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 Q6PEI3

Entry ID Method Resolution Chain Position Source
AF-Q6PEI3-F1 Predicted AlphaFoldDB

No variants for Q6PEI3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6PEI3

No associated diseases with Q6PEI3

1 regional properties for Q6PEI3

Type Name Position InterPro Accession
domain GPCR, rhodopsin-like, 7TM 51 - 324 IPR017452

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cell projection, lamellipodium
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
lamellipodium A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.

3 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
protein phosphatase 1 binding Binding to a protein phosphatase 1.
protein phosphatase activator activity Binds to and increases the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.

9 GO annotations of biological process

Name Definition
actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
closure of optic fissure The closure of the temporary ventral gap in the optic cup that contributes to its shaping.
enteric nervous system development The process whose specific outcome is the progression of the enteric nervous system over time, from its formation to the mature structure. The enteric nervous system is composed of two ganglionated neural plexuses in the gut wall which form one of the three major divisions of the autonomic nervous system. The enteric nervous system innervates the gastrointestinal tract, the pancreas, and the gall bladder. It contains sensory neurons, interneurons, and motor neurons. Thus the circuitry can autonomously sense the tension and the chemical environment in the gut and regulate blood vessel tone, motility, secretions, and fluid transport. The system is itself governed by the central nervous system and receives both parasympathetic and sympathetic innervation.
negative regulation of integrin-mediated signaling pathway Any process that stops, prevents or reduces the frequency, rate or extent of integrin-mediated signaling pathway.
neural crest cell migration The characteristic movement of cells from the dorsal ridge of the neural tube to a variety of locations in a vertebrate embryo.
neural tube closure The last step in the formation of the neural tube, where the paired neural folds are brought together and fuse at the dorsal midline.
positive regulation of catalytic activity Any process that activates or increases the activity of an enzyme.
regulation of cell cycle Any process that modulates the rate or extent of progression through the cell cycle.
Rho protein signal transduction The series of molecular signals within the cell that are mediated by a member of the Rho family of proteins switching to a GTP-bound active state.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P33304 AFR1 Protein AFR1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q8IZ21 PHACTR4 Phosphatase and actin regulator 4 Homo sapiens (Human) PR
Q2M3X8 Phactr1 Phosphatase and actin regulator 1 Mus musculus (Mouse) PR
10 20 30 40 50 60
MENRDDEVEH QHSTMGSEGG TAGDGTPPPK RKGKFSTLGK IFKPWKWRKK KSSEKFKETS
70 80 90 100 110 120
EVLERKMSMR RPRQELIEQG VLKELPDNES GEAHGHKAPY VKNGHTLPVG VGGSLALEQV
130 140 150 160 170 180
HSPSESEFRI NPVWLPQPED RRARAPSDGD HRGALGPRAS NQDDGRRGGW SVGTEDWKNN
190 200 210 220 230 240
LAWHGEDIRR GGRAHAEMDK RPGLMKAPSE DGRRTRPEPD WKPTLPRHSS VEEGRGRRES
250 260 270 280 290 300
DSSQYLPNSE MMRDTLREPL PPKQSIMPPK WLMTSTPEPG SDSLPRTPVH NPAAPSFCSS
310 320 330 340 350 360
NSSSSSSAGK PLRNVSSAGA NTAPPGGAPL TTSSAPCSMG TIPNHPSKQP PMPPPKPINR
370 380 390 400 410 420
SNNPAIMAEL TQGGMNLVPA KPSPPMPPKR TTPVTKRNPE DSPLTIASLP SILSEDMRAN
430 440 450 460 470 480
IPGGYQLPPP PPSPPLPTHI PPSPPRAHTH HLLHQHSYPY PLPQPLPVHF DPPSPPEDPP
490 500 510 520 530 540
ARDEDDYSDE EEEEEDDEDD EEPPPDHLPS PQSQPELEPR SRRCLVGELS VSVIPEGNNS
550 560 570 580 590 600
SEEEEDEEDQ HPEESDSDGP VLYKDDESDE DEEDDSPPSA LASRVKRKDT LALKLSSRPS
610 620 630 640 650 660
APDRQAPERQ AKSEHSGLSW QSKEQWEAIR TQIGTALTRR LSQRPTAEEL EQRNILQPKN
670 680 690 700 710 720
EADRQAEVRE IKRRLTRKLS QRPTVAELQA RKILRFHEYV EVTSAQDYDR RADKPWTKLT
730 740 750
PADKAAIRKE LNEFKSSEME VHEESRIYTR FHRP