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 Q8RWZ3

Entry ID Method Resolution Chain Position Source
AF-Q8RWZ3-F1 Predicted AlphaFoldDB

52 variants for Q8RWZ3

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_3_2146550_G_A 6 G>D No 1000Genomes
ENSVATH05787171 12 I>V No 1000Genomes
ENSVATH00310183 17 R>L No 1000Genomes
tmp_3_2146606_C_T 25 R>C No 1000Genomes
ENSVATH05787172 30 N>D No 1000Genomes
ENSVATH10533941 40 Q>L No 1000Genomes
tmp_3_2146666_C_G 45 Q>E No 1000Genomes
tmp_3_2146667_A_G 45 Q>R No 1000Genomes
ENSVATH10533942 70 L>V No 1000Genomes
tmp_3_2146878_A_G 86 D>G No 1000Genomes
ENSVATH13880659 99 T>I No 1000Genomes
ENSVATH05787186 114 A>T No 1000Genomes
ENSVATH00310186 115 V>I No 1000Genomes
tmp_3_2147188_G_A 119 A>T No 1000Genomes
ENSVATH05787187 137 P>A No 1000Genomes
tmp_3_2147367_C_G 141 P>R No 1000Genomes
tmp_3_2147378_A_T 145 N>Y No 1000Genomes
ENSVATH05787191 146 A>S No 1000Genomes
tmp_3_2147621_A_C 187 K>N No 1000Genomes
ENSVATH10533985 202 P>S No 1000Genomes
ENSVATH05787196 246 V>I No 1000Genomes
tmp_3_2147909_C_G 257 L>V No 1000Genomes
ENSVATH05787198 269 M>I No 1000Genomes
ENSVATH13880662 275 V>F No 1000Genomes
tmp_3_2148152_C_A 308 A>E No 1000Genomes
tmp_3_2148488_G_A 355 G>R No 1000Genomes
tmp_3_2148513_A_T 363 E>V No 1000Genomes
tmp_3_2148545_G_T 374 V>F No 1000Genomes
ENSVATH00310192 389 S>L No 1000Genomes
ENSVATH05787206 392 S>R No 1000Genomes
ENSVATH13880663 393 L>F No 1000Genomes
ENSVATH05787207 406 V>I No 1000Genomes
ENSVATH00310194 464 D>H No 1000Genomes
tmp_3_2148988_A_C 470 R>S No 1000Genomes
tmp_3_2149017_A_G 480 H>R No 1000Genomes
ENSVATH02120105 490 L>F No 1000Genomes
tmp_3_2149055_G_A 493 E>K No 1000Genomes
ENSVATH10533988 499 E>D No 1000Genomes
tmp_3_2149073_G_A 499 E>K No 1000Genomes
ENSVATH05787211 506 I>V No 1000Genomes
ENSVATH05787212 507 M>I No 1000Genomes
ENSVATH10533990 530 I>V No 1000Genomes
ENSVATH13880685 573 S>Y No 1000Genomes
ENSVATH13880686 575 R>G No 1000Genomes
ENSVATH00310197 600 V>F No 1000Genomes
tmp_3_2149805_A_G 629 I>V No 1000Genomes
ENSVATH05787222 630 S>N No 1000Genomes
tmp_3_2150126_G_T 703 A>S No 1000Genomes
ENSVATH00310199 711 K>N No 1000Genomes
ENSVATH10534038 723 L>F No 1000Genomes
tmp_3_2150532_T_C 785 S>P No 1000Genomes
tmp_3_2150542_T_G 788 V>G No 1000Genomes

No associated diseases with Q8RWZ3

2 regional properties for Q8RWZ3

Type Name Position InterPro Accession
domain Phospholipid/glycerol acyltransferase 83 - 213 IPR002123
domain 1-acyl-sn-glycerol-3-phosphate acyltransferase 81 - 210 IPR004552

Functions

Description
EC Number
Subcellular Localization
  • Peroxisome
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.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

2 GO annotations of molecular function

Name Definition
acyl-CoA dehydrogenase activity Catalysis of the reaction: acyl-CoA + oxidized
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

2 GO annotations of biological process

Name Definition
fatty acid beta-oxidation using acyl-CoA dehydrogenase A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
root hair elongation The process in which the root hair grows longer.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q6JQN1 ACAD10 Acyl-CoA dehydrogenase family member 10 Homo sapiens (Human) PR
10 20 30 40 50 60
MGSSTGDLVT RIQSAHRFDH DALFRFAADN VSGFPTNPSQ FKVSQFGHGQ SNPTFLIEVG
70 80 90 100 110 120
SGSSLKRYVL RKKPPGKLLQ SAHAVDREFQ VLRALGEHTQ VPVPKVFCLC TDPAVIGTAF
130 140 150 160 170 180
YIMEFMEGRI FIDPKLPNVA PERRNAIYRA TAKALASLHS ADVDAIGLEK YGRRGNYCKR
190 200 210 220 230 240
QIDRWFKQYL ASTSEGKPER NPKMFELVDW LRKNIPAEDS TGATSGLVHG DFRIDNLVFH
250 260 270 280 290 300
PSEDRVIGII DWELSTLGNQ MCDVAYSCMH YIVNVQLDKE HVSEGFETTG LPEGMLSMPE
310 320 330 340 350 360
FLLEYCSASG KPWPAANWKF YVAFSLFRAA SIYTGVYSRW LMGNASAGER ARNTGVQANE
370 380 390 400 410 420
LVESALGYIA RENVLPEHPP SVQRDVSPSY ESLVDGSGRF IPNRKVLELR QKLIKFMETH
430 440 450 460 470 480
IYPMENEFSK LAQSDMRWTV HPQEEKLKEM AKREGLWNLF VPVDSAARAR RELAATENKH
490 500 510 520 530 540
NLSGKSFDQL FGEGLTNLEY GYLCEIMGRS VWAPQVFNCG APDTGNMEVI LRYGNKEQIS
550 560 570 580 590 600
EWLIPLLEGR IRSGFAMTEP QVASSDATNI ECSIRRQGDS YVINGTKWWT SGAMDPRCRV
610 620 630 640 650 660
LILMGKTDFN APKHKQQSMI LVDMRTPGIS VKRPLTVFGF DDAPHGHAEI SFENVVVPAK
670 680 690 700 710 720
NILLGEGRGF EIAQGRLGPG RLHHCMRLIG AAERGMELMA QRALSRKTFG KFIAQHGSFV
730 740 750 760 770 780
SDLAKLRVEL EGTRLLVLEA ADHLDKFGNK KARGILAMAK VAAPNMALKV LDTAIQVHGA
790 800 810 820
AGVSSDTVLA HLWATARTLR IADGPDEVHL GTIGKLELQR ASKL