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 Q8VHQ9

Entry ID Method Resolution Chain Position Source
AF-Q8VHQ9-F1 Predicted AlphaFoldDB

39 variants for Q8VHQ9

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388699880 9 L>* No EVA
rs232228938 34 P>A No EVA
rs3388696843 38 A>VSDG* No EVA
rs3394649178 48 E>V No EVA
rs3394645233 62 H>L No EVA
rs3394694697 118 N>H No EVA
rs3388685862 169 T>S No EVA
rs3388700786 200 C>G No EVA
rs3388693648 204 D>V No EVA
rs3388694799 222 E>V No EVA
rs3388694692 224 V>D No EVA
rs3388704085 257 R>Q No EVA
rs3388703269 257 R>W No EVA
rs3388696906 284 V>M No EVA
rs3388700419 286 K>T No EVA
rs3388699829 288 I>N No EVA
rs3388685875 294 K>M No EVA
rs3388691597 301 V>E No EVA
rs3388688430 302 C>* No EVA
rs3388693626 317 I>V No EVA
rs3388685947 342 Q>K No EVA
rs3388700764 379 P>H No EVA
rs3388703227 380 W>* No EVA
rs3388700789 406 V>M No EVA
rs3394649187 449 R>S No EVA
rs3388704009 458 S>* No EVA
rs3388678145 464 Q>* No EVA
rs28168845 466 D>Y No EVA
rs3388700483 471 I>F No EVA
rs3388693641 473 H>R No EVA
rs3388698656 475 I>F No EVA
rs3388697224 484 K>M No EVA
rs3388691601 489 V>L No EVA
rs3388697306 520 P>S No EVA
rs3388694811 521 E>D No EVA
rs3388678185 576 C>R No EVA
rs3388699862 581 L>* No EVA
rs3388691586 588 A>D No EVA
rs3388700436 595 L>L No EVA

No associated diseases with Q8VHQ9

5 regional properties for Q8VHQ9

Type Name Position InterPro Accession
domain START domain 385 - 583 IPR002913
domain Thioesterase domain 69 - 135 IPR006683-1
domain Thioesterase domain 235 - 304 IPR006683-2
domain Hotdog acyl-CoA thioesterase (ACOT)-type domain 45 - 157 IPR033120-1
domain Hotdog acyl-CoA thioesterase (ACOT)-type domain 217 - 330 IPR033120-2

Functions

Description
EC Number 3.1.2.2 Thiolester hydrolases
Subcellular Localization
  • Mitochondrion matrix
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.

6 GO annotations of molecular function

Name Definition
acyl-CoA hydrolase activity Catalysis of the reaction: acyl-CoA + H2O = CoA + a carboxylate.
carboxylic ester hydrolase activity Catalysis of the hydrolysis of a carboxylic ester bond.
long-chain acyl-CoA hydrolase activity Catalysis of the reaction: H2O + a long-chain acyl-CoA = a long-chain carboxylate + CoA. A long chain is a chain of greater than 12 carbons in length.
long-chain fatty acyl-CoA binding Binding to a long-chain fatty acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
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.

6 GO annotations of biological process

Name Definition
acyl-CoA metabolic process The chemical reactions and pathways involving acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with an acyl group.
fatty acid metabolic process The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
intracellular signal transduction The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
negative regulation of cold-induced thermogenesis Any process that stops, prevents, or reduces the rate of cold-induced thermogenesis.
response to cold Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.
response to temperature stimulus Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a temperature stimulus.

10 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3SWX2 ACOT9 Acyl-coenzyme A thioesterase 9, mitochondrial Bos taurus (Bovine) PR
O00154 ACOT7 Cytosolic acyl coenzyme A thioester hydrolase Homo sapiens (Human) PR
Q9Y305 ACOT9 Acyl-coenzyme A thioesterase 9, mitochondrial Homo sapiens (Human) PR
Q8WYK0 ACOT12 Acetyl-coenzyme A thioesterase Homo sapiens (Human) PR
Q9R0X4 Acot9 Acyl-coenzyme A thioesterase 9, mitochondrial Mus musculus (Mouse) PR
Q32MW3 Acot10 Acyl-coenzyme A thioesterase 10, mitochondrial Mus musculus (Mouse) PR
Q9DBK0 Acot12 Acetyl-coenzyme A thioesterase Mus musculus (Mouse) PR
Q91V12 Acot7 Cytosolic acyl coenzyme A thioester hydrolase Mus musculus (Mouse) PR
Q64559 Acot7 Cytosolic acyl coenzyme A thioester hydrolase Rattus norvegicus (Rat) PR
Q99NB7 Acot12 Acetyl-coenzyme A thioesterase Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MIQNVGNHLR RGFASMFSNR TSRKSISHPE SGDPPTMAEG EGYRNPTEVQ MSQLVLPCHT
70 80 90 100 110 120
NHRGELSIGQ LLKWIDTTAC LSAERHAGCP CVTASMDDIY FDHTISVGQV VNIKAKVNRA
130 140 150 160 170 180
FNSSMEVGIQ VVSEDLCSEK QWSVCKALAT FVAHRELSKV KLKQVIPLTE EEKTEHGVAA
190 200 210 220 230 240
ERRRMRLVYA DTIKDLLTHC VIQDDLDKDC SNMVPAEKTR VESVELVLPP HANHQGNTFG
250 260 270 280 290 300
GQIMAWMENV ATIAASRLCH AHPTLKAIEM FHFRGPSQVG DRLVLKAIVN NAFKHSMEVG
310 320 330 340 350 360
VCVEAYRQEA ETQRRHINSA FMTFVVLDKD DQPQKLPWIR PQPGEGERRY REASARKKIR
370 380 390 400 410 420
LDRKYLVSCK QAEVALSVPW DPSNQVYLSY YNVSSLKTLM AKDNWVLSVE ISEVRLYILE
430 440 450 460 470 480
EDFLSFHLEM VVNVDAAQVF QLLSDLRRRP EWDKHYRSVE LVQQVDEDDA IYHVISPALS
490 500 510 520 530 540
GNTKPQDFVI LASRRKPCDN GDPYVIALRS VTLPTHHETP EYQRGETLCS GFCLWREGDQ
550 560 570 580 590
MTKVSYYNQA TPGFLNYVTT NVSGLSSEFY NTFKACESFL LDNRNDLAPS LQTL