Reviewed, UniProtKB/Swiss-Prot P14100 (PDE1A_BOVIN)

Names and origin

Protein names

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

Gene names

Name:

PDE1A

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Nucleoside 3',5'-cyclic phosphate + H(2)O = nucleoside 5'-phosphate.
Enzyme regulation	Type I PDE are activated by the binding of calmodulin in the presence of Ca(2+).
Subunit structure	Homodimer.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Calmodulin-binding cAMP cGMP
Molecular function	Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Freq	P62168	1	EBI-907809,EBI-907774	From a different organism.
Hpca	P84076	1	EBI-907809,EBI-908193	From a different organism.
NCALD	P61602	1	EBI-907809,EBI-908133

Alternative products

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

Isoform 2 (identifier: P14100-1)

Also known as: PDE1A2;

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 1 (identifier: P14100-2)

Also known as: PDE1A1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MGSTATETEELENTTFKYLIGEQTEKMWQRLKGI → MDDHVTIRRKHLQRPIFR

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 530	529	Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
Regions
	Region	24 – 44	21	Calmodulin-binding
	Region	193 – 501	309	Catalytic By similarity
Natural variations
	Alternative sequence	1 – 34	34	MGSTA…RLKGI → MDDHVTIRRKHLQRPIFR in isoform 1.
Experimental info
	Sequence conflict	237	1	H → G AA sequence Ref.5
	Sequence conflict	321	1	N → W AA sequence Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (PDE1A2) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 24CF83E5211AE06F	FASTA	530	60,843
	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
	Isoform 1 (PDE1A1) [UniParc]. Checksum: 7CE7D8A1C366CCE5		514	59,198
	10 20 30 40 50 60 MDDHVTIRRK HLQRPIFRLR CLVKQLEKGD VNVIDLKKNI EYAASVLEAV YIDETRRLLD 70 80 90 100 110 120 TDDELSDIQS DSVPSEVRDW LASTFTRKMG MMKKKSEEKP RFRSIVHVVQ AGIFVERMYR 130 140 150 160 170 180 KSYHMVGLAY PEAVIVTLKD VDKWSFDVFA LNEASGEHSL KFMIYELFTR YDLINRFKIP 190 200 210 220 230 240 VSCLIAFAEA LEVGYSKYKN PYHNLIHAAD VTQTVHYIML HTGIMHWLTE LEILAMVFAA 250 260 270 280 290 300 AIHDYEHTGT TNNFHIQTRS DVAILYNDRS VLENHHVSAA YRLMQEEEMN VLINLSKDDW 310 320 330 340 350 360 RDLRNLVIEM VLSTDMSGHF QQIKNIRNSL QQPEGLDKAK TMSLILHAAD ISHPAKSWKL 370 380 390 400 410 420 HHRWTMALME EFFLQGDKEA ELGLPFSPLC DRKSTMVAQS QIGFIDFIVE PTFSLLTDST 430 440 450 460 470 480 EKIIIPLIEE DSKTKTPSYG ASRRSNMKGT TNDGTYSPDY SLASVDLKSF KNSLVDIIQQ 490 500 510 NKERWKELAA QGEPDPHKNS DLVNAEEKHA ETHS

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	M90358 mRNA. Translation: AAA74560.1. L34069 mRNA. Translation: AAA92555.1. BC123449 mRNA. Translation: AAI23450.1.
PIR	A45334.
RefSeq	NP_776839.1.
UniGene	Bt.512
3D structure databases
HSSP	HSSP built from PDB template 1OYN based on UniProtKB Q08499.
SMR	P14100. Positions 142-471.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14100.
Genome annotation databases
Ensembl	ENSBTAG00000012100. Bos taurus. [Contig view]
GeneID	281969.
KEGG	bta:281969.
Phylogenomic databases
HOVERGEN	P14100.
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]
ProDom	P14100. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

PDE1A_BOVIN

Accession

Primary (citable) accession number: P14100
Secondary accession number(s): Q08E30, Q28063

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	September 2, 2008
This is version 70 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)