Reviewed, UniProtKB/Swiss-Prot P05063 (ALDOC_MOUSE)

Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase C
    EC=4.1.2.13
Alternative name(s):
    Brain-type aldolase
    Aldolase 3
    Zebrin II
    Scrapie-responsive protein 2

Gene names

Name:	Aldoc
Synonyms:	Aldo3, Scrg2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	fructose-bisphosphate aldolase activity Non-traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRNP	P04156	1	EBI-444845,EBI-977302	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 363	362	Fructose-bisphosphate aldolase C		PRO_0000216949
Sites
	Active site	188	1	Proton acceptor By similarity
	Active site	230	1	Schiff-base intermediate with dihydroxyacetone-P
	Binding site	56	1	Substrate
	Binding site	147	1	Substrate
	Site	363	1	Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate
Amino acid modifications
	Modified residue	39	1	Phosphoserine Ref.7
	Modified residue	119	1	Phosphothreonine Ref.8
	Modified residue	147	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	25	1	T → A in AAH04802. Ref.3
	Sequence conflict	25	1	T → A in AAH08184. Ref.3
	Sequence conflict	46	1	Q → E in BAC30300. Ref.2
	Sequence conflict	62	1	V → A in CAA27422. Ref.4
	Sequence conflict	113	1	V → L in CAA27422. Ref.4
	Sequence conflict	201	1	R → H in AAH04802. Ref.3
	Sequence conflict	201	1	R → H in AAH08184. Ref.3
	Sequence conflict	280	1	A → V in AAB32064. Ref.1
	Sequence conflict	358	1	I → V in AAH04802. Ref.3
	Sequence conflict	358	1	I → V in AAH08184. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P05063-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 085C58AF163581C6	FASTA	363	39,395
	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

References

	« Hide 'large scale' referencesShow '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: 7925012] [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. , 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: 16141072] [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: 15489334] [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: 3009179] [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: 10719228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-363, TISSUE SPECIFICITY. Strain: BALB/c. Tissue: Brain.
[7]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, MASS SPECTROMETRY. Tissue: Brain cortex.
[8]	Lubec G., Kang S. Submitted (APR-2007) to UniProtKB Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00119458.
PIR	ADMSC. A25388. I53145.
RefSeq	NP_033787.2.
UniGene	Mm.7729
3D structure databases
HSSP	HSSP built from PDB template 6ALD based on UniProtKB P00883.
SMR	P05063. Positions 3-344.
ModBase	Search...
Protein-protein interaction databases
IntAct	P05063. 3 interactions.
PTM databases
PhosphoSite	P05063.
Proteomic databases
PRIDE	P05063.
Genome annotation databases
Ensembl	ENSMUSG00000017390. Mus musculus. [Contig view]
GeneID	11676.
KEGG	mmu:11676.
Organism-specific databases
MGI	MGI:101863. Aldoc.
Phylogenomic databases
HOGENOM	P05063.
HOVERGEN	P05063.
OMA	P05063. ACPIKYT.
Enzyme and pathway databases
BRENDA	4.1.2.13. 244.
Gene expression databases
ArrayExpress	P05063.
Bgee	P05063.
CleanEx	MM_ALDOC.
GermOnline	ENSMUSG00000017390. Mus musculus.
Family and domain databases
InterPro	IPR000741. Aldolase_I. IPR013785. Aldolase_TIM. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR11627. Aldolase_I. 1 hit.
Pfam	PF00274. Glycolytic. 1 hit. [Graphical view]
ProDom	PD001128. Aldolase_I. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00158. ALDOLASE_CLASS_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	279307.
SOURCE	Search...

Entry information

Entry name

ALDOC_MOUSE

Accession

Primary (citable) accession number: P05063
Secondary accession number(s): Q64011 , Q8CA91, Q99K96, Q9DBA4, Q9JK32

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 103 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)