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 P48818

Entry ID Method Resolution Chain Position Source
AF-P48818-F1 Predicted AlphaFoldDB

157 variants for P48818

Variant ID(s) Position Change Description Diseaes Association Provenance
rs432568987 5 R>G No EVA
rs469654731 13 Q>P No EVA
rs438287394 15 L>M No EVA
rs456945348 16 R>S No EVA
rs473762903 20 V>G No EVA
rs435979649 23 W>S No EVA
rs453008705 26 E>A No EVA
rs453008705 26 E>G No EVA
rs466646586 40 Y>F No EVA
rs110823820 41 A>D No EVA
rs432017002 42 S>R No EVA
rs469047920 49 V>G No EVA
rs437740436 52 S>A No EVA
rs454847436 53 D>Y No EVA
rs474931659 54 S>A No EVA
rs440255208 55 Q>P No EVA
rs454053700 58 E>Q No EVA
rs470937146 59 A>S No EVA
rs439782088 63 E>A No EVA
rs463046472 65 R>L No EVA
rs483238039 66 A>T No EVA
rs433877260 72 S>P No EVA
rs471027565 80 G>R No EVA
rs456499453 81 Q>* No EVA
rs476713868 90 Y>C No EVA
rs476713868 90 Y>S No EVA
rs441379710 93 V>G No EVA
rs471921278 94 L>F No EVA
rs471921278 94 L>I No EVA
rs443856206 94 L>P No EVA
rs482670062 95 N>K No EVA
rs448128118 97 D>E No EVA
rs461843721 99 T>K No EVA
rs447495928 100 Q>H No EVA
rs478879865 100 Q>L No EVA
rs464313680 101 F>V No EVA
rs478098802 102 L>P No EVA
rs450000258 114 E>D No EVA
rs461687123 116 V>G No EVA
rs478760895 125 L>P No EVA
rs440904576 131 T>P No EVA
rs457975227 138 E>G No EVA
rs477996395 143 G>V No EVA
rs438611048 189 I>S No EVA
rs473126861 189 I>V No EVA
rs458822549 208 G>R No EVA
rs460952989 209 E>D No EVA
rs480802531 210 T>A No EVA
rs446536295 211 I>T No EVA
rs432025498 215 C>G No EVA
rs432025498 215 C>R No EVA
rs445797450 216 L>V No EVA
rs469163751 218 E>A No EVA
rs454814914 220 S>C No EVA
rs437928155 220 S>T No EVA
rs433946280 223 S>A No EVA
rs454087515 223 S>L No EVA
rs471108280 225 A>S No EVA
rs441359515 225 A>V No EVA
rs463119754 226 A>G No EVA
rs476827222 227 S>Y No EVA
rs385135118 236 P>T No EVA
rs459929216 240 Y>* No EVA
rs446423912 240 Y>S No EVA
rs476918571 241 Y>* No EVA
rs445714074 242 T>S No EVA
rs469199829 243 L>I No EVA
rs437769951 243 L>P No EVA
rs448318824 244 N>T No EVA
rs433833637 246 S>R No EVA
rs468486091 246 S>T No EVA
rs454125996 247 K>M No EVA
rs454125996 247 K>T No EVA
rs470939082 249 W>* No EVA
rs470939082 249 W>C No EVA
rs433310755 251 S>I No EVA
rs478800657 251 S>R No EVA
rs447620492 254 G>C No EVA
rs478127840 257 D>A No EVA
rs470129284 259 F>V No EVA
rs435726919 264 K>T No EVA
rs466231735 275 V>G No EVA
rs434935762 279 I>S No EVA
rs451757218 280 T>A No EVA
rs482669970 291 V>I No EVA
rs476194947 292 T>A No EVA
rs476194947 292 T>P No EVA
rs465045156 322 V>G No EVA
rs436839645 326 V>G No EVA
rs473793068 344 M>R No EVA
rs442722958 357 A>S No EVA
rs444520035 380 Q>H No EVA
rs461429134 381 E>A No EVA
rs475067014 383 L>Q No EVA
rs876059662 386 M>L No EVA
rs460690451 392 V>G No EVA
rs477764122 394 E>K No EVA
rs462796909 398 Y>N No EVA
rs455660233 404 M>L No EVA
rs876481737 445 E>G No EVA
rs110602318 456 R>H No EVA
rs1115819442 476 G>S No EVA
rs450083455 510 R>G No EVA
rs455747523 520 S>R No EVA
rs472711333 521 L>P No EVA
rs435039191 530 S>R No EVA
rs453732315 532 S>G No EVA
rs432791349 542 Q>K No EVA
rs476307060 555 K>M No EVA
rs441698889 556 K>N No EVA
rs441130989 559 I>F No EVA
rs469812138 562 Q>R No EVA
rs451438564 569 A>V No EVA
rs471606377 571 S>R No EVA
rs437088386 572 A>S No EVA
rs473866764 574 D>A No EVA
rs473866764 574 D>V No EVA
rs442798585 575 L>P No EVA
rs517384761 576 Y>* No EVA
rs459696578 576 Y>F No EVA
rs438877806 577 A>G No EVA
rs473501295 577 A>P No EVA
rs459127616 578 M>L No EVA
rs482392982 579 V>G No EVA
rs451085950 580 V>G No EVA
rs461664333 581 V>L No EVA
rs465772125 583 S>A No EVA
rs455175797 585 A>G No EVA
rs475181096 586 S>A No EVA
rs440728407 589 L>V No EVA
rs799670500 590 S>N No EVA
rs460863877 590 S>R No EVA
rs477725321 593 H>Q No EVA
rs458332993 595 T>R No EVA
rs481765210 597 Q>R No EVA
rs450494966 600 K>Q No EVA
rs467429509 601 M>R No EVA
rs481244528 602 L>I No EVA
rs466894137 604 D>E No EVA
rs432233663 605 S>T No EVA
rs452521245 608 I>V No EVA
rs469373461 609 E>Q No EVA
rs460742709 615 R>W No EVA
rs876175395 616 E>G No EVA
rs440090554 620 A>P No EVA
rs477232385 625 P>L No EVA
rs460384456 625 P>T No EVA
rs445830869 629 E>D No EVA
rs482865927 641 L>P No EVA
rs468532331 642 V>A No EVA
rs468532331 642 V>G No EVA
rs434115956 643 E>G No EVA
rs447666948 644 R>G No EVA
rs456545473 647 V>G No EVA
rs435843084 648 V>G No EVA
rs476718258 648 V>I No EVA
rs474589901 655 F>V No EVA

No associated diseases with P48818

5 regional properties for P48818

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 103 - 209 IPR013786

Functions

Description
EC Number 1.3.8.9 With a flavin as acceptor
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
extrinsic component of mitochondrial inner membrane The component of mitochondrial inner membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
mitochondrial nucleoid The region of a mitochondrion to which the DNA is confined.
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.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

6 GO annotations of molecular function

Name Definition
acyl-CoA dehydrogenase activity Catalysis of the reaction: acyl-CoA + oxidized
fatty-acyl-CoA binding Binding to a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group.
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.
identical protein binding Binding to an identical protein or proteins.
long-chain-acyl-CoA dehydrogenase activity Catalysis of the reaction: a long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized = a long-chain (2E)-enoyl-CoA + reduced
very-long-chain-acyl-CoA dehydrogenase activity Catalysis of the reaction: a very-long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized = a very-long-chain (2E)-enoyl-CoA + reduced

7 GO annotations of biological process

Name Definition
epithelial cell differentiation The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium.
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).
negative regulation of fatty acid biosynthetic process Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of fatty acids.
negative regulation of fatty acid oxidation Any process that stops, prevents, or reduces the frequency, rate or extent of fatty acid oxidation.
regulation of cholesterol metabolic process Any process that modulates the rate, frequency, or extent of cholesterol metabolism, the chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
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.
temperature homeostasis A homeostatic process in which an organism modulates its internal body temperature.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3ZBF6 ACADS Short-chain specific acyl-CoA dehydrogenase, mitochondrial Bos taurus (Bovine) PR
P49748 ACADVL Very long-chain specific acyl-CoA dehydrogenase, mitochondrial Homo sapiens (Human) PR
P50544 Acadvl Very long-chain specific acyl-CoA dehydrogenase, mitochondrial Mus musculus (Mouse) PR
P45953 Acadvl Very long-chain specific acyl-CoA dehydrogenase, mitochondrial Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MRAARMAQST GRQLLRLRGV SSWPGELLGQ PRPGPARRPY ASGVAQAAVD QSDSQPSEAS
70 80 90 100 110 120
TREKRANSVS KSFAVGTFKG QLTTDQVFPY PSVLNEDQTQ FLKELVGPVT RFFEEVNDAA
130 140 150 160 170 180
KNDMLERVEE TTMQGLKELG AFGLQVPNEL GGVGLCNTQY ARLVEIVGMY DLGVGIVLGA
190 200 210 220 230 240
HQSIGFKGIL LFGTKAQKEK YLPKLASGET IAAFCLTEPS SGSDAASIRS SAVPSPCGKY
250 260 270 280 290 300
YTLNGSKIWI SNGGLADIFT VFAKTPVTDT ATGAVKEKIT AFVVERSFGG VTHGPPEKKM
310 320 330 340 350 360
GIKASNTAEV YFDGVRVPAE NVLGEVGGGF KVAMHILNNG RFGMAAALAG TMKGIIAKAV
370 380 390 400 410 420
DHAANRTQFG EKIHNFGLIQ EKLARMAMLQ YVTESMAYMV SANMDQGSTD FQIEAAISKI
430 440 450 460 470 480
FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDLRIFRI FEGTNDILRL FVALQGCMDK
490 500 510 520 530 540
GKELSGLGNA LKNPFGNAGL LLGEAGKQLR RRAGLGSGLS LSGIVHQELS RSGELAVQAL
550 560 570 580 590 600
EQFATVVEAK LIKHKKDIIN EQFLLQRLAD SAIDLYAMVV VLSRASRSLS EGHPTAQHEK
610 620 630 640 650
MLCDSWCIEA AARIRENMTA LQSDPQQQEL FRNFKSISKA LVERGGVVTS NPLGF