P05063 (ALDOC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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. 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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Schiff base
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: Compara fructose 1,6-bisphosphate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway organ regeneration Inferred from electronic annotation. Source: Compara protein heterotetramerization Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara response to organic nitrogen Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay PubMed 14651853. Source: MGI
Molecular_function	fructose-bisphosphate aldolase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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
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 [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] [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. , 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.
[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] [Europe PMC] [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
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.
IPI	IPI00119458.
PIR	ADMSC. A25388. I53145.
RefSeq	NP_033787.2. NM_009657.3.
UniGene	Mm.7729.
3D structure databases
ProteinModelPortal	P05063.
SMR	P05063. Positions 3-344.
ModBase	Search...
Protein-protein interaction databases
IntAct	P05063. 5 interactions.
PTM databases
PhosphoSite	P05063.
2D gel databases
REPRODUCTION-2DPAGE	IPI00119458.
UCD-2DPAGE	P05063.
Proteomic databases
PaxDb	P05063.
PRIDE	P05063.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000017534; ENSMUSP00000017534; ENSMUSG00000017390. ENSMUST00000102478; ENSMUSP00000099536; ENSMUSG00000017390.
GeneID	11676.
KEGG	mmu:11676.
Organism-specific databases
CTD	230.
MGI	MGI:101863. Aldoc.
Phylogenomic databases
eggNOG	COG3588.
GeneTree	ENSGT00390000010235.
HOGENOM	HOG000220876.
HOVERGEN	HBG002386.
InParanoid	P05063.
KO	K01623.
OMA	RGQQDNA.
OrthoDB	EOG4X3H1J.
Enzyme and pathway databases
SABIO-RK	P05063.
UniPathway	UPA00109; UER00183.
Gene expression databases
ArrayExpress	P05063.
Bgee	P05063.
CleanEx	MM_ALDOC.
Genevestigator	P05063.
GermOnline	ENSMUSG00000017390. Mus musculus.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR000741. Aldolase_I. IPR013785. Aldolase_TIM. [Graphical view]
PANTHER	PTHR11627. PTHR11627. 1 hit.
Pfam	PF00274. Glycolytic. 1 hit. [Graphical view]
PROSITE	PS00158. ALDOLASE_CLASS_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ALDOC. mouse.
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:	April 3, 2013
This is version 133 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program