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 Q6NVF0

Entry ID Method Resolution Chain Position Source
AF-Q6NVF0-F1 Predicted AlphaFoldDB

45 variants for Q6NVF0

Variant ID(s) Position Change Description Diseaes Association Provenance
rs227153522 29 V>I No EVA
rs3410246432 43 I>F No EVA
rs3410146838 53 Q>* No EVA
rs30130935 85 R>Q No EVA
rs864266630 95 H>D No EVA
rs227418537 124 P>L No EVA
rs3389465159 138 T>N No EVA
rs3410471773 198 Q>R No EVA
rs3389552107 222 I>V No EVA
rs3409722980 227 T>A No EVA
rs3409992979 228 K>L No EVA
rs3389465149 263 C>S No EVA
rs3389514138 294 Q>L No EVA
rs3389551350 309 K>R No EVA
rs3410247158 349 G>W No EVA
rs216476492 397 T>I No EVA
rs216476492 397 T>S No EVA
rs247876485 404 T>A No EVA
rs3389573265 449 F>V No EVA
rs257816732 473 V>I No EVA
rs3389514092 486 D>Y No EVA
rs3389465177 488 S>T No EVA
rs3389465142 504 G>* No EVA
rs3389568612 506 N>I No EVA
rs3389556536 517 E>K No EVA
rs3389507166 536 V>A No EVA
rs3389573279 574 E>* No EVA
rs3389573232 577 K>* No EVA
rs3389559208 673 N>I No EVA
rs3389551374 713 E>D No EVA
rs30137468 743 H>Y No EVA
rs248646866 760 M>L No EVA
rs3410306069 798 P>A No EVA
rs3410217831 810 C>HEQSQDIADTAHNR* No EVA
rs3389568579 826 Q>L No EVA
rs30133537 843 R>H No EVA
rs3389514071 874 L>I No EVA
rs30134379 876 T>A No EVA
rs30134382 885 H>R No EVA
rs3409340011 895 L>V No EVA
rs3410471760 896 G>A No EVA
rs3410353665 896 G>R No EVA
rs3408969810 897 N>K No EVA
rs3409723034 898 E>Q No EVA
rs3410105812 901 D>Q No EVA

No associated diseases with Q6NVF0

7 regional properties for Q6NVF0

Type Name Position InterPro Accession
domain Rho GTPase-activating protein domain 720 - 900 IPR000198
domain Inositol polyphosphate-related phosphatase 237 - 538 IPR000300
domain Endonuclease/exonuclease/phosphatase 244 - 523 IPR005135
domain Inositol polyphosphate 5-phosphatase, clathrin binding domain 19 - 117 IPR031995
domain OCRL1, PH domain 11 - 115 IPR037787
domain OCRL1/INPP5B, INPP5c domain 239 - 532 IPR037793
domain Inositol polyphosphate 5-phosphatase OCRL, RhoGAP 667 - 895 IPR047078

Functions

Description
EC Number 3.1.3.36 Phosphoric monoester hydrolases
Subcellular Localization
  • Cytoplasmic vesicle, phagosome membrane
  • Early endosome membrane
  • Membrane, clathrin-coated pit
  • Cell projection, cilium, photoreceptor outer segment
  • Cell projection, cilium
  • Cytoplasmic vesicle
  • Endosome
  • Golgi apparatus, trans-Golgi network
  • Also found on macropinosomes
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

12 GO annotations of cellular component

Name Definition
clathrin-coated pit A part of the endomembrane system in the form of an invagination of a membrane upon which a clathrin coat forms, and that can be converted by vesicle budding into a clathrin-coated vesicle. Coated pits form on the plasma membrane, where they are involved in receptor-mediated selective transport of many proteins and other macromolecules across the cell membrane, in the trans-Golgi network, and on some endosomes.
clathrin-coated vesicle A vesicle with a coat formed of clathrin connected to the membrane via one of the clathrin adaptor complexes.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
early endosome A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways.
early endosome membrane The lipid bilayer surrounding an early endosome.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
phagocytic vesicle membrane The lipid bilayer surrounding a phagocytic vesicle.
photoreceptor outer segment The outer segment of a vertebrate photoreceptor that contains a stack of membrane discs embedded with photoreceptor proteins.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
trans-Golgi network The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.

8 GO annotations of molecular function

Name Definition
GTPase activator activity Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
inositol phosphate phosphatase activity Catalysis of the reaction: inositol phosphate(n) + H2O = inositol phosphate(n-1) + phosphate. This reaction is the removal of a phosphate group from an inositol phosphate.
inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity Catalysis of the reaction: 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
inositol-1,4,5-trisphosphate 5-phosphatase activity Catalysis of the reaction: 1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol 1,4-bisphosphate + phosphate.
inositol-polyphosphate 5-phosphatase activity Catalysis of the reactions: D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate, and 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity Catalysis of the reaction: phosphatidylinositol-3,4,5-trisphosphate + H2O = phosphatidylinositol-3,4-bisphosphate + phosphate.
phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.
small GTPase binding Binding to a small monomeric GTPase.

6 GO annotations of biological process

Name Definition
cilium assembly The assembly of a cilium, a specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface. Each cilium is bounded by an extrusion of the cytoplasmic membrane, and contains a regular longitudinal array of microtubules, anchored basally in a centriole.
in utero embryonic development The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus.
inositol phosphate dephosphorylation The process of removing a phosphate group from any mono- or polyphosphorylated inositol.
phosphatidylinositol dephosphorylation The process of removing one or more phosphate groups from a phosphatidylinositol.
regulation of GTPase activity Any process that modulates the rate of GTP hydrolysis by a GTPase.
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.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9NRR6 INPP5E Phosphatidylinositol polyphosphate 5-phosphatase type IV Homo sapiens (Human) PR
Q92835 INPP5D Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 Homo sapiens (Human) PR
P32019 INPP5B Type II inositol 1,4,5-trisphosphate 5-phosphatase Homo sapiens (Human) PR
Q9ES52 Inpp5d Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 Mus musculus (Mouse) PR
Q8K337 Inpp5b Type II inositol 1,4,5-trisphosphate 5-phosphatase Mus musculus (Mouse) PR
P97573 Inpp5d Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MEPRLPIGAQ PLAMVAGLEM KGPLREPCVL TLARRNGQYE LIIQLHGKEQ HVQDIIPINS
70 80 90 100 110 120
HFRCVQEAEE TLLIDIASNS GCKIRVQGDW TRERHFEIPD EERCLKFLSE VLEAQEAQSQ
130 140 150 160 170 180
LLVPEQKDSS SWYQKLDTMD KPAYSGLLGF EDNFSSLDLD KKMNTQNPRS GSHREPPPPP
190 200 210 220 230 240
SSSTRMLSRE KEASNKEQPK VTNTMRKLFV PNTQTGQREG LIKHILTKRE KEYVNIQSFR
250 260 270 280 290 300
FFVGTWNVNG QSPDSSLEPW LDCDPNPPDI YCIGFQELDL STEAFFYFES VKEQEWSLAV
310 320 330 340 350 360
ERGLPSKAKY RKVQLVRLVG MMLLIFARKD QCQYIRDVAT ETTGTGIMGK MGNKGGVAVR
370 380 390 400 410 420
FVFHNTTFCI VNSHLAAHVE EFERRNQDYK DICARMTFSV PNQTVPQVNI MKHDVVIWLG
430 440 450 460 470 480
DLNYRLCMPD ASEVKSLINK NELHKLLKFD QLNIQRTQKK AFADFNEGEI NFVPTYKYDS
490 500 510 520 530 540
KTDRWDSSGK CRVPAWCDRI LWRGINVNQL HYRSHMELKT SDHKPVSALF HIGVKVVDER
550 560 570 580 590 600
RYRKVFEDIV RIMDRMENDF LPSLELSRRE FFFENVKFRQ LQKEKFQISN NGQVPCHFSF
610 620 630 640 650 660
IPKLNDSQYC KPWLRAEPFE GYLEPNETLD ISLDVYVSKD SVTILNSGED KIEDILVLHL
670 680 690 700 710 720
DRGKDYFLTI GGNYLPSCFG TSLEALCRMK RPIREVPVTK LIDLEEDSYL EKEKSLLQMV
730 740 750 760 770 780
PLDEGTSERP LQVPKEIWLL VDHLFKYACH QEDLFQTPGM QEELQQIIDC LDTSIPETIP
790 800 810 820 830 840
GNNHSVAEAL LIFLEALPEP VICYELYQRC LDSAHDPRIC KQVISQLPRC HRNVFRYLMA
850 860 870 880 890
FLRELLKFSD YNNINTNMIA TLFSSLLLRP PPNLMTRQTP NDRQHAIQFL LVFLLGNEED