Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9C5Y0

Entry ID Method Resolution Chain Position Source
AF-Q9C5Y0-F1 Predicted AlphaFoldDB

36 variants for Q9C5Y0

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH06830881 59 D>G No 1000Genomes
ENSVATH00554111 60 K>R No 1000Genomes
tmp_4_16959682_T_C 65 D>G No 1000Genomes
ENSVATH00554110 66 K>R No 1000Genomes
tmp_4_16959667_C_T 70 S>N No 1000Genomes
ENSVATH12417107 138 K>Q No 1000Genomes
ENSVATH06830879 221 D>A No 1000Genomes
tmp_4_16959208_G_A 223 T>M No 1000Genomes
ENSVATH02962184 226 A>E No 1000Genomes
ENSVATH06830878 236 E>Q No 1000Genomes
ENSVATH02962181 266 I>V No 1000Genomes
ENSVATH06830877 273 K>E No 1000Genomes
ENSVATH02962180 274 V>F No 1000Genomes
ENSVATH06830875 277 D>A No 1000Genomes
ENSVATH06830876 277 D>H No 1000Genomes
ENSVATH06830876 277 D>Y No 1000Genomes
ENSVATH06830874 278 K>E No 1000Genomes
ENSVATH06830873 278 K>N No 1000Genomes
tmp_4_16958641_A_G 359 S>P No 1000Genomes
tmp_4_16958343_C_T 366 V>I No 1000Genomes
ENSVATH00554105 504 K>T No 1000Genomes
ENSVATH06830856 508 S>T No 1000Genomes
ENSVATH06830854 513 D>E No 1000Genomes
tmp_4_16957788_T_C 521 K>E No 1000Genomes
ENSVATH00554103 542 K>R No 1000Genomes
tmp_4_16957604_C_A 552 E>D No 1000Genomes
ENSVATH12417010 605 A>G No 1000Genomes
tmp_4_16957041_T_G 624 K>Q No 1000Genomes
tmp_4_16957019_A_C 631 V>G No 1000Genomes
ENSVATH12417007 678 L>V No 1000Genomes
ENSVATH06830844 691 Q>E No 1000Genomes
ENSVATH00554099 698 A>G No 1000Genomes
tmp_4_16956436_T_G 741 M>L No 1000Genomes
tmp_4_16956028_T_C 785 K>E No 1000Genomes
ENSVATH12416988 785 K>T No 1000Genomes
ENSVATH00554096 819 S>L No 1000Genomes

No associated diseases with Q9C5Y0

4 regional properties for Q9C5Y0

Type Name Position InterPro Accession
domain C2 domain 1 - 156 IPR000008
domain Phospholipase D/Transphosphatidylase 368 - 403 IPR001736-1
domain Phospholipase D/Transphosphatidylase 713 - 740 IPR001736-2
domain Phospholipase D, C-terminal 788 - 857 IPR024632

Functions

Description
EC Number 3.1.4.4 Phosphoric diester hydrolases
Subcellular Localization
  • Cell membrane ; Peripheral membrane protein
  • Colocalization with cortical microtubules also occurs
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
plant cell papilla A cell projection that is a short, rounded projection from a plant epidermal cell.
plant-type vacuole A closed structure that is completely surrounded by a unit membrane, contains liquid, and retains the same shape regardless of cell cycle phase. An example of this structure is found in Arabidopsis thaliana.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
plasmodesma A fine cytoplasmic channel, found in all higher plants, that connects the cytoplasm of one cell to that of an adjacent cell.

3 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
N-acylphosphatidylethanolamine-specific phospholipase D activity Catalysis of the release of N-acylethanolamine from N-acyl-phosphatidylethanolamine (NAPE) to generate N-acylethanolamine (NAE).
phospholipase D activity Catalysis of the reaction: a phosphatidylcholine + H2O = choline + a phosphatidate.

7 GO annotations of biological process

Name Definition
phosphatidic acid metabolic process The chemical reactions and pathways involving phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids.
phosphatidylcholine metabolic process The chemical reactions and pathways involving phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. They are important constituents of cell membranes.
phospholipid catabolic process The chemical reactions and pathways resulting in the breakdown of phospholipids, any lipid containing phosphoric acid as a mono- or diester.
positive regulation of abscisic acid-activated signaling pathway Any process that activates or increases the frequency, rate or extent of abscisic acid (ABA) signaling.
programmed cell death A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
regulation of stomatal closure Any process that modulates the rate, frequency, or extent of stomatal closure. Stomatal closure is the process of closing of stomata, pores in the epidermis of leaves and stems bordered by two guard cells and serving in gas exchange.
response to cold Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.

10 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q0V8L6 PLD2 Phospholipase D2 Bos taurus (Bovine) PR
O14939 PLD2 Phospholipase D2 Homo sapiens (Human) PR
Q13393 PLD1 Phospholipase D1 Homo sapiens (Human) PR
P97813 Pld2 Phospholipase D2 Mus musculus (Mouse) PR
Q9Z280 Pld1 Phospholipase D1 Mus musculus (Mouse) PR
P70496 Pld1 Phospholipase D1 Rattus norvegicus (Rat) PR
P70498 Pld2 Phospholipase D2 Rattus norvegicus (Rat) PR
P58766 PLDALPHA3 Phospholipase D alpha 3 Arabidopsis thaliana (Mouse-ear cress) PR
Q9LRZ5 PLDZETA1 Phospholipase D zeta 1 Arabidopsis thaliana (Mouse-ear cress) PR
Q9M9W8 PLPZETA2 Phospholipase D zeta 2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAEKVSEDVM LLHGDLDLKI VKARRLPNMD MFSEHLRRLF TACNACARPT DTDDVDPRDK
70 80 90 100 110 120
GEFGDKNIRS HRKVITSDPY VTVVVPQATL ARTRVLKNSQ EPLWDEKFNI SIAHPFAYLE
130 140 150 160 170 180
FQVKDDDVFG AQIIGTAKIP VRDIASGERI SGWFPVLGAS GKPPKAETAI FIDMKFTPFD
190 200 210 220 230 240
QIHSYRCGIA GDPERRGVRR TYFPVRKGSQ VRLYQDAHVM DGTLPAIGLD NGKVYEHGKC
250 260 270 280 290 300
WEDICYAISE AHHMIYIVGW SIFHKIKLVR ETKVPRDKDM TLGELLKYKS QEGVRVLLLV
310 320 330 340 350 360
WDDKTSHDKF GIKTPGVMGT HDEETRKFFK HSSVICVLSP RYASSKLGLF KQQASPSSSI
370 380 390 400 410 420
YIMTVVGTLF THHQKCVLVD TQAVGNNRKV TAFIGGLDLC DGRYDTPEHR ILHDLDTVFK
430 440 450 460 470 480
DDFHNPTFPA GTKAPRQPWH DLHCRIDGPA AYDVLINFEQ RWRKATRWKE FSLRLKGKTH
490 500 510 520 530 540
WQDDALIRIG RISWILSPVF KFLKDGTSII PEDDPCVWVS KEDDPENWHV QIFRSIDSGS
550 560 570 580 590 600
VKGFPKYEDE AEAQHLECAK RLVVDKSIQT AYIQTIRSAQ HFIYIENQYF LGSSYAWPSY
610 620 630 640 650 660
RDAGADNLIP MELALKIVSK IRAKERFAVY VVIPLWPEGD PKSGPVQEIL YWQSQTMQMM
670 680 690 700 710 720
YDVIAKELKA VQSDAHPLDY LNFYCLGKRE QLPDDMPATN GSVVSDSYNF QRFMIYVHAK
730 740 750 760 770 780
GMIVDDEYVL MGSANINQRS MAGTKDTEIA MGAYQPNHTW AHKGRHPRGQ VYGYRMSLWA
790 800 810 820 830 840
EHLGKTGDEF VEPSDLECLK KVNTISEENW KRFIDPKFSE LQGHLIKYPL QVDVDGKVSP
850 860
LPDYETFPDV GGKIIGAHSM ALPDTLTT