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Protein

Acyl-CoA synthetase family member 2, mitochondrial

Gene

Acsf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei493 – 4931ATPBy similarity
Binding sitei508 – 5081ATPBy similarity
Binding sitei599 – 5991ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi263 – 2719ATPBy similarity

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-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2388287. Acsf2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141MitochondrionSequence analysisAdd
BLAST
Chaini42 – 615574Acyl-CoA synthetase family member 2, mitochondrialPRO_0000315795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791N6-acetyllysineCombined sources
Modified residuei182 – 1821N6-acetyllysine; alternateCombined sources
Modified residuei182 – 1821N6-succinyllysine; alternateCombined sources
Modified residuei199 – 1991N6-acetyllysineCombined sources
Modified residuei340 – 3401N6-acetyllysineCombined sources
Modified residuei398 – 3981N6-acetyllysineCombined sources
Modified residuei478 – 4781N6-succinyllysineCombined sources
Modified residuei510 – 5101N6-acetyllysineCombined sources
Modified residuei544 – 5441N6-acetyllysine; alternateCombined sources
Modified residuei544 – 5441N6-succinyllysine; alternateCombined sources
Modified residuei570 – 5701N6-acetyllysine; alternateCombined sources
Modified residuei570 – 5701N6-succinyllysine; alternateCombined sources
Modified residuei599 – 5991N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8VCW8.
MaxQBiQ8VCW8.
PaxDbiQ8VCW8.
PRIDEiQ8VCW8.

PTM databases

iPTMnetiQ8VCW8.
PhosphoSiteiQ8VCW8.
SwissPalmiQ8VCW8.

Expressioni

Gene expression databases

BgeeiQ8VCW8.
CleanExiMM_ACSF2.
GenevisibleiQ8VCW8. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8VCW8. 3 interactions.
MINTiMINT-1860401.
STRINGi10090.ENSMUSP00000099453.

Structurei

3D structure databases

ProteinModelPortaliQ8VCW8.
SMRiQ8VCW8. Positions 102-609.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1177. Eukaryota.
COG0318. LUCA.
GeneTreeiENSGT00760000119304.
HOGENOMiHOG000229999.
HOVERGENiHBG103408.
InParanoidiQ8VCW8.
KOiK00666.
OMAiERERCTC.
OrthoDBiEOG7JMGD3.
PhylomeDBiQ8VCW8.
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.

Q8VCW8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVYHGMLRF GRLCIASLGA RGPRTLLSRP RPNSKLQSVR ALSSGMVNCT
60 70 80 90 100
NPLPIGGLSY IQGHTDSHLV NTTVGECLDA TAQRFPDREA LVILHENIRL
110 120 130 140 150
NFAQLKEEVD KAASGLLSIG LRKGDRLGMW GPNSYAWVLI QLATAQAGII
160 170 180 190 200
LVSVNPAYQS SELEYVLRKV GCKGIVFPKQ FKTQQYYDIL KQVCPELEKA
210 220 230 240 250
QPGALKSERL PDLTTVISVD APLPGTLLLD DIVAAGGKEQ NLAQLRYNQR
260 270 280 290 300
FLSCYDPINI QFTSGTTGNP KGATLSHHNI VNNSMLIGQR LKMPTKTAEE
310 320 330 340 350
LRLVLPSPLY HCLGSVGGTM VSMMHGATLL LSSPSFNGKK ALEAISREKG
360 370 380 390 400
TLLYGTPTMF VDILNQPDFS SYDFTSIRGG VIAGSPAPPE LIRAIINKMN
410 420 430 440 450
MKELVVVYGT TENSPVTFMN FPEDTLEQKA GSVGRIMPHT EAQIVNVETG
460 470 480 490 500
ELTNLNVPGE LYIRGYCVMQ GYWGEPQKTF ETVGQDKWYR TGDIALMDEQ
510 520 530 540 550
GFCKIVGRSK DMIIRGGENI YPAELEDFFL KHPQVQEAQV VGVKDERMGE
560 570 580 590 600
EICACIRLKS GETTTAEEIK AFCKGKISHF KIPRYIVFVE GYPLTISGKI
610
QKFKLREQME QHLKL
Length:615
Mass (Da):67,951
Last modified:March 1, 2002 - v1
Checksum:i84AF2B6FA13D91A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761V → L in BAE32109 (PubMed:19468303).Curated
Sequence conflicti200 – 2001A → G in BAE32109 (PubMed:19468303).Curated
Sequence conflicti231 – 2311D → Y in BAE32109 (PubMed:19468303).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034209 mRNA. Translation: BAC28632.1.
AK153582 mRNA. Translation: BAE32109.1.
AK169987 mRNA. Translation: BAE41499.1.
AL645764, AL645809 Genomic DNA. Translation: CAI24962.1.
AL645809, AL645764 Genomic DNA. Translation: CAI25585.1.
BC018371 mRNA. Translation: AAH18371.1.
BC063269 mRNA. Translation: AAH63269.1.
CCDSiCCDS25259.1.
RefSeqiNP_722502.1. NM_153807.2.
UniGeneiMm.386885.

Genome annotation databases

EnsembliENSMUST00000103164; ENSMUSP00000099453; ENSMUSG00000076435.
GeneIDi264895.
KEGGimmu:264895.
UCSCiuc007kzc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034209 mRNA. Translation: BAC28632.1.
AK153582 mRNA. Translation: BAE32109.1.
AK169987 mRNA. Translation: BAE41499.1.
AL645764, AL645809 Genomic DNA. Translation: CAI24962.1.
AL645809, AL645764 Genomic DNA. Translation: CAI25585.1.
BC018371 mRNA. Translation: AAH18371.1.
BC063269 mRNA. Translation: AAH63269.1.
CCDSiCCDS25259.1.
RefSeqiNP_722502.1. NM_153807.2.
UniGeneiMm.386885.

3D structure databases

ProteinModelPortaliQ8VCW8.
SMRiQ8VCW8. Positions 102-609.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VCW8. 3 interactions.
MINTiMINT-1860401.
STRINGi10090.ENSMUSP00000099453.

PTM databases

iPTMnetiQ8VCW8.
PhosphoSiteiQ8VCW8.
SwissPalmiQ8VCW8.

Proteomic databases

EPDiQ8VCW8.
MaxQBiQ8VCW8.
PaxDbiQ8VCW8.
PRIDEiQ8VCW8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103164; ENSMUSP00000099453; ENSMUSG00000076435.
GeneIDi264895.
KEGGimmu:264895.
UCSCiuc007kzc.1. mouse.

Organism-specific databases

CTDi80221.
MGIiMGI:2388287. Acsf2.

Phylogenomic databases

eggNOGiKOG1177. Eukaryota.
COG0318. LUCA.
GeneTreeiENSGT00760000119304.
HOGENOMiHOG000229999.
HOVERGENiHBG103408.
InParanoidiQ8VCW8.
KOiK00666.
OMAiERERCTC.
OrthoDBiEOG7JMGD3.
PhylomeDBiQ8VCW8.
TreeFamiTF313466.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiAcsf2. mouse.
PROiQ8VCW8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VCW8.
CleanExiMM_ACSF2.
GenevisibleiQ8VCW8. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Diencephalon and Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  4. "Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome."
    Watkins P.A., Maiguel D., Jia Z., Pevsner J.
    J. Lipid Res. 48:2736-2750(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-182, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-182; LYS-478; LYS-544; LYS-570 AND LYS-599, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-182; LYS-199; LYS-340; LYS-398; LYS-510; LYS-544 AND LYS-570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACSF2_MOUSE
AccessioniPrimary (citable) accession number: Q8VCW8
Secondary accession number(s): Q3TDU9, Q3U5G9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 124 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.