CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013703
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain fatty acid transport protein 3 
Protein Synonyms/Alias
 FATP-3; Fatty acid transport protein 3; Solute carrier family 27 member 3; Very long-chain acyl-CoA synthetase homolog 3; VLCS-3 
Gene Name
 SLC27A3 
Gene Synonyms/Alias
 ACSVL3; FATP3; PSEC0067; UNQ367/PRO703 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
436LVNQPPSKAERGHKVubiquitination[1, 2]
682LATTETFKQQKVRMAubiquitination[3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 Has acyl-CoA ligase activity for long-chain and very- long-chain fatty acids. Does not exhibit fatty acid transport activity (By similarity). 
Sequence Annotation
 NP_BIND 332 343 AMP (Potential).  
Keyword
 Alternative splicing; Complete proteome; Fatty acid metabolism; Ligase; Lipid metabolism; Membrane; Mitochondrion; Nucleotide-binding; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 730 AA 
Protein Sequence
MGVCQRTRAP WKEKSQLERA ALGFRKGGSG MFASGWNQTV PIEEAGSMAA LLLLPLLLLL 60
PLLLLKLHLW PQLRWLPADL AFAVRALCCK RALRARALAA AAADPEGPEG GCSLAWRLAE 120
LAQQRAAHTF LIHGSRRFSY SEAERESNRA ARAFLRALGW DWGPDGGDSG EGSAGEGERA 180
APGAGDAAAG SGAEFAGGDG AARGGGAAAP LSPGATVALL LPAGPEFLWL WFGLAKAGLR 240
TAFVPTALRR GPLLHCLRSC GARALVLAPE FLESLEPDLP ALRAMGLHLW AAGPGTHPAG 300
ISDLLAEVSA EVDGPVPGYL SSPQSITDTC LYIFTSGTTG LPKAARISHL KILQCQGFYQ 360
LCGVHQEDVI YLALPLYHMS GSLLGIVGCM GIGATVVLKS KFSAGQFWED CQQHRVTVFQ 420
YIGELCRYLV NQPPSKAERG HKVRLAVGSG LRPDTWERFV RRFGPLQVLE TYGLTEGNVA 480
TINYTGQRGA VGRASWLYKH IFPFSLIRYD VTTGEPIRDP QGHCMATSPG EPGLLVAPVS 540
QQSPFLGYAG GPELAQGKLL KDVFRPGDVF FNTGDLLVCD DQGFLRFHDR TGDTFRWKGE 600
NVATTEVAEV FEALDFLQEV NVYGVTVPGH EGRAGMAALV LRPPHALDLM QLYTHVSENL 660
PPYARPRFLR LQESLATTET FKQQKVRMAN EGFDPSTLSD PLYVLDQAVG AYLPLTTARY 720
SALLAGNLRI 730 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
 GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:Compara.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS