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P97524

- S27A2_RAT

UniProt

P97524 - S27A2_RAT

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Protein

Very long-chain acyl-CoA synthetase

Gene

Slc27a2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes (By similarity).By similarity

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.
ATP + a very-long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi222 – 23312AMPSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: UniProtKB
  3. very long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  1. long-chain fatty acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Very long-chain acyl-CoA synthetase (EC:6.2.1.-)
Short name:
VLACS
Short name:
VLCS
Alternative name(s):
Fatty acid transport protein 2
Short name:
FATP-2
Fatty-acid-coenzyme A ligase, very long-chain 1
Long-chain-fatty-acid--CoA ligase (EC:6.2.1.3)
Solute carrier family 27 member 2
THCA-CoA ligase
Very long-chain-fatty-acid-CoA ligase
Gene namesi
Name:Slc27a2
Synonyms:Acsvl1, Facvl1, Fatp2, Vlacs, Vlcs
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi71103. Slc27a2.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Peroxisome membrane 1 Publication; Multi-pass membrane protein 1 Publication
Note: Peripheral membrane associated with the lumenal side of peroxisomes.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44LumenalBy similarity
Transmembranei5 – 2723HelicalSequence AnalysisAdd
BLAST
Topological domaini28 – 10679CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei107 – 12721HelicalSequence AnalysisAdd
BLAST
Topological domaini128 – 267140LumenalSequence AnalysisAdd
BLAST
Transmembranei268 – 28821HelicalSequence AnalysisAdd
BLAST
Topological domaini289 – 620332CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB
  2. integral component of peroxisomal membrane Source: UniProtKB
  3. intracellular membrane-bounded organelle Source: RGD
  4. peroxisomal membrane Source: HGNC
  5. peroxisome Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Very long-chain acyl-CoA synthetasePRO_0000193206Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei291 – 2911N6-acetyllysineBy similarity
Modified residuei577 – 5771PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP97524.
PRIDEiP97524.

Expressioni

Gene expression databases

GenevestigatoriP97524.

Interactioni

Protein-protein interaction databases

BioGridi249304. 1 interaction.
STRINGi10116.ENSRNOP00000063336.

Structurei

3D structure databases

ProteinModelPortaliP97524.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0318.
HOGENOMiHOG000044189.
HOVERGENiHBG005642.
InParanoidiP97524.
KOiK08746.
PhylomeDBiP97524.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97524-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPVLYTGLA GLLLLPLLLT CCCPYLLQDV RFFLQLANMA RQVRSYRQRR
60 70 80 90 100
PVRTILHVFL EQARKTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDHLG
110 120 130 140 150
LRQGDCVALF MGNEPAYVWL WLGLLKLGCP MACLNYNIRA KSLLHCFQCC
160 170 180 190 200
GAKVLLASPE LHEAVEEVLP TLKKEGVSVF YVSRTSNTNG VDTVLDKVDG
210 220 230 240 250
VSADPIPESW RSEVTFTTPA VYIYTSGTTG LPKAATINHH RLWYGTSLAL
260 270 280 290 300
RSGIKAHDVI YTTMPLYHSA ALMIGLHGCI VVGATFALRS KFSASQFWDD
310 320 330 340 350
CRKYNATVIQ YIGELLRYLC NTPQKPNDRD HKVKIALGNG LRGDVWREFI
360 370 380 390 400
KRFGDIHIYE FYASTEGNIG FMNYPRKIGA VGRENYLQKK VVRHELIKYD
410 420 430 440 450
VEKDEPVRDA NGYCIKVPKG EVGLLICKIT ELTPFFGYAG GKTQTEKKKL
460 470 480 490 500
RDVFKKGDVY FNSGDLLMID RENFIYFHDR VGDTFRWKGE NVATTEVADI
510 520 530 540 550
VGLVDFVEEV NVYGVPVPGH EGRIGMASIK MKENYEFNGK KLFQHISEYL
560 570 580 590 600
PSYSRPRFLR IQDTIEITGT FKHRKVTLME EGFNPSVIKD TLYFMDDTEK
610 620
TYVPMTEDIY NAIIDKTLKL
Length:620
Mass (Da):70,694
Last modified:May 1, 1997 - v1
Checksum:i6CF9362DC3805526
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85100 mRNA. Translation: BAA12722.1.
RefSeqiNP_113924.1. NM_031736.1.
UniGeneiRn.3608.

Genome annotation databases

GeneIDi65192.
KEGGirno:65192.
UCSCiRGD:71103. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85100 mRNA. Translation: BAA12722.1 .
RefSeqi NP_113924.1. NM_031736.1.
UniGenei Rn.3608.

3D structure databases

ProteinModelPortali P97524.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249304. 1 interaction.
STRINGi 10116.ENSRNOP00000063336.

Proteomic databases

PaxDbi P97524.
PRIDEi P97524.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 65192.
KEGGi rno:65192.
UCSCi RGD:71103. rat.

Organism-specific databases

CTDi 11001.
RGDi 71103. Slc27a2.

Phylogenomic databases

eggNOGi COG0318.
HOGENOMi HOG000044189.
HOVERGENi HBG005642.
InParanoidi P97524.
KOi K08746.
PhylomeDBi P97524.

Miscellaneous databases

NextBioi 614116.

Gene expression databases

Genevestigatori P97524.

Family and domain databases

InterProi IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of cDNA encoding rat very long-chain acyl-CoA synthetase."
    Uchiyama A., Aoyama T., Kamijo K., Uchida Y., Kondo N., Orii T., Hashimoto T.
    J. Biol. Chem. 271:30360-30365(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Wistar.
    Tissue: Liver.
  2. "Intraperoxisomal localization of very-long-chain fatty acyl-CoA synthetase: implication in X-adrenoleukodystrophy."
    Smith B.T., Sengupta T.K., Singh I.
    Exp. Cell Res. 254:309-320(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiS27A2_RAT
AccessioniPrimary (citable) accession number: P97524
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3