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 Q3T0R7

Entry ID Method Resolution Chain Position Source
AF-Q3T0R7-F1 Predicted AlphaFoldDB

28 variants for Q3T0R7

Variant ID(s) Position Change Description Diseaes Association Provenance
rs441695456 13 K>E No EVA
rs459954412 15 T>N No EVA
rs473035015 15 T>P No EVA
rs439764267 16 P>S No EVA
rs209468994 20 Y>H No EVA
rs522531637 21 G>R No EVA
rs455071023 22 G>C No EVA
rs434879103 26 D>G No EVA
rs466194542 28 T>S No EVA
rs716926053 38 R>K No EVA
rs446647974 39 A>S No EVA
rs464320575 40 A>G No EVA
rs432959731 40 A>S No EVA
rs450695494 46 V>G No EVA
rs461587567 47 S>* No EVA
rs481664691 47 S>A No EVA
rs481664691 47 S>P No EVA
rs479582518 48 P>S No EVA
rs479582518 48 P>T No EVA
rs439818033 59 V>A No EVA
rs439818033 59 V>G No EVA
rs444608224 60 M>I No EVA
rs436087797 62 S>C No EVA
rs433138791 137 K>M No EVA
rs517849578 191 K>E No EVA
rs480776685 319 V>E No EVA
rs467049559 325 P>S No EVA
rs435625594 375 K>N No EVA

No associated diseases with Q3T0R7

5 regional properties for Q3T0R7

Type Name Position InterPro Accession
conserved_site Acyl-CoA dehydrogenase, conserved site 215 - 227 IPR006089-1
conserved_site Acyl-CoA dehydrogenase, conserved site 435 - 454 IPR006089-2
domain Acyl-CoA oxidase/dehydrogenase, middle domain 213 - 315 IPR006091
domain Acyl-CoA dehydrogenase/oxidase C-terminal 327 - 473 IPR009075
domain Acyl-CoA dehydrogenase/oxidase, N-terminal 102 - 209 IPR013786

Functions

Description
EC Number 2.3.1.9 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

6 GO annotations of molecular function

Name Definition
acetyl-CoA C-acetyltransferase activity Catalysis of the reaction: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
acetyl-CoA C-acyltransferase activity Catalysis of the reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
acetyl-CoA hydrolase activity Catalysis of the reaction: acetyl-CoA + H(2)O = acetate + CoA + H(+).
acyl-CoA hydrolase activity Catalysis of the reaction: acyl-CoA + H2O = CoA + a carboxylate.
myristoyl-CoA hydrolase activity Catalysis of the reaction: myristoyl-CoA + H2O <=> H+ + tetradecanoate + coenzyme A.
palmitoyl-CoA hydrolase activity Catalysis of the reaction: palmitoyl-CoA + H2O = CoA + palmitate.

2 GO annotations of biological process

Name Definition
fatty acid beta-oxidation A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Any process that stops, prevents or reduces the frequency, rate or extent of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P42765 ACAA2 3-ketoacyl-CoA thiolase, mitochondrial Homo sapiens (Human) PR
Q8BWT1 Acaa2 3-ketoacyl-CoA thiolase, mitochondrial Mus musculus (Mouse) PR
10 20 30 40 50 60
MALLRGVFIV AAKRTPFGAY GGLLKDFTPT DMAEFAARAA LSAGRVSPET VDSVVVGNVM
70 80 90 100 110 120
QSSSDAIYLA RHVGLRVGIP KETPAITINR LCGSGFQSIV SGCQEICSRD SEVVLCGGTE
130 140 150 160 170 180
SMSQAPYCVR NIRFGTKLGS ELKLEDTLWT GLTDTHVQMP MAITAENLAV KHQISREDCD
190 200 210 220 230 240
RYALQSQQRW KTANDAGYFD NEMAPVEVKT RKGKQTMQVD EHPRPQTTME QLNKLPPVFK
250 260 270 280 290 300
KEGTVTAGNA SGVSDGAGAV IIASEDAVKK HNFTPLARIV GYFVSGCDPT IMGIGPVPAI
310 320 330 340 350 360
SGALKKTGLS LKDMDLVEVN EAFAPQYLAV EKSLNLDPSK TNVNGGAIAL GHPLAGSGSR
370 380 390
ITAHLVHELR RRGGKYAVGS ACIGGGQGIA VIIENTA