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Protein

Acyl-CoA synthetase family member 2, mitochondrial

Gene

Acsf2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei493ATPBy similarity1
Binding sitei508ATPBy similarity1
Binding sitei599ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi263 – 271ATPBy similarity9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-75105. Fatty Acyl-CoA Biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA synthetase family member 2, mitochondrial (EC:6.2.1.-)
Gene namesi
Name:Acsf2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1562656. Acsf2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 49MitochondrionSequence analysisAdd BLAST49
ChainiPRO_000031579750 – 615Acyl-CoA synthetase family member 2, mitochondrialAdd BLAST566

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei179N6-acetyllysineBy similarity1
Modified residuei182N6-acetyllysine; alternateBy similarity1
Modified residuei182N6-succinyllysine; alternateBy similarity1
Modified residuei199N6-acetyllysineBy similarity1
Modified residuei340N6-acetyllysineBy similarity1
Modified residuei398N6-acetyllysineBy similarity1
Modified residuei478N6-succinyllysineBy similarity1
Modified residuei510N6-acetyllysineBy similarity1
Modified residuei544N6-acetyllysine; alternateBy similarity1
Modified residuei544N6-succinyllysine; alternateBy similarity1
Modified residuei570N6-acetyllysine; alternateBy similarity1
Modified residuei570N6-succinyllysine; alternateBy similarity1
Modified residuei599N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ499N5.
PRIDEiQ499N5.

PTM databases

iPTMnetiQ499N5.
PhosphoSitePlusiQ499N5.

Expressioni

Gene expression databases

BgeeiENSRNOG00000003330.
GenevisibleiQ499N5. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004673.

Structurei

3D structure databases

ProteinModelPortaliQ499N5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1177. Eukaryota.
COG0318. LUCA.
GeneTreeiENSGT00760000119304.
HOGENOMiHOG000229999.
HOVERGENiHBG103408.
InParanoidiQ499N5.
KOiK00666.
OMAiMYSIPEI.
OrthoDBiEOG091G0XVH.
PhylomeDBiQ499N5.
TreeFamiTF313466.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q499N5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVYLGMLRL GRLCVASLGA RGPRTPLSRP WPNSKLQGVR AFSSGMVDCT
60 70 80 90 100
NPLPIGGLSY IQGHTDSHLV NKTVGECLDA TAQRFPNREA LVIIHENIRL
110 120 130 140 150
NFAQLKEEVD RAASGLLSIG LRKGDRLGMW GPNSYAWVLI QLATAQAGII
160 170 180 190 200
LVSVNPAYQA SELEYVLRKV GCKGIVFPKQ FKTQQYYNIL KQVCPELEKA
210 220 230 240 250
QPGALKSERL PDLTTVISVD APLPGTLLLD EVVAAGGKEQ NLAQLRYHQG
260 270 280 290 300
FLSCYDPINI QFTSGTTGNP KGATLSHHNI VNNSNLIGQR LKMPAKTAEE
310 320 330 340 350
LRMVLPCPLY HCLGSVGGTM VSVVHGATLL LSSPSFNGKK ALEAISREKG
360 370 380 390 400
TLLYGTPTMF VDILNQPDFS SYDFTTIRGG VIAGSLAPPE LIRAIISKMN
410 420 430 440 450
MKELVVVYGT TENSPVTFMN FPEDTLEQKA GSVGRIMPHT EAQIVNMETG
460 470 480 490 500
ELTKLNMPGE LCIRGYCVMQ GYWGEPQKTF ETVGQDRWYR TGDIASMDEQ
510 520 530 540 550
GFCRIVGRSK DMIIRGGENI YPAELEDFFH KHPQVQEAQV VGVKDDRMGE
560 570 580 590 600
EICACIRLKS GETTTEEEIK AFCKGKISHF KIPRYIVFVE GYPLTVSGKI
610
QKFKLREQME QHLKL
Length:615
Mass (Da):67,886
Last modified:September 13, 2005 - v1
Checksum:i96F95B2186C01348
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC099826 mRNA. Translation: AAH99826.1.
RefSeqiNP_001030123.1. NM_001034951.1.
UniGeneiRn.146366.

Genome annotation databases

EnsembliENSRNOT00000004673; ENSRNOP00000004673; ENSRNOG00000003330.
GeneIDi619561.
KEGGirno:619561.
UCSCiRGD:1562656. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC099826 mRNA. Translation: AAH99826.1.
RefSeqiNP_001030123.1. NM_001034951.1.
UniGeneiRn.146366.

3D structure databases

ProteinModelPortaliQ499N5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004673.

PTM databases

iPTMnetiQ499N5.
PhosphoSitePlusiQ499N5.

Proteomic databases

PaxDbiQ499N5.
PRIDEiQ499N5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004673; ENSRNOP00000004673; ENSRNOG00000003330.
GeneIDi619561.
KEGGirno:619561.
UCSCiRGD:1562656. rat.

Organism-specific databases

CTDi80221.
RGDi1562656. Acsf2.

Phylogenomic databases

eggNOGiKOG1177. Eukaryota.
COG0318. LUCA.
GeneTreeiENSGT00760000119304.
HOGENOMiHOG000229999.
HOVERGENiHBG103408.
InParanoidiQ499N5.
KOiK00666.
OMAiMYSIPEI.
OrthoDBiEOG091G0XVH.
PhylomeDBiQ499N5.
TreeFamiTF313466.

Enzyme and pathway databases

ReactomeiR-RNO-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

PROiQ499N5.

Gene expression databases

BgeeiENSRNOG00000003330.
GenevisibleiQ499N5. RN.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiACSF2_RAT
AccessioniPrimary (citable) accession number: Q499N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 13, 2005
Last modified: November 2, 2016
This is version 75 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.