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 P55772

Entry ID Method Resolution Chain Position Source
AF-P55772-F1 Predicted AlphaFoldDB

29 variants for P55772

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389495557 84 C>Y No EVA
rs248887205 91 I>V No EVA
rs3389548497 115 L>P No EVA
rs258492218 121 H>Q No EVA
rs3389505237 149 L>Q No EVA
rs50631529 158 S>G No EVA
rs3389550705 170 T>I No EVA
rs3389554309 172 Q>K No EVA
rs3389486377 180 I>N No EVA
rs3389543341 183 N>T No EVA
rs3389550723 187 G>D No EVA
rs3389532447 190 T>I No EVA
rs262287260 276 V>I No EVA
rs235685804 289 V>I No EVA
rs254463842 302 K>E No EVA
rs254415654 312 Q>R No EVA
rs215791797 314 R>Q No EVA
rs3409437576 320 D>V No EVA
rs3389518247 347 V>I No EVA
rs3389518247 347 V>L No EVA
rs3389495534 354 G>W No EVA
rs3389554362 364 F>I No EVA
rs3389505283 369 F>L No EVA
rs3389543427 372 V>L No EVA
rs3389532424 373 A>S No EVA
rs3389505239 397 E>G No EVA
rs3389518201 406 K>M No EVA
rs253593016 438 H>Y No EVA
rs215403547 507 K>N No EVA

No associated diseases with P55772

No regional properties for P55772

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P55772

Functions

Description
EC Number 3.6.1.5 In phosphorus-containing anhydrides
Subcellular Localization
  • Membrane ; Multi-pass membrane protein
  • Membrane, caveola
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

13 GO annotations of cellular component

Name Definition
basement membrane A collagen-containing extracellular matrix consisting of a thin layer of dense material found in various animal tissues interposed between the cells and the adjacent connective tissue. It consists of the basal lamina plus an associated layer of reticulin fibers.
basolateral plasma membrane The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis.
cell surface The external part of the cell wall and/or plasma membrane.
external side of plasma membrane The leaflet of the plasma membrane that faces away from the cytoplasm and any proteins embedded or anchored in it or attached to its surface.
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
postsynaptic density An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
synaptic membrane A specialized area of membrane on either the presynaptic or the postsynaptic side of a synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell.
synaptic vesicle A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.

8 GO annotations of molecular function

Name Definition
ADP phosphatase activity Catalysis of the reaction: ADP + H2O = AMP + phosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GDP phosphatase activity Catalysis of the reaction: GDP + H2O = GMP + phosphate.
identical protein binding Binding to an identical protein or proteins.
nucleoside diphosphate phosphatase activity Catalysis of the reaction: a nucleoside diphosphate + H2O = a nucleoside monophosphate + phosphate.
ribonucleoside triphosphate phosphatase activity Catalysis of the reaction: a ribonucleoside triphosphate + H2O = a ribonucleoside diphosphate + H+ + phosphate.
UDP phosphatase activity Catalysis of the reaction: UDP + H2O = UMP + phosphate.

7 GO annotations of biological process

Name Definition
ADP catabolic process The chemical reactions and pathways resulting in the breakdown of ADP, adenosine 5'-diphosphate.
G protein-coupled receptor signaling pathway The series of molecular signals initiated by a ligand binding to its receptor, in which the activated receptor promotes the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, and ends with regulation of a downstream cellular process. The pathway can start from the plasma membrane, Golgi or nuclear membrane.
negative regulation of ATP biosynthetic process Any process that stops, prevents or reduces the frequency, rate or extent of ATP biosynthetic process.
negative regulation of dopamine secretion Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of dopamine.
nucleoside diphosphate catabolic process The chemical reactions and pathways resulting in the breakdown of a nucleoside diphosphate, a compound consisting of a nucleobase linked to a deoxyribose or ribose sugar esterified with diphosphate on the sugar.
platelet activation A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug.
purine ribonucleoside diphosphate catabolic process The chemical reactions and pathways resulting in the breakdown of purine ribonucleoside diphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with diphosphate on the sugar.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9NQZ7 ENTPD7 Ectonucleoside triphosphate diphosphohydrolase 7 Homo sapiens (Human) PR
Q3TCT4 Entpd7 Ectonucleoside triphosphate diphosphohydrolase 7 Mus musculus (Mouse) PR
P97687 Entpd1 Ectonucleoside triphosphate diphosphohydrolase 1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MEDIKDSKVK RFCSKNILII LGFTSILAVI ALIAVGLTQN KPLPENVKYG IVLDAGSSHT
70 80 90 100 110 120
NLYIYKWPAE KENDTGVVQQ LEECQVKGPG ISKYAQKTDE IGAYLAECME LSTELIPTSK
130 140 150 160 170 180
HHQTPVYLGA TAGMRLLRME SEQSADEVLA AVSTSLKSYP FDFQGAKIIT GQEEGAYGWI
190 200 210 220 230 240
TINYLLGRFT QEQSWLSLIS DSQKQETFGA LDLGGASTQI TFVPQNSTIE SPENSLQFRL
250 260 270 280 290 300
YGEDYTVYTH SFLCYGKDQA LWQKLAKDIQ VSSGGVLKDP CFNPGYEKVV NVSELYGTPC
310 320 330 340 350 360
TKRFEKKLPF DQFRIQGTGD YEQCHQSILE LFNNSHCPYS QCAFNGVFLP PLHGSFGAFS
370 380 390 400 410 420
AFYFVMDFFK KVAKNSVISQ EKMTEITKNF CSKSWEETKT SYPSVKEKYL SEYCFSGAYI
430 440 450 460 470 480
LSLLQGYNFT DSSWEQIHFM GKIKDSNAGW TLGYMLNLTN MIPAEQPLSP PLPHSTYIGL
490 500
MVLFSLLLVA VAITGLFIYS KPSYFWKEAV