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Protein

Fructose-bisphosphate aldolase C

Gene

Aldoc

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

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Substrate
Binding sitei147 – 1471Substrate
Active sitei188 – 1881Proton acceptorBy similarity
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P
Sitei363 – 3631Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  1. cytoskeletal protein binding Source: MGI
  2. fructose-bisphosphate aldolase activity Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. apoptotic process Source: Ensembl
  3. epithelial cell differentiation Source: Ensembl
  4. fructose 1,6-bisphosphate metabolic process Source: UniProtKB
  5. glycolytic process Source: UniProtKB-UniPathway
  6. organ regeneration Source: Ensembl
  7. protein heterotetramerization Source: Ensembl
  8. protein homotetramerization Source: Ensembl
  9. response to hypoxia Source: Ensembl
  10. response to organic cyclic compound Source: Ensembl
  11. response to organonitrogen compound Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiREACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
SABIO-RKP05063.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Aldoc
Synonyms:Aldo3, Scrg2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:101863. Aldoc.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: Ensembl
  2. extracellular vesicular exosome Source: MGI
  3. mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 363362Fructose-bisphosphate aldolase CPRO_0000216949Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131N6-succinyllysineBy similarity
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei39 – 391PhosphoserineBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei111 – 1111N-acetylated lysineBy similarity
Modified residuei119 – 1191PhosphothreonineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei276 – 2761PhosphoserineBy similarity
Modified residuei309 – 3091PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05063.
PaxDbiP05063.
PRIDEiP05063.

2D gel databases

REPRODUCTION-2DPAGEIPI00119458.
UCD-2DPAGEP05063.

PTM databases

PhosphoSiteiP05063.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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

Gene expression databases

BgeeiP05063.
CleanExiMM_ALDOC.
GenevestigatoriP05063.

Interactioni

Subunit structurei

Homotetramer. Interacts with ATP6V1E1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198068. 1 interaction.
IntActiP05063. 6 interactions.
MINTiMINT-1864918.

Structurei

3D structure databases

ProteinModelPortaliP05063.
SMRiP05063. Positions 3-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP05063.
KOiK01623.
OMAiWRGQQDN.
OrthoDBiEOG744T94.
PhylomeDBiP05063.
TreeFamiTF314203.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05063-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHSYPALSA EQKKELSDIA LRIVTPGKGI LAADESVGSM AKRLSQIGVE
60 70 80 90 100
NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD
110 120 130 140 150
KGILVGIKVD KGVVPLAGTD GETTTQGLDG LLERCAQYKK DGADFAKWRC
160 170 180 190 200
VLKISDRTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
210 220 230 240 250
RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYSPEEIA
260 270 280 290 300
MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC PLPRPWALTF
310 320 330 340 350
SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEMNGLAAQ GRYEGSGDGG
360
AAAQSLYIAN HAY
Length:363
Mass (Da):39,395
Last modified:January 23, 2007 - v4
Checksum:i085C58AF163581C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251T → A in AAH04802 (PubMed:15489334).Curated
Sequence conflicti25 – 251T → A in AAH08184 (PubMed:15489334).Curated
Sequence conflicti46 – 461Q → E in BAC30300 (PubMed:16141072).Curated
Sequence conflicti62 – 621V → A in CAA27422 (PubMed:3009179).Curated
Sequence conflicti113 – 1131V → L in CAA27422 (PubMed:3009179).Curated
Sequence conflicti201 – 2011R → H in AAH04802 (PubMed:15489334).Curated
Sequence conflicti201 – 2011R → H in AAH08184 (PubMed:15489334).Curated
Sequence conflicti280 – 2801A → V in AAB32064 (PubMed:7925012).Curated
Sequence conflicti358 – 3581I → V in AAH04802 (PubMed:15489334).Curated
Sequence conflicti358 – 3581I → V in AAH08184 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25099.1.
PIRiA25388. ADMSC.
I53145.
RefSeqiNP_001290352.1. NM_001303423.1.
NP_033787.2. NM_009657.4.
UniGeneiMm.7729.

Genome annotation databases

EnsembliENSMUST00000017534; ENSMUSP00000017534; ENSMUSG00000017390.
ENSMUST00000102478; ENSMUSP00000099536; ENSMUSG00000017390.
GeneIDi11676.
KEGGimmu:11676.
UCSCiuc007kiw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25099.1.
PIRiA25388. ADMSC.
I53145.
RefSeqiNP_001290352.1. NM_001303423.1.
NP_033787.2. NM_009657.4.
UniGeneiMm.7729.

3D structure databases

ProteinModelPortaliP05063.
SMRiP05063. Positions 3-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198068. 1 interaction.
IntActiP05063. 6 interactions.
MINTiMINT-1864918.

PTM databases

PhosphoSiteiP05063.

2D gel databases

REPRODUCTION-2DPAGEIPI00119458.
UCD-2DPAGEP05063.

Proteomic databases

MaxQBiP05063.
PaxDbiP05063.
PRIDEiP05063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017534; ENSMUSP00000017534; ENSMUSG00000017390.
ENSMUST00000102478; ENSMUSP00000099536; ENSMUSG00000017390.
GeneIDi11676.
KEGGimmu:11676.
UCSCiuc007kiw.1. mouse.

Organism-specific databases

CTDi230.
MGIiMGI:101863. Aldoc.

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP05063.
KOiK01623.
OMAiWRGQQDN.
OrthoDBiEOG744T94.
PhylomeDBiP05063.
TreeFamiTF314203.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
ReactomeiREACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
SABIO-RKP05063.

Miscellaneous databases

ChiTaRSiAldoc. mouse.
NextBioi279307.
PROiP05063.
SOURCEiSearch...

Gene expression databases

BgeeiP05063.
CleanExiMM_ALDOC.
GenevestigatoriP05063.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [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(2004) [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(2003) [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(1985) [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 (DEC-2008) 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, IDENTIFICATION BY 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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-363, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Brain.

Entry informationi

Entry nameiALDOC_MOUSE
AccessioniPrimary (citable) accession number: P05063
Secondary accession number(s): Q64011
, Q8CA91, Q99K96, Q9DBA4, Q9JK32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3

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 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.