CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008951
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-binding cassette sub-family D member 3 
Protein Synonyms/Alias
 68 kDa peroxisomal membrane protein; PMP68; 70 kDa peroxisomal membrane protein; PMP70 
Gene Name
 Abcd3 
Gene Synonyms/Alias
 Pmp70; Pxmp1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
39ALGLHGKKSGKPPLQubiquitination[1]
42LHGKKSGKPPLQNNEacetylation[2, 3]
61KERAVVDKVFLSRLSacetylation[2, 4, 5]
61KERAVVDKVFLSRLSubiquitination[1]
72SRLSQILKIMVPRTFubiquitination[1]
260KMTIMEQKYEGEYRYacetylation[2, 3, 5, 6, 7]
260KMTIMEQKYEGEYRYubiquitination[1]
286IAFYNGNKREKQTIHacetylation[3]
286IAFYNGNKREKQTIHubiquitination[1]
289YNGNKREKQTIHSVFacetylation[3]
399TELMQVLKDLNHGRYacetylation[2, 5]
399TELMQVLKDLNHGRYubiquitination[1]
416TMVSQQEKGIEGAQAubiquitination[1]
479CGPNGCGKSSLFRVLubiquitination[1]
529QVIYPDGKEDQKKRGacetylation[2, 3, 5, 7]
529QVIYPDGKEDQKKRGubiquitination[1]
533PDGKEDQKKRGISDQacetylation[2, 3, 5]
534DGKEDQKKRGISDQVubiquitination[1]
543GISDQVLKEYLDNVQacetylation[3]
543GISDQVLKEYLDNVQubiquitination[1]
576DVLSGGEKQRMAMARubiquitination[1]
615YIYSHCRKVGITLFTubiquitination[1]
648GRGNYEFKKITEDTVacetylation[3, 5]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [5] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [6] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [7] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 
Functional Description
  
Sequence Annotation
 DOMAIN 85 372 ABC transmembrane type-1.
 DOMAIN 434 659 ABC transporter.
 NP_BIND 473 480 ATP (Potential).
 REGION 2 199 Interaction with PEX19 (By similarity).
 REGION 2 124 Targeting to peroxisomes (By similarity).
 MOD_RES 260 260 N6-acetyllysine.
 MOD_RES 399 399 N6-acetyllysine (By similarity).
 MOD_RES 424 424 Phosphoserine.
 CARBOHYD 12 12 N-linked (GlcNAc...) (Potential).
 CARBOHYD 106 106 N-linked (GlcNAc...) (Potential).
 CARBOHYD 206 206 N-linked (GlcNAc...) (Potential).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Glycoprotein; Membrane; Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 659 AA 
Protein Sequence
MAAFSKYLTA RNTSLAGAAF LLLCLLHKRR RALGLHGKKS GKPPLQNNEK EGKKERAVVD 60
KVFLSRLSQI LKIMVPRTFC KETGYLLLIA VMLVSRTYCD VWMIQNGTLI ESGIIGRSSK 120
DFKRYLFNFI AAMPLISLVN NFLKYGLNEL KLCFRVRLTR YLYEEYLQAF TYYKMGNLDN 180
RIANPDQLLT QDVEKFCNSV VDLYSNLSKP FLDIVLYIFK LTSAIGAQGP ASMMAYLLVS 240
GLFLTRLRRP IGKMTIMEQK YEGEYRYVNS RLITNSEEIA FYNGNKREKQ TIHSVFRKLV 300
EHLHNFIFFR FSMGFIDSII AKYVATVVGY LVVSRPFLDL AHPRHLHSTH SELLEDYYQS 360
GRMLLRMSQA LGRIVLAGRE MTRLAGFTAR ITELMQVLKD LNHGRYERTM VSQQEKGIEG 420
AQASPLVPGA GEIINTDNII KFDHVPLATP NGDILIQDLS FEVRSGANVL ICGPNGCGKS 480
SLFRVLGELW PLFGGRLTKP ERGKLFYVPQ RPYMTLGTLR DQVIYPDGKE DQKKRGISDQ 540
VLKEYLDNVQ LGHILEREGG WDSVQDWMDV LSGGEKQRMA MARLFYHKPQ FAILDECTSA 600
VSVDVEDYIY SHCRKVGITL FTVSHRKSLW KHHEYYLHMD GRGNYEFKKI TEDTVEFGS 659 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005782; C:peroxisomal matrix; IEA:Compara.
 GO:0005778; C:peroxisomal membrane; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
 GO:0006635; P:fatty acid beta-oxidation; IEA:Compara.
 GO:0007031; P:peroxisome organization; IEA:Compara.
 GO:0042760; P:very long-chain fatty acid catabolic process; IEA:Compara. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR010509; ABC_Ald_N.
 IPR003439; ABC_transporter-like.
 IPR017871; ABC_transporter_CS.
 IPR017940; ABC_transporter_type1.
 IPR011527; ABC_transptrTM_dom_typ1.
 IPR005283; FA_transporter.
 IPR027417; P-loop_NTPase. 
Pfam
 PF06472; ABC_membrane_2
 PF00005; ABC_tran 
SMART
 SM00382; AAA 
PROSITE
 PS50929; ABC_TM1F
 PS00211; ABC_TRANSPORTER_1
 PS50893; ABC_TRANSPORTER_2 
PRINTS