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 Q9R0X4

Entry ID Method Resolution Chain Position Source
AF-Q9R0X4-F1 Predicted AlphaFoldDB

25 variants for Q9R0X4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3411594325 71 P>S No EVA
rs3412312923 78 P>S No EVA
rs3389574061 87 I>N No EVA
rs3412603593 175 N>K No EVA
rs3389592961 184 M>I No EVA
rs234121038 220 I>V No EVA
rs3389577375 232 Q>E No EVA
rs3389588224 258 R>M No EVA
rs3389574105 269 L>M No EVA
rs260219360 306 V>I No EVA
rs3409684609 313 G>A No EVA
rs3411092800 316 M>I No EVA
rs3412348135 319 A>P No EVA
rs3389592885 332 G>S No EVA
rs3411092846 340 V>G No EVA
rs3389581771 347 K>* No EVA
rs3389580570 355 L>P No EVA
rs3412431762 365 Q>L No EVA
rs3389574604 381 D>E No EVA
rs3411985101 381 D>N No EVA
rs3389588187 402 P>S No EVA
rs3412792903 404 I>V No EVA
rs3411594447 412 S>F No EVA
rs3412792927 423 K>SMPFAP* No EVA
rs212109067 427 T>I No EVA

No associated diseases with Q9R0X4

2 regional properties for Q9R0X4

Type Name Position InterPro Accession
domain Hotdog acyl-CoA thioesterase (ACOT)-type domain 85 - 209 IPR033120-1
domain Hotdog acyl-CoA thioesterase (ACOT)-type domain 289 - 401 IPR033120-2

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
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.
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.

4 GO annotations of molecular function

Name Definition
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.
carboxylic ester hydrolase activity Catalysis of the hydrolysis of a carboxylic ester bond.
palmitoyl-CoA hydrolase activity Catalysis of the reaction: palmitoyl-CoA + H2O = CoA + palmitate.

3 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.
long-chain fatty acid metabolic process The chemical reactions and pathways involving long-chain fatty acids, A long-chain fatty acid is a fatty acid with a chain length between C13 and C22.
short-chain fatty acid metabolic process The chemical reactions and pathways involving fatty acids with a chain length of less than C6.

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
Q8WYK0 ACOT12 Acetyl-coenzyme A thioesterase Homo sapiens (Human) 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
Q9DBK0 Acot12 Acetyl-coenzyme A thioesterase Mus musculus (Mouse) PR
Q91V12 Acot7 Cytosolic acyl coenzyme A thioester hydrolase Mus musculus (Mouse) PR
Q8VHQ9 Acot11 Acyl-coenzyme A thioesterase 11 Mus musculus (Mouse) PR
Q32MW3 Acot10 Acyl-coenzyme A thioesterase 10, mitochondrial 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
MKRAAIRLWT LNKGLLTHGR GLSQGSQYKI SEPLHIHQVR DKLREIVGVS TVWRDHVKAM
70 80 90 100 110 120
EERKLLHSFL PKSQKVLPPR KMRDSYIEVL LPLGTDPELR DKYVTVQNTV RFGRILEDLD
130 140 150 160 170 180
SLGVLVCYMH NHNHSTKMSP LSIVTVLVDK IDMCKHSLSP EQDIKFTGHV SWVGNTSMEV
190 200 210 220 230 240
KMKMFQLHND EKYWPVLDAT FVMVARDSEN KGPAFVNPLI PENKEEEELF KQGELNKSRR
250 260 270 280 290 300
IAFSTSSLLK VAPSSEERNI IHELFLTTLD PKTISFQSRI LPPKAVWMED TKLKSLDICH
310 320 330 340 350 360
PQERNVFNRI FGGFLMRKAY ELAWATACSF GGSRPYVVTV DDIMFQKPVE VGSLLFLSSQ
370 380 390 400 410 420
VCFTQDNYIQ VRVHSEVSSL DSREHMTTNV FHFTFMSEKE VPLIFPKTYG ESMLYLDGQR
430
HFKSMSTPVT LKKDYPVEP