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Protein

Acyl-CoA synthetase short-chain family member 3, mitochondrial

Gene

Acss3

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

Functioni

Activates acetate so that it can be used for lipid synthesis or for energy generation.By similarity

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei534 – 5341ATPBy similarity
Binding sitei549 – 5491ATPBy similarity
Binding sitei560 – 5601ATPBy similarity
Binding sitei619 – 6191Coenzyme ABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi420 – 4223ATPBy similarity
Nucleotide bindingi441 – 4466ATPBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA synthetase short-chain family member 3, mitochondrial (EC:6.2.1.1)
Gene namesi
Name:Acss3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2685720. Acss3.

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 – 2929MitochondrionSequence analysisAdd
BLAST
Chaini30 – 682653Acyl-CoA synthetase short-chain family member 3, mitochondrialPRO_0000320625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei513 – 5131N6-succinyllysineCombined sources
Modified residuei519 – 5191N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ14DH7.
PaxDbiQ14DH7.
PRIDEiQ14DH7.

PTM databases

iPTMnetiQ14DH7.
PhosphoSiteiQ14DH7.

Expressioni

Gene expression databases

BgeeiQ14DH7.
CleanExiMM_ACSS3.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000128209.

Structurei

3D structure databases

ProteinModelPortaliQ14DH7.
SMRiQ14DH7. Positions 56-680.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni222 – 2254Coenzyme A bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00820000127056.
HOGENOMiHOG000229981.
HOVERGENiHBG014401.
InParanoidiQ14DH7.
KOiK01908.
OMAiLPVKHGS.
OrthoDBiEOG7XDBFC.
PhylomeDBiQ14DH7.
TreeFamiTF354241.

Family and domain databases

InterProiIPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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: Q14DH7-1) [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
MKPSWLQCRK VTGAGTLGAP LPGSPSVRGA AVTRRALVAG FGGRGCRALT
60 70 80 90 100
TGSGGEYKTH FAASVADPER FWGKAAEQIS WYKPWTKTLE SRYPPSTSWF
110 120 130 140 150
VEGMLNICYN AIDRHIENGQ GDKIAIIYDS PVTDTKATIS YKEVLEQVSK
160 170 180 190 200
LAGVLVKQGV KKGDTVVIYM PMIPQAIYTM LACARIGAIH SLIFGGFASK
210 220 230 240 250
ELSTRIDHAK PKVVVTASFG IEPGRKVEYI PLLEEALRIG QHRPDRVLIY
260 270 280 290 300
SRPNMEKVPL MSGRDLDWEE EMAKAQSHDC VPVLSEHPLY ILYTSGTTGL
310 320 330 340 350
PKGVVRPTGG YAVMLNWTMS SIYGLKPGEV WWAASDLGWV VGHSYICYGP
360 370 380 390 400
LLHGNTTVLY EGKPVGTPDA GAYFRVLAEH GVAALFTAPT AIRAIRQQDP
410 420 430 440 450
GAALGKQYSL TRFKTLFVAG ERCDVETLEW SKKVFRVPVL DHWWQTETGS
460 470 480 490 500
PITASCIGLG NSKTPPPGQA GKCVPGYNVM ILDDNMQKLK ARSLGNIVVK
510 520 530 540 550
LPLPPGAFSG LWKNQEAFKH LYFEKFPGYY DTMDAGYMDE EGYLYVMSRV
560 570 580 590 600
DDVINVAGHR ISAGAIEESV LSHGTVADCA VVGKEDPLKG HVPLALCVLK
610 620 630 640 650
KDVNASEEQV LEEIVKHVRQ SIGPVAAFRN AVFVKQLPKT RSGKIPRSTL
660 670 680
SALVNGKPYK VTPTIEDPSI FGHIEEVLKQ AV
Length:682
Mass (Da):74,518
Last modified:February 26, 2008 - v2
Checksum:iB865D534C631D5D1
GO
Isoform 2 (identifier: Q14DH7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     479-479: V → GRYLLHHSAESLTPPAMGK
     480-682: Missing.

Show »
Length:497
Mass (Da):54,137
Checksum:i129841385217FAF1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti477 – 4771Y → N in BAC28254 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei479 – 4791V → GRYLLHHSAESLTPPAMGK in isoform 2. 2 PublicationsVSP_031693
Alternative sequencei480 – 682203Missing in isoform 2. 2 PublicationsVSP_031694Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033376 mRNA. Translation: BAC28254.1.
AC111014 Genomic DNA. No translation available.
AC121946 Genomic DNA. No translation available.
AC134457 Genomic DNA. No translation available.
BC113198 mRNA. Translation: AAI13199.1.
CCDSiCCDS24159.1. [Q14DH7-2]
CCDS48688.1. [Q14DH7-1]
RefSeqiNP_001136276.1. NM_001142804.1. [Q14DH7-1]
NP_941038.2. NM_198636.3. [Q14DH7-2]
UniGeneiMm.336072.

Genome annotation databases

EnsembliENSMUST00000044668; ENSMUSP00000040823; ENSMUSG00000035948. [Q14DH7-2]
ENSMUST00000165067; ENSMUSP00000128209; ENSMUSG00000035948. [Q14DH7-1]
GeneIDi380660.
KEGGimmu:380660.
UCSCiuc007gyv.2. mouse. [Q14DH7-2]
uc011xna.1. mouse. [Q14DH7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033376 mRNA. Translation: BAC28254.1.
AC111014 Genomic DNA. No translation available.
AC121946 Genomic DNA. No translation available.
AC134457 Genomic DNA. No translation available.
BC113198 mRNA. Translation: AAI13199.1.
CCDSiCCDS24159.1. [Q14DH7-2]
CCDS48688.1. [Q14DH7-1]
RefSeqiNP_001136276.1. NM_001142804.1. [Q14DH7-1]
NP_941038.2. NM_198636.3. [Q14DH7-2]
UniGeneiMm.336072.

3D structure databases

ProteinModelPortaliQ14DH7.
SMRiQ14DH7. Positions 56-680.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000128209.

PTM databases

iPTMnetiQ14DH7.
PhosphoSiteiQ14DH7.

Proteomic databases

MaxQBiQ14DH7.
PaxDbiQ14DH7.
PRIDEiQ14DH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044668; ENSMUSP00000040823; ENSMUSG00000035948. [Q14DH7-2]
ENSMUST00000165067; ENSMUSP00000128209; ENSMUSG00000035948. [Q14DH7-1]
GeneIDi380660.
KEGGimmu:380660.
UCSCiuc007gyv.2. mouse. [Q14DH7-2]
uc011xna.1. mouse. [Q14DH7-1]

Organism-specific databases

CTDi79611.
MGIiMGI:2685720. Acss3.

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00820000127056.
HOGENOMiHOG000229981.
HOVERGENiHBG014401.
InParanoidiQ14DH7.
KOiK01908.
OMAiLPVKHGS.
OrthoDBiEOG7XDBFC.
PhylomeDBiQ14DH7.
TreeFamiTF354241.

Miscellaneous databases

PROiQ14DH7.
SOURCEiSearch...

Gene expression databases

BgeeiQ14DH7.
CleanExiMM_ACSS3.

Family and domain databases

InterProiIPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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: Lung.
  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] (ISOFORM 2).
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver and Lung.
  5. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "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-519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACSS3_MOUSE
AccessioniPrimary (citable) accession number: Q14DH7
Secondary accession number(s): Q8BZX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: June 8, 2016
This is version 82 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.