[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; PubMed=7678006 [NCBI, ExPASy, EBI, Israel, Japan] Sonnenburg W.K., Seger D., Beavo J.A.; "Molecular cloning of a cDNA encoding the '61-kDa' calmodulin-stimulated cyclic nucleotide phosphodiesterase. Tissue-specific expression of structurally related isoforms."; J. Biol. Chem. 268:645-652(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Lung; DOI=10.1074/jbc.270.52.30989; PubMed=8537356 [NCBI, ExPASy, EBI, Israel, Japan] Sonnenburg W.K., Seger D., Kwak K.S., Huang J., Charbonneau H., Beavo J.A.; "Identification of inhibitory and calmodulin-binding domains of the PDE1A1 and PDE1A2 calmodulin-stimulated cyclic nucleotide phosphodiesterases."; J. Biol. Chem. 270:30989-31000(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). STRAIN=Hereford; TISSUE=Hippocampus; NIH - Mammalian Gene Collection (MGC) project; Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[4]	PROTEIN SEQUENCE OF 2-530 (ISOFORM 2). TISSUE=Brain; DOI=10.1021/bi00246a009; PubMed=1651111 [NCBI, ExPASy, EBI, Israel, Japan] Charbonneau H., Kumar S., Novack J.P., Blumenthal D.K., Griffin P.R., Shabanowitz J., Hunt D.F., Beavo J.A., Walsh K.A.; "Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain."; Biochemistry 30:7931-7940(1991).
[5]	PROTEIN SEQUENCE OF 194-427. TISSUE=Brain; PubMed=3025833 [NCBI, ExPASy, EBI, Israel, Japan] Charbonneau H., Beier N., Walsh K.A., Beavo J.A.; "Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species."; Proc. Natl. Acad. Sci. U.S.A. 83:9308-9312(1986).

Comments

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 Ca(2+).
SUBUNIT: Homodimer.
INTERACTION:
P62168:Freq (xeno); NbExp=1; IntAct=EBI-907809, EBI-907774;
P84076:Hpca (xeno); NbExp=1; IntAct=EBI-907809, EBI-908193;
P61602:NCALD; NbExp=1; IntAct=EBI-907809, EBI-908133;

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	2
Synonyms	PDE1A2
Isoform ID	P14100-1
This is the isoform sequence displayed in this entry.

Name	1
Synonyms	PDE1A1
Isoform ID	P14100-2
Features which should be applied to build the isoform sequence: VSP_004546.

SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M90358; AAA74560.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L34069; AAA92555.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC123449; AAI23450.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A45334; A45334.

NP_776839.1; -.

3D structure databases

HSSP

Q08499; 1OYN. [HSSP ENTRY / PDB]

SMR

P14100; 142-471.

ModBase

P14100.

Protein-protein interaction databases

IntAct

P14100; -.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR003607; Met-dep_phosphohydro_HD.
IPR002073; PDEase.
IPR013706; PDEase_N.
Graphical view of domain structure.

Pfam

PF00233; PDEase_I; 1.
PF08499; PDEase_I_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00387; PDIESTERASE1.

SMART

SM00471; HDc; 1.
SMART graphical view of domain structure.

PROSITE

PS00126; PDEASE_I; 1.

BLOCKS

P14100.

Genome annotation databases

Ensembl

ENSBTAG00000012100; Bos taurus. [Contig view]

GeneID

281969; -.

Phylogenomic databases

HOVERGEN

P14100; -.

Other

ProtoNet

P14100.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Calmodulin-binding; cAMP; cGMP; Direct protein sequencing; Hydrolase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 530`	`529`	`Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A.`	`PRO_0000198784`
`REGION`	`24 44`	`21`	`Calmodulin-binding.`
`REGION`	`193 501`	`309`	`Catalytic (By similarity).`
`VAR_SEQ`	`1 34`		`MGSTATETEELENTTFKYLIGEQTEKMWQRLKGI -> MDDHVTIRRKHLQRPIFR (in isoform 1).`	`VSP_004546`
`CONFLICT`	`237 237`		`H -> G (in Ref. 5; AA sequence).`
`CONFLICT`	`321 321`		`N -> W (in Ref. 5; AA sequence).`

Sequence information

Length: 530 AA [This is the length of the unprocessed precursor]

Molecular weight: 60843 Da [This is the MW of the unprocessed precursor]

CRC64: 24CF83E5211AE06F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGSTATETEE LENTTFKYLI GEQTEKMWQR LKGILRCLVK QLEKGDVNVI DLKKNIEYAA 

        70         80         90        100        110        120 
SVLEAVYIDE TRRLLDTDDE LSDIQSDSVP SEVRDWLAST FTRKMGMMKK KSEEKPRFRS 

       130        140        150        160        170        180 
IVHVVQAGIF VERMYRKSYH MVGLAYPEAV IVTLKDVDKW SFDVFALNEA SGEHSLKFMI 

       190        200        210        220        230        240 
YELFTRYDLI NRFKIPVSCL IAFAEALEVG YSKYKNPYHN LIHAADVTQT VHYIMLHTGI 

       250        260        270        280        290        300 
MHWLTELEIL AMVFAAAIHD YEHTGTTNNF HIQTRSDVAI LYNDRSVLEN HHVSAAYRLM 

       310        320        330        340        350        360 
QEEEMNVLIN LSKDDWRDLR NLVIEMVLST DMSGHFQQIK NIRNSLQQPE GLDKAKTMSL 

       370        380        390        400        410        420 
ILHAADISHP AKSWKLHHRW TMALMEEFFL QGDKEAELGL PFSPLCDRKS TMVAQSQIGF 

       430        440        450        460        470        480 
IDFIVEPTFS LLTDSTEKII IPLIEEDSKT KTPSYGASRR SNMKGTTNDG TYSPDYSLAS 

       490        500        510        520        530 
VDLKSFKNSL VDIIQQNKER WKELAAQGEP DPHKNSDLVN AEEKHAETHS

P14100 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools