Reviewed, UniProtKB/Swiss-Prot Q14123 (PDE1C_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

PDE1C

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	709 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. Has a high affinity for both cAMP and cGMP.
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	Type I PDE are activated by the binding of calmodulin in the presence of Ca2+.
Subunit structure	Homodimer By similarity.
Tissue specificity	Expressed in several tissues, including brain and heart.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Calmodulin-binding Metal-binding cAMP cGMP
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	signal transduction Inferred from electronic annotation. Source: InterPro
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.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

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

Note: Additional isoforms seem to exist.

Isoform PDE1C2 (identifier: Q14123-1)

Also known as: HCam-3A;

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 PDE1C1 (identifier: Q14123-2)

Also known as: HCam-3B;

The sequence of this isoform differs from the canonical sequence as follows:
     631-634: GTKQ → DSQE
     635-709: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 709

709

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

PRO_0000198792

Regions

Region

202 – 521

320

Catalytic By similarity

Sites

Active site

228

1

Proton donor By similarity

Metal binding

232

1

Divalent metal cation 1 By similarity

Metal binding

268

1

Divalent metal cation 1 By similarity

Metal binding

269

1

Divalent metal cation 1 By similarity

Metal binding

269

1

Divalent metal cation 2 By similarity

Metal binding

376

1

Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue

3

1

Phosphoserine

Modified residue

469

1

Phosphoserine

Natural variations

Alternative sequence

631 – 634

4

GTKQ → DSQE in isoform PDE1C1.

VSP_004552

Alternative sequence

635 – 709

75

Missing in isoform PDE1C1.

VSP_004553

Secondary structure

1

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709

Helix Strand Turn

Details...

Turn

164 – 167

4

Helix

173 – 179

7

Helix

184 – 195

12

Helix

198 – 201

4

Helix

206 – 218

13

Beta strand

223 – 225

3

Helix

230 – 244

15

Helix

247 – 249

3

Turn

250 – 252

3

Helix

255 – 267

13

Turn

268 – 271

4

Helix

277 – 282

6

Helix

286 – 290

5

Turn

291 – 293

3

Helix

296 – 307

12

Helix

308 – 313

6

Helix

323 – 338

16

Helix

342 – 344

3

Helix

345 – 354

10

Helix

365 – 376

12

Helix

379 – 381

3

Helix

384 – 407

24

Turn

418 – 420

3

Helix

423 – 433

11

Helix

435 – 445

11

Turn

446 – 450

5

Helix

451 – 459

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform PDE1C2 (HCam-3A) [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 77133D4DDBE5F7C0	FASTA	709	80,760
	10 20 30 40 50 60 MESPTKEIEE FESNSLKYLQ PEQIEKIWLR LRGLRKYKKT SQRLRSLVKQ LERGEASVVD 70 80 90 100 110 120 LKKNLEYAAT VLESVYIDET RRLLDTEDEL SDIQSDAVPS EVRDWLASTF TRQMGMMLRR 130 140 150 160 170 180 SDEKPRFKSI VHAVQAGIFV ERMYRRTSNM VGLSYPPAVI EALKDVDKWS FDVFSLNEAS 190 200 210 220 230 240 GDHALKFIFY ELLTRYDLIS RFKIPISALV SFVEALEVGY SKHKNPYHNL MHAADVTQTV 250 260 270 280 290 300 HYLLYKTGVA NWLTELEIFA IIFSAAIHDY EHTGTTNNFH IQTRSDPAIL YNDRSVLENH 310 320 330 340 350 360 HLSAAYRLLQ DDEEMNILIN LSKDDWREFR TLVIEMVMAT DMSCHFQQIK AMKTALQQPE 370 380 390 400 410 420 AIEKPKALSL MLHTADISHP AKAWDLHHRW TMSLLEEFFR QGDREAELGL PFSPLCDRKS 430 440 450 460 470 480 TMVAQSQVGF IDFIVEPTFT VLTDMTEKIV SPLIDETSQT GGTGQRRSSL NSISSSDAKR 490 500 510 520 530 540 SGVKTSGSEG SAPINNSVIS VDYKSFKATW TEVVHINRER WRAKVPKEEK AKKEAEEKAR 550 560 570 580 590 600 LAAEEQQKEM EAKSQAEEGA SGKAEKKTSG ETKNQVNGTR ANKSDNPRGK NSKAEKSSGE 610 620 630 640 650 660 QQQNGDFKDG KNKTDKKDHS NIGNDSKKTD GTKQRSHGSP APSTSSTCRL TLPVIKPPLR 670 680 690 700 HFKRPAYASS SYAPSVSKKT DEHPARYKML DQRIKMKKIQ NISHNWNRK
	Isoform PDE1C1 (HCam-3B). Checksum: 73F9A72EDCEAF6F7	FASTA	634	72,208
	10 20 30 40 50 60 MESPTKEIEE FESNSLKYLQ PEQIEKIWLR LRGLRKYKKT SQRLRSLVKQ LERGEASVVD 70 80 90 100 110 120 LKKNLEYAAT VLESVYIDET RRLLDTEDEL SDIQSDAVPS EVRDWLASTF TRQMGMMLRR 130 140 150 160 170 180 SDEKPRFKSI VHAVQAGIFV ERMYRRTSNM VGLSYPPAVI EALKDVDKWS FDVFSLNEAS 190 200 210 220 230 240 GDHALKFIFY ELLTRYDLIS RFKIPISALV SFVEALEVGY SKHKNPYHNL MHAADVTQTV 250 260 270 280 290 300 HYLLYKTGVA NWLTELEIFA IIFSAAIHDY EHTGTTNNFH IQTRSDPAIL YNDRSVLENH 310 320 330 340 350 360 HLSAAYRLLQ DDEEMNILIN LSKDDWREFR TLVIEMVMAT DMSCHFQQIK AMKTALQQPE 370 380 390 400 410 420 AIEKPKALSL MLHTADISHP AKAWDLHHRW TMSLLEEFFR QGDREAELGL PFSPLCDRKS 430 440 450 460 470 480 TMVAQSQVGF IDFIVEPTFT VLTDMTEKIV SPLIDETSQT GGTGQRRSSL NSISSSDAKR 490 500 510 520 530 540 SGVKTSGSEG SAPINNSVIS VDYKSFKATW TEVVHINRER WRAKVPKEEK AKKEAEEKAR 550 560 570 580 590 600 LAAEEQQKEM EAKSQAEEGA SGKAEKKTSG ETKNQVNGTR ANKSDNPRGK NSKAEKSSGE 610 620 630 QQQNGDFKDG KNKTDKKDHS NIGNDSKKTD DSQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases." Loughney K., Martins T.J., Harris E.A.S., Sadhu K., Hicks J.B., Sonnenburg W.K., Beavo J.A., Ferguson K. J. Biol. Chem. 271:796-806(1996) [PubMed: 8557689] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE1C1 AND PDE1C2). Tissue: Heart.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE1C2).
[3]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-469, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U40371 mRNA. Translation: AAC50437.1.
U40372 mRNA. Translation: AAA96961.1.
AK056170 mRNA. Translation: BAG51638.1.

IPI

IPI00028928.
IPI00215657.

RefSeq

NP_005011.1.

UniGene

Hs.655694

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LXS	model	-	A	163-460	[»]

SMR

Q14123. Positions 151-524.

ModBase

Search...

Protein-protein interaction databases

STRING

Q14123.

PTM databases

PhosphoSite

Q14123.

Proteomic databases

PRIDE

Q14123.

Genome annotation databases

Ensembl

ENST00000321453; ENSP00000318105; ENSG00000154678; Homo sapiens. [Genome view]
ENST00000396191; ENSP00000379494; ENSG00000154678; Homo sapiens. [Genome view]

GeneID

5137.

KEGG

hsa:5137.

UCSC

uc003tcm.1. human.

Organism-specific databases

CTD

5137.

GeneCards

GC07M031759.

H-InvDB

HIX0006578.

HGNC

HGNC:8776. PDE1C.

MIM

602987. gene.

PharmGKB

PA33124.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17123.

HOVERGEN

Q14123.

Enzyme and pathway databases

BRENDA

3.1.4.17. 247.

Reactome

REACT_11061. Signalling by NGF.
REACT_15295. Opioid Signalling.

Gene expression databases

ArrayExpress

Q14123.

Bgee

Q14123.

CleanEx

HS_PDE1C.

Genevestigator

Q14123.

GermOnline

ENSG00000154678. Homo sapiens.

Family and domain databases

InterPro

IPR003607. Metal-dep_PHydrolase_HD_dom.
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

19808.

SOURCE

Search...

Entry information

Entry name

PDE1C_HUMAN

Accession

Primary (citable) accession number: Q14123
Secondary accession number(s): B3KPC6, Q14124

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	February 9, 2010
This is version 85 of the entry and version 1 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.