguson K., Gelinas R. Cell. Signal. 9:519-529(1997) [PubMed: 9419816] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase." Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M. J. Biol. Chem. 267:18683-18688(1992) [PubMed: 1326532] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 222-337.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U56976 mRNA. Translation: AAC50769.1.
U86078 mRNA. Translation: AAC51872.1.
BC032226 mRNA. Translation: AAH32226.1.
M94539 mRNA. Translation: AAA58405.1.

IPI

IPI00005592.

PIR

JC6129.

RefSeq

NP_000915.1.

UniGene

Hs.530871

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LXR	model	-	A	158-461	[»]
1TAZ	X-ray	1.77	A	146-506	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q01064.

PTM databases

PhosphoSite

Q01064.

Proteomic databases

PRIDE

Q01064.

Genome annotation databases

Ensembl

ENST00000243052; ENSP00000243052; ENSG00000123360; Homo sapiens. [Genome view]
ENST00000394277; ENSP00000377818; ENSG00000123360; Homo sapiens. [Genome view]

GeneID

5153.

KEGG

hsa:5153.

UCSC

uc001sgd.1. human.

Organism-specific databases

CTD

5153.

GeneCards

GC12P053229.

H-InvDB

HIX0010700.

HGNC

HGNC:8775. PDE1B.

HPA

HPA018492.

MIM

171891. gene.

PharmGKB

PA33123.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q01064.

HOVERGEN

Q01064.

OMA

DVDVGDP.

Enzyme and pathway databases

BRENDA

3.1.4.17. 247.

Reactome

REACT_11061. Signalling by NGF.
REACT_14797. Signaling by GPCR.
REACT_15295. Opioid Signalling.

Gene expression databases

ArrayExpress

Q01064.

Bgee

Q01064.

CleanEx

HS_PDE1B.

Genevestigator

Q01064.

GermOnline

ENSG00000123360. Homo sapiens.

Family and domain databases

InterPro

IPR003607. Met-dep_phosphohydro_HD.
IPR002073. PDEase.
IPR013706. PDEase_N.
[Graphical view]

Pfam

PF00233. PDEase_I. 1 hit.
PF08499. PDEase_I_N. 1 hit.
[Graphical view]

PRINTS

PR00387. PDIESTERASE1.

SMART

SM00471. HDc. 1 hit.
[Graphical view]

PROSITE

PS00126. PDEASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

19926.

SOURCE

Search...

Entry information

Entry name

PDE1B_HUMAN

Accession

Primary (citable) accession number: Q01064
Secondary accession number(s): Q92825

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	July 15, 1998
Last modified:	November 3, 2009
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.