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Q80WC9

- ACSF4_MOUSE

UniProt

Q80WC9 - ACSF4_MOUSE

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Protein

Acyl-CoA synthetase family member 4

Gene
Aasdh, Acsf4, U26
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei427 – 4271ATP By similarity
Binding sitei441 – 4411ATP By similarity
Binding sitei526 – 5261ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi197 – 2059ATP By similarity

GO - Molecular functioni

  1. acid-thiol ligase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. L-aminoadipate-semialdehyde dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. fatty acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, NAD, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Aasdh
Synonyms:Acsf4, U26
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2442517. Aasdh.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11001100Acyl-CoA synthetase family member 4PRO_0000315804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei591 – 5911O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residuei651 – 6511Phosphoserine By similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEiQ80WC9.

PTM databases

PhosphoSiteiQ80WC9.

Expressioni

Inductioni

According to 1 Publication, it is up-regulated by lysine-rich diet, while according to 1 Publication levels of expression are not significantly changed even when diets differed markedly in PQQ and lysine content.2 Publications

Gene expression databases

BgeeiQ80WC9.
CleanExiMM_AASDH.
GenevestigatoriQ80WC9.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000113792.

Structurei

3D structure databases

ProteinModelPortaliQ80WC9.
SMRiQ80WC9. Positions 150-606, 754-1091.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini554 – 62875Acyl carrierAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1520.
GeneTreeiENSGT00440000033811.
HOGENOMiHOG000033793.
HOVERGENiHBG057704.
InParanoidiQ80WC9.
KOiK00142.
OMAiTMRATGD.
OrthoDBiEOG77T14J.
PhylomeDBiQ80WC9.
TreeFamiTF314245.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
2.140.10.10. 1 hit.
InterProiIPR009081. 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]
PfamiPF00501. AMP-binding. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
SMARTiSM00564. PQQ. 6 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50998. SSF50998. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q80WC9-1) [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

MTLQELVLRT ASVYMDRTAV CFDEGNNQPP VCYSYKALLS AASELSHFLI     50
AHCDFGGIRE IGLYCQPGIN LPSWILGILQ VPAAYAPIDP DSPPSLSTYF 100
MKKCDLKYVL VEKQQLSKFK SSHETVLNYD TVSVEHKDLA LFRLHWEDGR 150
VSTVLGDRAD QHKVTDREDR VSAESRTPEK EHMDMRHDGC LAYVLHTSGT 200
TGTPKIVRVP HACILPNIQH FRSLFDITQE DILFLASPLT FDPSVVEIFV 250
SLSSGACLLI VPTSVKVLPS KLADILFSRH RVTVLQATPT LLRRFGSELI 300
KSTVLSAHTS LRVLALGGEA FPSLTILKSW RGKGNRTQIF NIYGITEVSS 350
WATFYRIPEE ILNSAVKHES PVQLGSPLLG TVIEVRDQNG SPVLEGTGQV 400
FLGGKNRVCF LDDEMTVPLG TMRATGDFVT VKDGEIFFLG RKDSQIKRHG 450
KRLNIALVQQ VAEELRQVES CAVTWYNQER LILFIVSKVD LVKDCIFKEL 500
QKHLPAHALP DDMVLIDTLP FTCHGKVDVS ELNKIYLDYI SSQPRNELHG 550
KEELWGKLQY LWKSILCLPE DPEDTLKVPA NSVFLDSGGD SLKSMRLLSE 600
IERLTGTAIP GLLEVILSSS LLDVYNHIVQ AVFTPEDRKA NRSYTTKRKF 650
SDADPEEASG KPARLESAWP SNHAGETNSV IALSRGSQVL SLGAGRLLTQ 700
LGLCLPVCSL DLIPQTNTQI LKSLSPPAPD ENLEKPPLFQ QGSPVVGAMA 750
MALRERWRSD TGKCVDASPL LVRAAVQDKP STTVYIGSHS HTVKAVDLSS 800
GETRWEQLLG DRIESSACVS KCGNFIVVGC YNGLVYVLKS NSGEKYWTFT 850
TEDAVKSSPA VDPTTGLIYV GSHDQHAYAL DIYEKKCVWK LNCEGALFSS 900
PCVSLSPHHL YCATLGGLLL ALNPASGSTV WKRSCGKPLF SSPRCYQQYI 950
CIGCVDGSLL CFTHSGEQVW RFAAGGPIFS SPCVSAAEQE IFFGSHDCFI 1000
YCCSKEGHLR WKFETTARVY ATPFAFSNHP RSDDALLAAA STDGKLWVLE 1050
SRSGELRSVY ELPGEVFSSP VVWESMLVIG CRNNYIYCLD LLCGDKNNQV 1100
Length:1,100
Mass (Da):121,569
Last modified:June 1, 2003 - v1
Checksum:i86B303CFF07B234C
GO
Isoform 2 (identifier: Q80WC9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     368-1100: Missing.

Note: No experimental confirmation available.

Show »
Length:367
Mass (Da):40,964
Checksum:i19368BB77FDDF580
GO
Isoform 3 (identifier: Q80WC9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     223-1100: Missing.

Note: No experimental confirmation available.

Show »
Length:222
Mass (Da):25,031
Checksum:i2850F469893CD77F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei223 – 1100878Missing in isoform 3. VSP_030714Add
BLAST
Alternative sequencei368 – 1100733Missing in isoform 2. VSP_030715Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS19366.1. [Q80WC9-1]
RefSeqiNP_776126.1. NM_173765.3. [Q80WC9-1]
XP_006534916.1. XM_006534853.1. [Q80WC9-1]
UniGeneiMm.39271.

Genome annotation databases

EnsembliENSMUST00000069709; ENSMUSP00000069279; ENSMUSG00000055923. [Q80WC9-1]
ENSMUST00000120963; ENSMUSP00000113792; ENSMUSG00000055923. [Q80WC9-1]
ENSMUST00000146570; ENSMUSP00000117639; ENSMUSG00000055923.
GeneIDi231326.
KEGGimmu:231326.
UCSCiuc008xvi.2. mouse. [Q80WC9-1]
uc008xvk.2. mouse. [Q80WC9-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS19366.1. [Q80WC9-1 ]
RefSeqi NP_776126.1. NM_173765.3. [Q80WC9-1 ]
XP_006534916.1. XM_006534853.1. [Q80WC9-1 ]
UniGenei Mm.39271.

3D structure databases

ProteinModelPortali Q80WC9.
SMRi Q80WC9. Positions 150-606, 754-1091.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000113792.

PTM databases

PhosphoSitei Q80WC9.

Proteomic databases

PRIDEi Q80WC9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000069709 ; ENSMUSP00000069279 ; ENSMUSG00000055923 . [Q80WC9-1 ]
ENSMUST00000120963 ; ENSMUSP00000113792 ; ENSMUSG00000055923 . [Q80WC9-1 ]
ENSMUST00000146570 ; ENSMUSP00000117639 ; ENSMUSG00000055923 .
GeneIDi 231326.
KEGGi mmu:231326.
UCSCi uc008xvi.2. mouse. [Q80WC9-1 ]
uc008xvk.2. mouse. [Q80WC9-3 ]

Organism-specific databases

CTDi 132949.
MGIi MGI:2442517. Aasdh.

Phylogenomic databases

eggNOGi COG1520.
GeneTreei ENSGT00440000033811.
HOGENOMi HOG000033793.
HOVERGENi HBG057704.
InParanoidi Q80WC9.
KOi K00142.
OMAi TMRATGD.
OrthoDBi EOG77T14J.
PhylomeDBi Q80WC9.
TreeFami TF314245.

Miscellaneous databases

ChiTaRSi AASDH. mouse.
NextBioi 380501.
PROi Q80WC9.
SOURCEi Search...

Gene expression databases

Bgeei Q80WC9.
CleanExi MM_AASDH.
Genevestigatori Q80WC9.

Family and domain databases

Gene3Di 1.10.1200.10. 1 hit.
2.140.10.10. 1 hit.
InterProi IPR009081. 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 ]
Pfami PF00501. AMP-binding. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view ]
SMARTi SM00564. PQQ. 6 hits.
[Graphical view ]
SUPFAMi SSF47336. SSF47336. 1 hit.
SSF50998. SSF50998. 1 hit.
PROSITEi PS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiACSF4_MOUSE
AccessioniPrimary (citable) accession number: Q80WC9
Secondary accession number(s): Q3V3L2, Q505K4, Q8BRP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 96 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

External Data

Dasty 3

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