Search Results

Overview

Uniprot IDP28288
Protein NameATP-binding cassette sub-family D member 3
Gene NameABCD3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
289 YNGNKREKQTVHSVF
298 TVHSVFRKLVEHLHN
347 LSHPRHLKSTHSELL
399 TELMQVLKDLNHGKY
405 LKDLNHGKYERTMVS
6 **MAAFSKYLTARNS

Function

Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long-chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-chain fatty acids-CoA and bile acids from the cytosol to the peroxisome lumen for beta-oxydation (PubMed:11248239, PubMed:24333844, PubMed:25168382, PubMed:29397936). Has fatty acyl-CoA thioesterase and ATPase activities (PubMed:29397936). Probably hydrolyzes fatty acyl-CoAs into free fatty acids prior to their ATP-dependent transport into peroxisomes (By similarity). Thus, play a role in regulation of LCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation (PubMed:24333844, PubMed:25944712)

Protein Sequence

10 MAAFSKYLTA 20 RNSSLAGAAF 30 LLLCLLHKRR 40 RALGLHGKKS 50 GKPPLQNNEK 60 EGKKERAVVD 70 KVFFSRLIQI 80 LKIMVPRTFC 90 KETGYLVLIA 100 VMLVSRTYCD 110 VWMIQNGTLI 120 ESGIIGRSRK 130 DFKRYLLNFI 140 AAMPLISLVN 150 NFLKYGLNEL 160 KLCFRVRLTK 170 YLYEEYLQAF 180 TYYKMGNLDN 190 RIANPDQLLT 200 QDVEKFCNSV 210 VDLYSNLSKP 220 FLDIVLYIFK 230 LTSAIGAQGP 240 ASMMAYLVVS 250 GLFLTRLRRP 260 IGKMTITEQK 270 YEGEYRYVNS 280 RLITNSEEIA 290 FYNGNKREKQ 300 TVHSVFRKLV 310 EHLHNFILFR 320 FSMGFIDSII 330 AKYLATVVGY 340 LVVSRPFLDL 350 SHPRHLKSTH 360 SELLEDYYQS 370 GRMLLRMSQA 380 LGRIVLAGRE 390 MTRLAGFTAR 400 ITELMQVLKD 410 LNHGKYERTM 420 VSQQEKGIEG 430 VQVIPLIPGA 440 GEIIIADNII 450 KFDHVPLATP 460 NGDVLIRDLN 470 FEVRSGANVL 480 ICGPNGCGKS 490 SLFRVLGELW 500 PLFGGRLTKP 510 ERGKLFYVPQ 520 RPYMTLGTLR 530 DQVIYPDGRE 540 DQKRKGISDL 550 VLKEYLDNVQ 560 LGHILEREGG 570 WDSVQDWMDV 580 LSGGEKQRMA 590 MARLFYHKPQ 600 FAILDECTSA 610 VSVDVEGYIY 620 SHCRKVGITL 630 FTVSHRKSLW 640 KHHEYYLHMD 650 GRGNYEFKQI TEDTVEFGS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016020 membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005782 peroxisomal matrix
Cellular Component GO:0005778 peroxisomal membrane
Cellular Component GO:0005777 peroxisome
Molecular Function GO:0140359 ABC-type transporter activity
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0042626 ATPase-coupled transmembrane transporter activity
Molecular Function GO:0047617 fatty acyl-CoA hydrolase activity
Molecular Function GO:0005324 long-chain fatty acid transmembrane transporter activity
Molecular Function GO:0042803 protein homodimerization activity
Biological Process GO:0015721 bile acid and bile salt transport
Biological Process GO:0006699 bile acid biosynthetic process
Biological Process GO:0006635 fatty acid beta-oxidation
Biological Process GO:0006633 fatty acid biosynthetic process
Biological Process GO:0015910 long-chain fatty acid import into peroxisome
Biological Process GO:0007031 peroxisome organization
Biological Process GO:1903512 phytanic acid metabolic process
Biological Process GO:0009410 response to xenobiotic stimulus
Biological Process GO:0042760 very long-chain fatty acid catabolic process
Biological Process GO:0000038 very long-chain fatty acid metabolic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.