P14100

PR
Gene name
PDE1A
Protein name
Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
Names
Cam-PDE 1A, 61 kDa Cam-PDE
Species
Bos taurus (Bovine)
KEGG Pathway
bta:281969
EC number
3.1.4.17: Phosphoric diester hydrolases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

76-149 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P14100

Entry ID Method Resolution Chain Position Source
AF-P14100-F1 Predicted AlphaFoldDB

82 variants for P14100

Variant ID(s) Position Change Description Diseaes Association Provenance
rs470038885 87 D>E No EVA
rs477061183 88 S>P No EVA
rs465739230 122 V>L No EVA
rs434384673 126 Q>* No EVA
rs454538235 127 A>T No EVA
rs468844126 129 I>T No EVA
rs437532502 132 E>A No EVA
rs521665114 137 K>R No EVA
rs445377497 149 A>G No EVA
rs135334830 150 V>G No EVA
rs136483847 151 I>V No EVA
rs454071723 152 V>E No EVA
rs433946433 152 V>I No EVA
rs466885860 153 T>K No EVA
rs133948977 154 L>I No EVA
rs435686059 181 Y>* No EVA
rs444877525 212 S>C No EVA
rs383444553 229 Q>K No EVA
rs455004628 236 L>P No EVA
rs444025827 246 E>Q No EVA
rs458259722 246 E>V No EVA
rs447034670 259 H>P No EVA
rs474452948 278 V>F No EVA
rs456695917 284 D>G No EVA
rs476822228 285 R>G No EVA
rs723749669 285 R>H No EVA
rs439053322 286 S>A No EVA
rs472758314 305 M>I No EVA
rs458967260 314 D>E No EVA
rs479198372 315 D>E No EVA
rs454688237 320 R>G No EVA
rs474821809 320 R>Q No EVA
rs463447227 336 F>L No EVA
rs439182428 337 Q>H No EVA
rs477181596 337 Q>P No EVA
rs459279556 340 K>* No EVA
rs479886517 341 N>H No EVA
rs448720262 341 N>K No EVA
rs468737089 346 L>F No EVA
rs482210915 351 G>A No EVA
rs459321428 353 D>N No EVA
rs801092581 355 A>V No EVA
rs443751931 358 M>V No EVA
rs479193805 361 I>V No EVA
rs441603272 369 H>P No EVA
rs462273113 375 K>E No EVA
rs482371800 379 R>Q No EVA
rs458284631 385 M>T No EVA
rs476967593 394 K>N No EVA
rs468540333 417 Q>L No EVA
rs468540333 417 Q>P No EVA
rs437187022 418 I>T No EVA
rs439158473 422 D>E No EVA
rs459194241 423 F>C No EVA
rs442299564 424 I>L No EVA
rs451121813 426 E>G No EVA
rs482467973 426 E>K No EVA
rs478302177 427 P>Q No EVA
rs458166291 427 P>S No EVA
rs446820460 430 S>F No EVA
rs466981067 431 L>P No EVA
rs448263372 433 T>K No EVA
rs479677493 433 T>P No EVA
rs468531780 436 T>P No EVA
rs436969620 438 K>* No EVA
rs457177246 443 L>R No EVA
rs464184465 446 E>K No EVA
rs432863367 448 S>A No EVA
rs452763433 450 T>N No EVA
rs472785453 451 K>N No EVA
rs441604875 452 T>P No EVA
rs455958165 456 G>R No EVA
rs476197719 456 G>V No EVA
rs444546555 457 A>S No EVA
rs478265122 458 S>T No EVA
rs440560870 459 R>I No EVA
rs476782539 463 M>I No EVA
rs438715962 464 K>E No EVA
rs458788192 464 K>N No EVA
rs471478069 465 G>R No EVA
rs440283091 465 G>V No EVA
rs460301744 500 R>M No EVA

No associated diseases with P14100

3 regional properties for P14100

Type Name Position InterPro Accession
conserved_site 14-3-3 protein, conserved site 45 - 55 IPR023409-1
conserved_site 14-3-3 protein, conserved site 217 - 236 IPR023409-2
domain 14-3-3 domain 7 - 248 IPR023410

Functions

Description
EC Number 3.1.4.17 Phosphoric diester hydrolases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.

6 GO annotations of molecular function

Name Definition
3',5'-cyclic-GMP phosphodiesterase activity Catalysis of the reaction: 3',5'-cyclic GMP + H2O = GMP + H+.
3',5'-cyclic-nucleotide phosphodiesterase activity Catalysis of the reaction: a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate.
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity Catalysis of the reactions: nucleoside 3',5'-cyclic GMP + H2O = GMP + H+; this activity is activated by binding to calcium-bound calmodulin.
calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity Catalysis of the reactions: 3',5'-cyclic AMP + H2O = AMP + H+ and 3',5'-cyclic GMP + H2O = GMP + H+; this activity is activated by binding to calcium-bound calmodulin.
metal ion binding Binding to a metal ion.

1 GO annotations of biological process

Name Definition
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P23439 PDE6B Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta Bos taurus (Bovine) PR
Q28156 PDE5A cGMP-specific 3',5'-cyclic phosphodiesterase Bos taurus (Bovine) SS
P54750 PDE1A Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A Homo sapiens (Human) PR
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
VDLKSFKNSL VDIIQQNKER WKELAAQGEP DPHKNSDLVN AEEKHAETHS