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Q80WC9 (ACSF4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-CoA synthetase family member 4

EC=6.2.1.-
Alternative name(s):
2-aminoadipic 6-semialdehyde dehydrogenase
Protein LYS2 homolog
Putative aminoadipate-semialdehyde dehydrogenase
EC=1.2.1.31
Gene names
Name:Aasdh
Synonyms:Acsf4, U26
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1100 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA By similarity. Putative 2-aminoadipic 6-semialdehyde dehydrogenase, which may be involved in lysine catabolism. Ref.1

Catalytic activity

(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.

Induction

According to Ref.1, it is up-regulated by lysine-rich diet, while according to Ref.6 levels of expression are not significantly changed even when diets differed markedly in PQQ and lysine content. Ref.1 Ref.6

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Contains 1 acyl carrier domain.

Caution

According to Ref.1, it may bind pyrroloquinoline quinone (PQQ) cofactor. However, their conclusions are based on prediction tools and indirect results and are not confirmed by Ref.4 and Ref.5. The relevance of PQQ-binding is therefore unclear in vivo.

In invertebrates, aminoadipate-semialdehyde dehydrogenase reaction is a key step of the L-lysine biosynthesis pathway, which is not fully conserved in vertebrates. It has been suggested by Ref.1 that this protein participates in the reverse reaction (i.e. in lysine catabolism), however the relevance of this catalytic activity in vivo remains unclear.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80WC9-1)

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.
Isoform 2 (identifier: Q80WC9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     368-1100: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q80WC9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     223-1100: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11001100Acyl-CoA synthetase family member 4
PRO_0000315804

Regions

Domain554 – 62875Acyl carrier
Nucleotide binding197 – 2059ATP By similarity

Sites

Binding site4271ATP By similarity
Binding site4411ATP By similarity
Binding site5261ATP By similarity

Amino acid modifications

Modified residue5911O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residue6511Phosphoserine By similarity

Natural variations

Alternative sequence223 – 1100878Missing in isoform 3.
VSP_030714
Alternative sequence368 – 1100733Missing in isoform 2.
VSP_030715

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 86B303CFF07B234C

FASTA1,100121,569
        10         20         30         40         50         60 
MTLQELVLRT ASVYMDRTAV CFDEGNNQPP VCYSYKALLS AASELSHFLI AHCDFGGIRE 

        70         80         90        100        110        120 
IGLYCQPGIN LPSWILGILQ VPAAYAPIDP DSPPSLSTYF MKKCDLKYVL VEKQQLSKFK 

       130        140        150        160        170        180 
SSHETVLNYD TVSVEHKDLA LFRLHWEDGR VSTVLGDRAD QHKVTDREDR VSAESRTPEK 

       190        200        210        220        230        240 
EHMDMRHDGC LAYVLHTSGT TGTPKIVRVP HACILPNIQH FRSLFDITQE DILFLASPLT 

       250        260        270        280        290        300 
FDPSVVEIFV SLSSGACLLI VPTSVKVLPS KLADILFSRH RVTVLQATPT LLRRFGSELI 

       310        320        330        340        350        360 
KSTVLSAHTS LRVLALGGEA FPSLTILKSW RGKGNRTQIF NIYGITEVSS WATFYRIPEE 

       370        380        390        400        410        420 
ILNSAVKHES PVQLGSPLLG TVIEVRDQNG SPVLEGTGQV FLGGKNRVCF LDDEMTVPLG 

       430        440        450        460        470        480 
TMRATGDFVT VKDGEIFFLG RKDSQIKRHG KRLNIALVQQ VAEELRQVES CAVTWYNQER 

       490        500        510        520        530        540 
LILFIVSKVD LVKDCIFKEL QKHLPAHALP DDMVLIDTLP FTCHGKVDVS ELNKIYLDYI 

       550        560        570        580        590        600 
SSQPRNELHG KEELWGKLQY LWKSILCLPE DPEDTLKVPA NSVFLDSGGD SLKSMRLLSE 

       610        620        630        640        650        660 
IERLTGTAIP GLLEVILSSS LLDVYNHIVQ AVFTPEDRKA NRSYTTKRKF SDADPEEASG 

       670        680        690        700        710        720 
KPARLESAWP SNHAGETNSV IALSRGSQVL SLGAGRLLTQ LGLCLPVCSL DLIPQTNTQI 

       730        740        750        760        770        780 
LKSLSPPAPD ENLEKPPLFQ QGSPVVGAMA MALRERWRSD TGKCVDASPL LVRAAVQDKP 

       790        800        810        820        830        840 
STTVYIGSHS HTVKAVDLSS GETRWEQLLG DRIESSACVS KCGNFIVVGC YNGLVYVLKS 

       850        860        870        880        890        900 
NSGEKYWTFT TEDAVKSSPA VDPTTGLIYV GSHDQHAYAL DIYEKKCVWK LNCEGALFSS 

       910        920        930        940        950        960 
PCVSLSPHHL YCATLGGLLL ALNPASGSTV WKRSCGKPLF SSPRCYQQYI CIGCVDGSLL 

       970        980        990       1000       1010       1020 
CFTHSGEQVW RFAAGGPIFS SPCVSAAEQE IFFGSHDCFI YCCSKEGHLR WKFETTARVY 

      1030       1040       1050       1060       1070       1080 
ATPFAFSNHP RSDDALLAAA STDGKLWVLE SRSGELRSVY ELPGEVFSSP VVWESMLVIG 

      1090       1100 
CRNNYIYCLD LLCGDKNNQV 

« Hide

Isoform 2 [UniParc].

Checksum: 19368BB77FDDF580
Show »

FASTA36740,964
Isoform 3 [UniParc].

Checksum: 2850F469893CD77F
Show »

FASTA22225,031

References

« Hide 'large scale' references
[1]"Nutritional biochemistry: a new redox-cofactor vitamin for mammals."
Kasahara T., Kato T.
Nature 422:832-832(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POSSIBLE FUNCTION, INDUCTION.
[2]"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. expand/collapse author list , 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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-645 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Brain cortex and Hypothalamus.
[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] (ISOFORMS 1 AND 2).
Tissue: Olfactory epithelium.
[4]"Biochemistry: role of PQQ as a mammalian enzyme cofactor?"
Felton L.M., Anthony C.
Nature 433:E10-E10(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: COMMENT ON PUBMED:12712191 RESULTS.
[5]"Biochemistry: is pyrroloquinoline quinone a vitamin?"
Rucker R., Storms D., Sheets A., Tchaparian E., Fascetti A.
Nature 433:E10-E11(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: COMMENT ON PUBMED:12712191 RESULTS.
[6]"Pyrroloquinoline quinone nutritional status alters lysine metabolism and modulates mitochondrial DNA content in the mouse and rat."
Bauerly K.A., Storms D.H., Harris C.B., Hajizadeh S., Sun M.Y., Cheung C.P., Satre M.A., Fascetti A.J., Tchaparian E., Rucker R.B.
Biochim. Biophys. Acta 1760:1741-1748(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB095954 mRNA. Translation: BAC75954.1.
AK038779 mRNA. Translation: BAE43303.1.
AK043807 mRNA. Translation: BAC31660.1.
BC094507 mRNA. Translation: AAH94507.1.
BC128330 mRNA. Translation: AAI28331.1.
RefSeqNP_776126.1. NM_173765.3.
XP_006534916.1. XM_006534853.1.
UniGeneMm.39271.

3D structure databases

ProteinModelPortalQ80WC9.
SMRQ80WC9. Positions 1-606, 753-1091.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000113792.

PTM databases

PhosphoSiteQ80WC9.

Proteomic databases

PRIDEQ80WC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000069709; ENSMUSP00000069279; ENSMUSG00000055923. [Q80WC9-1]
ENSMUST00000120963; ENSMUSP00000113792; ENSMUSG00000055923. [Q80WC9-1]
ENSMUST00000146570; ENSMUSP00000117639; ENSMUSG00000055923.
GeneID231326.
KEGGmmu:231326.
UCSCuc008xvi.2. mouse. [Q80WC9-1]
uc008xvk.2. mouse. [Q80WC9-3]

Organism-specific databases

CTD132949.
MGIMGI:2442517. Aasdh.

Phylogenomic databases

eggNOGCOG1520.
GeneTreeENSGT00440000033811.
HOGENOMHOG000033793.
HOVERGENHBG057704.
InParanoidQ80WC9.
KOK00142.
OMATMRATGD.
OrthoDBEOG77T14J.
TreeFamTF314245.

Gene expression databases

ArrayExpressQ80WC9.
BgeeQ80WC9.
CleanExMM_AASDH.
GenevestigatorQ80WC9.

Family and domain databases

Gene3D1.10.1200.10. 1 hit.
2.140.10.10. 1 hit.
InterProIPR009081. Acyl_carrier_prot-like.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR006162. PPantetheine_attach_site.
IPR018391. PQQ_beta_propeller_repeat.
IPR027295. Quinonprotein_ADH-like_fam.
IPR011047. Quinonprotein_ADH-like_supfam.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
SMARTSM00564. PQQ. 6 hits.
[Graphical view]
SUPFAMSSF47336. SSF47336. 1 hit.
SSF50998. SSF50998. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAASDH. mouse.
NextBio380501.
PROQ80WC9.
SOURCESearch...

Entry information

Entry nameACSF4_MOUSE
AccessionPrimary (citable) accession number: Q80WC9
Secondary accession number(s): Q3V3L2, Q505K4, Q8BRP4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: March 19, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot