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P05063 (ALDOC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase C

EC=4.1.2.13
Alternative name(s):
Aldolase 3
Brain-type aldolase
Scrapie-responsive protein 2
Zebrin II
Gene names
Name:Aldoc
Synonyms:Aldo3, Scrg2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homotetramer. Interacts with ATP6V1E1 By similarity.

Tissue specificity

Expressed exclusively in Purkinje cells in bands running from anterior to posterior across most of the cerebellum. Expressed at higher levels in the brains of BSE-infected animals. Ref.1 Ref.6

Developmental stage

Expression begins in the first week of postnatal life. Ref.1

Miscellaneous

In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 363362Fructose-bisphosphate aldolase C
PRO_0000216949

Sites

Active site1881Proton acceptor By similarity
Active site2301Schiff-base intermediate with dihydroxyacetone-P
Binding site561Substrate
Binding site1471Substrate
Site3631Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue1111N6-acetyllysine By similarity

Experimental info

Sequence conflict251T → A in AAH04802. Ref.3
Sequence conflict251T → A in AAH08184. Ref.3
Sequence conflict461Q → E in BAC30300. Ref.2
Sequence conflict621V → A in CAA27422. Ref.4
Sequence conflict1131V → L in CAA27422. Ref.4
Sequence conflict2011R → H in AAH04802. Ref.3
Sequence conflict2011R → H in AAH08184. Ref.3
Sequence conflict2801A → V in AAB32064. Ref.1
Sequence conflict3581I → V in AAH04802. Ref.3
Sequence conflict3581I → V in AAH08184. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P05063 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 085C58AF163581C6

FASTA36339,395
        10         20         30         40         50         60 
MPHSYPALSA EQKKELSDIA LRIVTPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR 

        70         80         90        100        110        120 
QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGILVGIKVD KGVVPLAGTD 

       130        140        150        160        170        180 
GETTTQGLDG LLERCAQYKK DGADFAKWRC VLKISDRTPS ALAILENANV LARYASICQQ 

       190        200        210        220        230        240 
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC 

       250        260        270        280        290        300 
PIKYSPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC PLPRPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEMNGLAAQ GRYEGSGDGG AAAQSLYIAN 


HAY 

« Hide

References

« Hide 'large scale' references
[1]"The cloning of zebrin II reveals its identity with aldolase C."
Ahn A.H., Dziennis S., Hawkes R., Herrup K.
Development 120:2081-2090(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: C57BL/6J.
Tissue: Cerebellum.
[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].
Strain: C57BL/6J.
Tissue: Cerebellum and Spinal cord.
[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].
Tissue: Mammary gland.
[4]"Structure and expression of mouse aldolase genes. Brain-specific aldolase C amino acid sequence is closely related to aldolase A."
Paolella G., Buono P., Mancini P., Izzo P., Salvatore F.
Eur. J. Biochem. 156:229-235(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-227.
[5]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13; 29-57; 61-69; 73-96; 102-108; 112-134; 154-215; 244-258; 260-289; 305-315; 319-330 AND 332-363, MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[6]"Enhanced levels of scrapie responsive gene mRNA in BSE-infected mouse brain."
Dandoy-Dron F.C., Benboudjema L., Guillo F., Jaegly A., Jasmin C., Dormont D., Tovey M.G., Dron M.
Brain Res. Mol. Brain Res. 76:173-179(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-363, TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S72537 mRNA. Translation: AAB32064.1.
AK005077 mRNA. Translation: BAB23801.1.
AK039267 mRNA. Translation: BAC30300.1.
BC004802 mRNA. Translation: AAH04802.1.
BC008184 mRNA. Translation: AAH08184.1.
X03796 mRNA. Translation: CAA27422.1.
AJ132391 mRNA. Translation: CAB77178.1.
PIRADMSC. A25388.
I53145.
RefSeqNP_033787.2. NM_009657.3.
XP_006532096.1. XM_006532033.1.
UniGeneMm.7729.

3D structure databases

ProteinModelPortalP05063.
SMRP05063. Positions 3-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198068. 1 interaction.
IntActP05063. 6 interactions.
MINTMINT-1864918.

PTM databases

PhosphoSiteP05063.

2D gel databases

REPRODUCTION-2DPAGEIPI00119458.
UCD-2DPAGEP05063.

Proteomic databases

PaxDbP05063.
PRIDEP05063.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017534; ENSMUSP00000017534; ENSMUSG00000017390.
ENSMUST00000102478; ENSMUSP00000099536; ENSMUSG00000017390.
GeneID11676.
KEGGmmu:11676.
UCSCuc007kiw.1. mouse.

Organism-specific databases

CTD230.
MGIMGI:101863. Aldoc.

Phylogenomic databases

eggNOGCOG3588.
GeneTreeENSGT00390000010235.
HOGENOMHOG000220876.
HOVERGENHBG002386.
InParanoidP05063.
KOK01623.
OMARGQQDNA.
OrthoDBEOG744T94.
TreeFamTF314203.

Enzyme and pathway databases

SABIO-RKP05063.
UniPathwayUPA00109; UER00183.

Gene expression databases

BgeeP05063.
CleanExMM_ALDOC.
GenevestigatorP05063.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALDOC. mouse.
NextBio279307.
PROP05063.
SOURCESearch...

Entry information

Entry nameALDOC_MOUSE
AccessionPrimary (citable) accession number: P05063
Secondary accession number(s): Q64011 expand/collapse secondary AC list , Q8CA91, Q99K96, Q9DBA4, Q9JK32
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 141 of the entry and version 4 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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