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Protein

Acyl-CoA synthetase family member 3, mitochondrial

Gene

Acsf3

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

Functioni

Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei455 – 4551ATPBy similarity
Binding sitei469 – 4691ATPBy similarity
Binding sitei561 – 5611ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi202 – 2109ATPBy 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-75876. Synthesis of very long-chain fatty acyl-CoAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA synthetase family member 3, mitochondrial (EC:6.2.1.-)
Gene namesi
Name:Acsf3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2182591. Acsf3.

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 – 2727MitochondrionSequence analysisAdd
BLAST
Chaini28 – 583556Acyl-CoA synthetase family member 3, mitochondrialPRO_0000315801Add
BLAST

Proteomic databases

EPDiQ3URE1.
MaxQBiQ3URE1.
PaxDbiQ3URE1.
PRIDEiQ3URE1.

PTM databases

iPTMnetiQ3URE1.
PhosphoSiteiQ3URE1.

Expressioni

Gene expression databases

BgeeiQ3URE1.
CleanExiMM_ACSF3.
GenevisibleiQ3URE1. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000015160.

Structurei

3D structure databases

ProteinModelPortaliQ3URE1.
SMRiQ3URE1. Positions 52-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1176. Eukaryota.
COG0318. LUCA.
GeneTreeiENSGT00760000119304.
HOGENOMiHOG000229983.
HOVERGENiHBG100430.
InParanoidiQ3URE1.
KOiK18660.
OMAiVGFPLPT.
OrthoDBiEOG7W9RVK.
PhylomeDBiQ3URE1.
TreeFamiTF312995.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3URE1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPPHLALPFR RLFWSLASSQ LIPRRHRGHS LLPTTPEAHT DGSVPVFIRA
60 70 80 90 100
LAFGDRIALI DKYGHHTYRE LYDRSLCLAQ EICRLQGCKV GDLQEERVSF
110 120 130 140 150
LCSNDVSYVV AQWASWMSGG VAVPLYWKHP EAQLEYFIQD SRSSLVVVGQ
160 170 180 190 200
EYLERLSPLA QRLGVPLLPL TPAVYHGATE KPTEQPVEES GWRDRGAMIF
210 220 230 240 250
YTSGTTGRPK GALSTHRNLA AVVTGLVHSW AWTKNDVILH VLPLHHVHGV
260 270 280 290 300
VNKLLCPLWV GATCVMLPEF SAQQVWEKFL SSEAPQITVF MAVPTVYSKL
310 320 330 340 350
LDYYDKHFTQ PHVQDFVRAV CKERIRLMVS GSAALPVPLL EKWRSATGHT
360 370 380 390 400
LLERYGMTEI GMALSNPLTE ARVPGSVGTP LPGVEVRIIS ENPQKGSPYI
410 420 430 440 450
IHAEGNERGT KVTPGFEEKE GELLVRGPSV FREYWDKPEE TKSAFTSDGW
460 470 480 490 500
FRTGDTAVFK DARYWIRGRT SVDIIKTGGY KVSALEIERH LLAHPSITDV
510 520 530 540 550
AVIGVPDMTW GQRVTAVVAL QEGHSLSHGD LKEWARGVLA PYAVPSELLL
560 570 580
VEEIPRNQMG KVNKKELLKQ LYPSGQRSQP GQG
Length:583
Mass (Da):65,077
Last modified:January 15, 2008 - v2
Checksum:iBA1D80C18F91D27D
GO
Isoform 2 (identifier: Q3URE1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     327-367: LMVSGSAALP...TEIGMALSNP → FCGDPIARSG...REGDKGEVIV
     368-583: Missing.

Note: No experimental confirmation available.
Show »
Length:367
Mass (Da):41,362
Checksum:i1EF29DCA3A6D66F8
GO

Sequence cautioni

The sequence AAH22709.3 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei327 – 36741LMVSG…ALSNP → FCGDPIARSGSTHHLRKPAE GFPLHHPCRGKREGDKGEVI V in isoform 2. 1 PublicationVSP_030705Add
BLAST
Alternative sequencei368 – 583216Missing in isoform 2. 1 PublicationVSP_030706Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK141579 mRNA. Translation: BAE24747.1.
BC022709 mRNA. Translation: AAH22709.3. Different initiation.
CCDSiCCDS40505.1. [Q3URE1-1]
RefSeqiNP_659181.2. NM_144932.3. [Q3URE1-1]
XP_006531093.1. XM_006531030.1. [Q3URE1-1]
XP_006531094.1. XM_006531031.1. [Q3URE1-1]
XP_006531095.1. XM_006531032.1. [Q3URE1-1]
UniGeneiMm.334875.

Genome annotation databases

EnsembliENSMUST00000015160; ENSMUSP00000015160; ENSMUSG00000015016. [Q3URE1-1]
GeneIDi257633.
KEGGimmu:257633.
UCSCiuc009ntr.1. mouse. [Q3URE1-2]
uc009nts.1. mouse. [Q3URE1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK141579 mRNA. Translation: BAE24747.1.
BC022709 mRNA. Translation: AAH22709.3. Different initiation.
CCDSiCCDS40505.1. [Q3URE1-1]
RefSeqiNP_659181.2. NM_144932.3. [Q3URE1-1]
XP_006531093.1. XM_006531030.1. [Q3URE1-1]
XP_006531094.1. XM_006531031.1. [Q3URE1-1]
XP_006531095.1. XM_006531032.1. [Q3URE1-1]
UniGeneiMm.334875.

3D structure databases

ProteinModelPortaliQ3URE1.
SMRiQ3URE1. Positions 52-572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000015160.

PTM databases

iPTMnetiQ3URE1.
PhosphoSiteiQ3URE1.

Proteomic databases

EPDiQ3URE1.
MaxQBiQ3URE1.
PaxDbiQ3URE1.
PRIDEiQ3URE1.

Protocols and materials databases

DNASUi257633.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015160; ENSMUSP00000015160; ENSMUSG00000015016. [Q3URE1-1]
GeneIDi257633.
KEGGimmu:257633.
UCSCiuc009ntr.1. mouse. [Q3URE1-2]
uc009nts.1. mouse. [Q3URE1-1]

Organism-specific databases

CTDi197322.
MGIiMGI:2182591. Acsf3.

Phylogenomic databases

eggNOGiKOG1176. Eukaryota.
COG0318. LUCA.
GeneTreeiENSGT00760000119304.
HOGENOMiHOG000229983.
HOVERGENiHBG100430.
InParanoidiQ3URE1.
KOiK18660.
OMAiVGFPLPT.
OrthoDBiEOG7W9RVK.
PhylomeDBiQ3URE1.
TreeFamiTF312995.

Enzyme and pathway databases

ReactomeiR-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

ChiTaRSiAcsf3. mouse.
PROiQ3URE1.
SOURCEiSearch...

Gene expression databases

BgeeiQ3URE1.
CleanExiMM_ACSF3.
GenevisibleiQ3URE1. 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

  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] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Hippocampus.
  2. "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] OF 193-583 (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver and Spleen.

Entry informationi

Entry nameiACSF3_MOUSE
AccessioniPrimary (citable) accession number: Q3URE1
Secondary accession number(s): Q78IW2, Q8VC75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: June 8, 2016
This is version 86 of the entry and version 2 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.