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

2 structures for Q6PFD5

Entry ID Method Resolution Chain Position Source
5IZU X-ray 249 A B/D 963-977 PDB
AF-Q6PFD5-F1 Predicted AlphaFoldDB

33 variants for Q6PFD5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388711648 33 Y>* No EVA
rs3388711656 78 P>S No EVA
rs238251429 218 T>P No EVA
rs3388714081 243 S>I No EVA
rs3388708271 259 W>* No EVA
rs3388700874 321 D>V No EVA
rs3388708306 323 Q>H No EVA
rs3388704902 364 H>L No EVA
rs3388700268 387 C>S No EVA
rs3388710595 403 E>D No EVA
rs3388719225 454 R>H No EVA
rs3388700300 497 R>P No EVA
rs3388715831 511 Q>K No EVA
rs3388711707 537 K>* No EVA
rs3388714106 564 H>R No EVA
rs3388709462 624 A>T No EVA
rs3388715870 644 D>G No EVA
rs3388709429 735 W>R No EVA
rs3388707933 794 E>D No EVA
rs3388713478 840 L>I No EVA
rs3388710647 872 G>D No EVA
rs3388700795 872 G>S No EVA
rs3388718372 878 Q>R No EVA
rs3388718432 893 Q>H No EVA
rs3388715847 894 L>P No EVA
rs3388714605 895 K>M No EVA
rs3388714605 895 K>T No EVA
rs3388704866 901 L>F No EVA
rs3388708297 904 P>L No EVA
rs3394671150 931 L>Q No EVA
rs3388700878 936 R>L No EVA
rs3388718434 953 S>L No EVA
rs3388710639 975 T>I No EVA

No associated diseases with Q6PFD5

2 regional properties for Q6PFD5

Type Name Position InterPro Accession
repeat Leucine-rich repeat 71 - 92 IPR001611-1
repeat Leucine-rich repeat 93 - 114 IPR001611-2

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane ; Peripheral membrane protein
  • Postsynaptic density
  • Synapse
  • Postsynaptic density of neuronal cells
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 GO annotations of cellular component

Name Definition
anchoring junction A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix.
cholinergic synapse A synapse that uses acetylcholine as a neurotransmitter.
dendritic spine A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity.
glutamatergic synapse A synapse that uses glutamate as a neurotransmitter.
neuromuscular junction The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential.
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.
postsynaptic specialization A network of proteins within and adjacent to the postsynaptic membrane. 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.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.

5 GO annotations of molecular function

Name Definition
amyloid-beta binding Binding to an amyloid-beta peptide/protein.
molecular adaptor activity The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.
PDZ domain binding Binding to a PDZ domain of a protein, a domain found in diverse signaling proteins.
protein domain specific binding Binding to a specific domain of a protein.
scaffold protein binding Binding to a scaffold protein. Scaffold proteins are crucial regulators of many key signaling pathways. Although not strictly defined in function, they are known to interact and/or bind with multiple members of a signaling pathway, tethering them into complexes.

4 GO annotations of biological process

Name Definition
modification of synaptic structure Any process that modifies the structure/morphology of a synapse.
protein-containing complex assembly The aggregation, arrangement and bonding together of a set of macromolecules to form a protein-containing complex.
regulation of postsynaptic neurotransmitter receptor activity Any process that modulates the frequency, rate or extent of neurotransmitter receptor activity involved in synaptic transmission. Modulation may be via an effect on ligand affinity, or effector funtion such as ion selectivity or pore opening/closing in ionotropic receptors.
signaling The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O95886 DLGAP3 Disks large-associated protein 3 Homo sapiens (Human) PR
P97838 Dlgap3 Disks large-associated protein 3 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MRGYHGDRGS HPRPARFADQ QHMDVGPAAR APYLLGSREA FSTEPRFCAP RAGLGHLSPE
70 80 90 100 110 120
GPLSLSEGPS SVGPEGGPGG VGAGGGSSTF PRMYPGQGPF DTCEDCVGHP QGKGATRLPP
130 140 150 160 170 180
TLLDQFEKQL PVQQDGFHTL PYQRGPAGPG PGPGSGAAPE ARSESPSRIR HLVHSVQKLF
190 200 210 220 230 240
AKSHSLEAPG KRDYNGPKAD GRGSSGGDSY SGPGSGGTPT SHHHHHHHHH HHHQSRHGKR
250 260 270 280 290 300
SKSKDRKGDG RHQTKATGWW SSDDNLDSDS GFLGGRPPGE PGGPFCLDAP DGSYRDLSFK
310 320 330 340 350 360
GRSGGSEGRC LACTGMSMSL DGQSVKRSAW HTMMVSQGRD GYPGAGPGKG LLGPETKAKA
370 380 390 400 410 420
RTYHYLQVPQ DDWGGYPTGG KDGEIPCRRM RSGSYIKAMG DEESGDSDGS PKTSPKALAR
430 440 450 460 470 480
RFASRRSSSV DTARINCCVP PRIHPRSSIP GYSRSLTTGQ LSEEFNQQLE AVCGSVFGEL
490 500 510 520 530 540
ESQAVDALDL PGCFRMRSHS YLRAIQAGCS QDDDCLPLLA APASVSGRPG SSFNFRKAPP
550 560 570 580 590 600
PIPPGSQAPP RISITAQSST DSAHESFTAA EGPARRCSSA DGLDGPTMGA RTLELAPVPP
610 620 630 640 650 660
RASPKPPTLI IKTIPGREEL RSLARQRKWR PSIGVQVETI SDSDTENRSR REFHSIGVQV
670 680 690 700 710 720
EEDKRRARFK RSNSVTAGVQ ADLELEGLAG LATVATEDKA LQFGRSFQRH ASEPQPGPRA
730 740 750 760 770 780
PTYSVFRTVH TQGQWAYREG YPLPYEPPAT DGSPGPTPVP APGPGSGRRD SWMERGSRSL
790 800 810 820 830 840
PDSGRTSPCP RDGEWFIKML RAEVEKLEHW CQQMEREAED YELPEEILEK IRSAVGSTQL
850 860 870 880 890 900
LLSQKVQQFF RLCQQSLDPT AFPVPTFQDL AGFWDLLQLS IEDVTLKFLE LQQLKANSWK
910 920 930 940 950 960
LLEPKEEKKV PPPIPKKPSR GRGVPVKERS LDSVDRQRQE ARKRLLAAKR AASFRHSSAT
970
ESADSIEIYI PEAQTRL