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Protein

Carbonyl reductase family member 4

Gene

Cbr4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The heteroteramer with HSD17B8 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity. May play a role in biosynthesis of fatty acids in mitochondria. The homotetramer may act as NADPH-dependent quinone reductase. Has broad substrate specificity and reduces 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and p-quinones (in vitro) (By similarity).By similarity

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei134 – 1341SubstrateBy similarity
Active sitei147 – 1471Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 3125NAD or NADPBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonyl reductase family member 4 (EC:1.-.-.-)
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.-)
Quinone reductase CBR4
Gene namesi
Name:Cbr4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2384567. Cbr4.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236Carbonyl reductase family member 4PRO_0000319879Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei40 – 401N6-acetyllysineCombined sources
Modified residuei96 – 961N6-acetyllysineCombined sources
Modified residuei194 – 1941N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ91VT4.
MaxQBiQ91VT4.
PaxDbiQ91VT4.
PRIDEiQ91VT4.

PTM databases

iPTMnetiQ91VT4.

Expressioni

Gene expression databases

BgeeiQ91VT4.
CleanExiMM_CBR4.
ExpressionAtlasiQ91VT4. baseline and differential.
GenevisibleiQ91VT4. MM.

Interactioni

Subunit structurei

Homotetramer. Heterotetramer with HSD17B8; contains two molecules of HSD17B8 and CBR4 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ91VT4. 2 interactions.
MINTiMINT-4121071.
STRINGi10090.ENSMUSP00000034058.

Structurei

3D structure databases

ProteinModelPortaliQ91VT4.
SMRiQ91VT4. Positions 1-236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1200. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG002145.
InParanoidiQ91VT4.
KOiK11539.
OMAiHIAYNTT.
OrthoDBiEOG70KGQM.
PhylomeDBiQ91VT4.
TreeFamiTF354265.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91VT4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKVCAVFGG SRGIGRAVAQ LMAQKGYRLA IVSRNLEVAK VTAGELGGNH
60 70 80 90 100
LAFRCDVAKE QDVQSTFQEM EKHLGPVNFL VNAAGINRDS LLVRTKTEDM
110 120 130 140 150
ISQLHTNLLG SMLTCKAAMK TMIQQGGSIV NVGSIIGLKG NVGQSAYSAT
160 170 180 190 200
KGGLVGFSRS LAKEVARKKI RVNVVAPGFI RTDMTRHLKE EHFKKNIPLG
210 220 230
RFGETLEVAH AVVFLLESPY ITGHVLIVDG GLQLTV
Length:236
Mass (Da):25,415
Last modified:February 26, 2008 - v2
Checksum:i546F400177DDC7F1
GO

Sequence cautioni

The sequence BAC31519.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891D → G in AAH09118 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK043313 mRNA. Translation: BAC31519.1. Different initiation.
AK150763 mRNA. Translation: BAE29830.1.
BC009118 mRNA. Translation: AAH09118.1.
CCDSiCCDS40349.1.
RefSeqiNP_663570.2. NM_145595.2.
UniGeneiMm.29059.

Genome annotation databases

EnsembliENSMUST00000034058; ENSMUSP00000034058; ENSMUSG00000031641.
GeneIDi234309.
KEGGimmu:234309.
UCSCiuc009lub.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK043313 mRNA. Translation: BAC31519.1. Different initiation.
AK150763 mRNA. Translation: BAE29830.1.
BC009118 mRNA. Translation: AAH09118.1.
CCDSiCCDS40349.1.
RefSeqiNP_663570.2. NM_145595.2.
UniGeneiMm.29059.

3D structure databases

ProteinModelPortaliQ91VT4.
SMRiQ91VT4. Positions 1-236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91VT4. 2 interactions.
MINTiMINT-4121071.
STRINGi10090.ENSMUSP00000034058.

PTM databases

iPTMnetiQ91VT4.

Proteomic databases

EPDiQ91VT4.
MaxQBiQ91VT4.
PaxDbiQ91VT4.
PRIDEiQ91VT4.

Protocols and materials databases

DNASUi234309.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034058; ENSMUSP00000034058; ENSMUSG00000031641.
GeneIDi234309.
KEGGimmu:234309.
UCSCiuc009lub.2. mouse.

Organism-specific databases

CTDi84869.
MGIiMGI:2384567. Cbr4.

Phylogenomic databases

eggNOGiKOG1200. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG002145.
InParanoidiQ91VT4.
KOiK11539.
OMAiHIAYNTT.
OrthoDBiEOG70KGQM.
PhylomeDBiQ91VT4.
TreeFamiTF354265.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

PROiQ91VT4.
SOURCEiSearch...

Gene expression databases

BgeeiQ91VT4.
CleanExiMM_CBR4.
ExpressionAtlasiQ91VT4. baseline and differential.
GenevisibleiQ91VT4. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 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].
    Strain: C57BL/6J.
    Tissue: Bone marrow macrophage and Cerebellum.
  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].
    Strain: 129.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "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-40; LYS-96 AND LYS-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCBR4_MOUSE
AccessioniPrimary (citable) accession number: Q91VT4
Secondary accession number(s): Q3UBY4, Q8BXV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: June 8, 2016
This is version 107 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.