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Protein

Acyl-CoA synthetase family member 3, mitochondrial

Gene

ACSF3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei457 – 4571ATPBy similarity
Binding sitei471 – 4711ATPBy similarity
Binding sitei563 – 5631ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi202 – 2109ATPBy similarity

GO - Molecular functioni

  1. acid-thiol ligase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. malonyl-CoA synthetase activity Source: UniProtKB

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB
  2. fatty acid metabolic process Source: UniProtKB
  3. malonate catabolic 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:
Acyl-CoA synthetase family member 3, mitochondrial (EC:6.2.1.-)
Gene namesi
Name:ACSF3
ORF Names:PSEC0197
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:27288. ACSF3.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Combined malonic and methylmalonic aciduria1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA metabolic disease characterized by malonic and methylmalonic aciduria, with urinary excretion of much larger amounts of methylmalonic acid than malonic acid, in the presence of normal malonyl-CoA decarboxylase activity. Clinical features include coma, ketoacidosis, hypoglycemia, failure to thrive, microcephaly, dystonia, axial hypotonia and/or developmental delay, and neurologic manifestations including seizures, psychiatric disease and/or cognitive decline.

See also OMIM:614265
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti198 – 1981M → R in CMAMMA. 1 Publication
VAR_066504
Natural varianti243 – 2431P → L in CMAMMA. 1 Publication
Corresponds to variant rs140986055 [ dbSNP | Ensembl ].
VAR_066505
Natural varianti358 – 3581T → I in CMAMMA. 1 Publication
VAR_066506
Natural varianti359 – 3591E → K in CMAMMA. 1 Publication
Corresponds to variant rs150487794 [ dbSNP | Ensembl ].
VAR_066507
Natural varianti462 – 4621K → T in CMAMMA. 1 Publication
VAR_066508
Natural varianti465 – 4706Missing in CMAMMA. 1 Publication
VAR_066509
Natural varianti471 – 4711R → Q in CMAMMA. 1 Publication
VAR_066510
Natural varianti471 – 4711R → W in CMAMMA. 1 Publication
Corresponds to variant rs138680796 [ dbSNP | Ensembl ].
VAR_066511
Natural varianti480 – 4801G → S in CMAMMA. 1 Publication
VAR_066512
Natural varianti558 – 5581R → W in CMAMMA. 1 Publication
Corresponds to variant rs141090143 [ dbSNP | Ensembl ].
VAR_066513

Organism-specific databases

MIMi614265. phenotype.
Orphaneti289504. Combined malonic and methylmalonic acidemia.
PharmGKBiPA162375375.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8383MitochondrionSequence AnalysisAdd
BLAST
Chaini84 – 576493Acyl-CoA synthetase family member 3, mitochondrialPRO_0000315800Add
BLAST

Proteomic databases

MaxQBiQ4G176.
PaxDbiQ4G176.
PRIDEiQ4G176.

PTM databases

PhosphoSiteiQ4G176.

Expressioni

Gene expression databases

BgeeiQ4G176.
CleanExiHS_ACSF3.
ExpressionAtlasiQ4G176. baseline and differential.
GenevestigatoriQ4G176.

Organism-specific databases

HPAiHPA008322.
HPA008323.

Interactioni

Protein-protein interaction databases

BioGridi128248. 9 interactions.
STRINGi9606.ENSP00000320646.

Structurei

3D structure databases

ProteinModelPortaliQ4G176.
SMRiQ4G176. Positions 49-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0318.
GeneTreeiENSGT00760000119304.
HOGENOMiHOG000229983.
HOVERGENiHBG100430.
InParanoidiQ4G176.
KOiK18660.
OMAiWAWSKDD.
OrthoDBiEOG7W9RVK.
PhylomeDBiQ4G176.
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]

Sequencei

Sequence statusi: Complete.

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

Q4G176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPHVVLTFR RLGCALASCR LAPARHRGSG LLHTAPVARS DRSAPVFTRA
60 70 80 90 100
LAFGDRIALV DQHGRHTYRE LYSRSLRLSQ EICRLCGCVG GDLREERVSF
110 120 130 140 150
LCANDASYVV AQWASWMSGG VAVPLYRKHP AAQLEYVICD SQSSVVLASQ
160 170 180 190 200
EYLELLSPVV RKLGVPLLPL TPAIYTGAVE EPAEVPVPEQ GWRNKGAMII
210 220 230 240 250
YTSGTTGRPK GVLSTHQNIR AVVTGLVHKW AWTKDDVILH VLPLHHVHGV
260 270 280 290 300
VNALLCPLWV GATCVMMPEF SPQQVWEKFL SSETPRINVF MAVPTIYTKL
310 320 330 340 350
MEYYDRHFTQ PHAQDFLRAV CEEKIRLMVS GSAALPLPVL EKWKNITGHT
360 370 380 390 400
LLERYGMTEI GMALSGPLTT AVRLPGSVGT PLPGVQVRIV SENPQREACS
410 420 430 440 450
YTIHAEGDER GTKVTPGFEE KEGELLVRGP SVFREYWNKP EETKSAFTLD
460 470 480 490 500
GWFKTGDTVV FKDGQYWIRG RTSVDIIKTG GYKVSALEVE WHLLAHPSIT
510 520 530 540 550
DVAVIGVPDM TWGQRVTAVV TLREGHSLSH RELKEWARNV LAPYAVPSEL
560 570
VLVEEIPRNQ MGKIDKKALI RHFHPS
Length:576
Mass (Da):64,130
Last modified:May 18, 2010 - v3
Checksum:i60F0D5020817EF70
GO

Sequence cautioni

The sequence AAH72391.1 differs from that shown.Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481A → V in AAH28399 (PubMed:15489334).Curated
Sequence conflicti278 – 2781K → E in BAC11654 (PubMed:16303743).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21L → P.1 Publication
Corresponds to variant rs7188200 [ dbSNP | Ensembl ].
VAR_038306
Natural varianti17 – 171A → P.1 Publication
Corresponds to variant rs11547019 [ dbSNP | Ensembl ].
VAR_038307
Natural varianti198 – 1981M → R in CMAMMA. 1 Publication
VAR_066504
Natural varianti243 – 2431P → L in CMAMMA. 1 Publication
Corresponds to variant rs140986055 [ dbSNP | Ensembl ].
VAR_066505
Natural varianti358 – 3581T → I in CMAMMA. 1 Publication
VAR_066506
Natural varianti359 – 3591E → K in CMAMMA. 1 Publication
Corresponds to variant rs150487794 [ dbSNP | Ensembl ].
VAR_066507
Natural varianti372 – 3721V → M.1 Publication
Corresponds to variant rs3743979 [ dbSNP | Ensembl ].
VAR_038308
Natural varianti462 – 4621K → T in CMAMMA. 1 Publication
VAR_066508
Natural varianti465 – 4706Missing in CMAMMA. 1 Publication
VAR_066509
Natural varianti471 – 4711R → Q in CMAMMA. 1 Publication
VAR_066510
Natural varianti471 – 4711R → W in CMAMMA. 1 Publication
Corresponds to variant rs138680796 [ dbSNP | Ensembl ].
VAR_066511
Natural varianti480 – 4801G → S in CMAMMA. 1 Publication
VAR_066512
Natural varianti558 – 5581R → W in CMAMMA. 1 Publication
Corresponds to variant rs141090143 [ dbSNP | Ensembl ].
VAR_066513

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075499 mRNA. Translation: BAC11654.1.
AK290963 mRNA. Translation: BAF83652.1.
AC009113 Genomic DNA. No translation available.
AC135782 Genomic DNA. No translation available.
CH471184 Genomic DNA. Translation: EAW66744.1.
BC028399 mRNA. Translation: AAH28399.1.
BC072391 mRNA. Translation: AAH72391.1. Sequence problems.
CCDSiCCDS10974.1.
RefSeqiNP_001120686.1. NM_001127214.3.
NP_001230208.1. NM_001243279.2.
NP_777577.2. NM_174917.4.
UniGeneiHs.461727.
Hs.720526.

Genome annotation databases

EnsembliENST00000317447; ENSP00000320646; ENSG00000176715.
ENST00000406948; ENSP00000384627; ENSG00000176715.
ENST00000614302; ENSP00000479130; ENSG00000176715.
GeneIDi197322.
KEGGihsa:197322.
UCSCiuc002fmp.3. human.

Polymorphism databases

DMDMi296439438.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075499 mRNA. Translation: BAC11654.1.
AK290963 mRNA. Translation: BAF83652.1.
AC009113 Genomic DNA. No translation available.
AC135782 Genomic DNA. No translation available.
CH471184 Genomic DNA. Translation: EAW66744.1.
BC028399 mRNA. Translation: AAH28399.1.
BC072391 mRNA. Translation: AAH72391.1. Sequence problems.
CCDSiCCDS10974.1.
RefSeqiNP_001120686.1. NM_001127214.3.
NP_001230208.1. NM_001243279.2.
NP_777577.2. NM_174917.4.
UniGeneiHs.461727.
Hs.720526.

3D structure databases

ProteinModelPortaliQ4G176.
SMRiQ4G176. Positions 49-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128248. 9 interactions.
STRINGi9606.ENSP00000320646.

PTM databases

PhosphoSiteiQ4G176.

Polymorphism databases

DMDMi296439438.

Proteomic databases

MaxQBiQ4G176.
PaxDbiQ4G176.
PRIDEiQ4G176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317447; ENSP00000320646; ENSG00000176715.
ENST00000406948; ENSP00000384627; ENSG00000176715.
ENST00000614302; ENSP00000479130; ENSG00000176715.
GeneIDi197322.
KEGGihsa:197322.
UCSCiuc002fmp.3. human.

Organism-specific databases

CTDi197322.
GeneCardsiGC16P089160.
H-InvDBHIX0013347.
HGNCiHGNC:27288. ACSF3.
HPAiHPA008322.
HPA008323.
MIMi614245. gene.
614265. phenotype.
neXtProtiNX_Q4G176.
Orphaneti289504. Combined malonic and methylmalonic acidemia.
PharmGKBiPA162375375.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0318.
GeneTreeiENSGT00760000119304.
HOGENOMiHOG000229983.
HOVERGENiHBG100430.
InParanoidiQ4G176.
KOiK18660.
OMAiWAWSKDD.
OrthoDBiEOG7W9RVK.
PhylomeDBiQ4G176.
TreeFamiTF312995.

Miscellaneous databases

GeneWikiiACSF3.
GenomeRNAii197322.
NextBioi89644.
PROiQ4G176.
SOURCEiSearch...

Gene expression databases

BgeeiQ4G176.
CleanExiHS_ACSF3.
ExpressionAtlasiQ4G176. baseline and differential.
GenevestigatoriQ4G176.

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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANTS PRO-2; PRO-17 AND MET-372.
    Tissue: Brain.
  6. "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.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: VARIANTS CMAMMA ARG-198; LEU-243; ILE-358; LYS-359; THR-462; 465-GLN--GLY-470 DEL; GLN-471; TRP-471; SER-480 AND TRP-558, FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiACSF3_HUMAN
AccessioniPrimary (citable) accession number: Q4G176
Secondary accession number(s): A8K4J8
, C9JQL6, Q6INA0, Q8N2F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 18, 2010
Last modified: March 4, 2015
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.