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P09117

- ALDOC_RAT

UniProt

P09117 - ALDOC_RAT

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Protein
Fructose-bisphosphate aldolase C
Gene
Aldoc
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 acceptor By 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. fructose-bisphosphate aldolase activity Source: UniProtKB
  2. protein binding Source: RGD
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiREACT_217998. Gluconeogenesis.
REACT_225694. Glycolysis.
SABIO-RKiP09117.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase C (EC:4.1.2.13)
Alternative name(s):
Brain-type aldolase
Gene namesi
Name:Aldoc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi2091. Aldoc.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: RGD
  2. cytoplasm Source: RGD
  3. mitochondrion Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 363362Fructose-bisphosphate aldolase C
PRO_0000216951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP09117.
PRIDEiP09117.

2D gel databases

World-2DPAGEi0004:P09117.

PTM databases

PhosphoSiteiP09117.

Expressioni

Tissue specificityi

High expression in the adult brain.1 Publication

Developmental stagei

Detected at low concentration in practically all the fetal tissues and its expression markedly and rapidly decreased after birth.1 Publication

Gene expression databases

ArrayExpressiP09117.
GenevestigatoriP09117.

Interactioni

Subunit structurei

Homotetramer. Interacts with ATP6V1E1 By similarity.

Protein-protein interaction databases

BioGridi246381. 3 interactions.
IntActiP09117. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP09117.
SMRiP09117. Positions 3-344.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP09117.
KOiK01623.
OMAiRGQQDNA.
OrthoDBiEOG744T94.
PhylomeDBiP09117.
TreeFamiTF314203.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
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.

P09117-1 [UniParc]FASTAAdd to Basket

« Hide

MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE    50
NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQE 100
KGILVGIKVD KGVVPLAGTD GETTTQGLDG LLERCAQYKK DGADFAKWRC 150
VLKISDRTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK 200
RCQFVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYSPEEIA 250
MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC SLPRPWALTF 300
SYGRALQASA LSAWRGQRDN AGAATEEFIK RAEMNGLAAQ GKYEGSGDGG 350
AAAQSLYVAN HAY 363
Length:363
Mass (Da):39,284
Last modified:January 23, 2007 - v3
Checksum:i00FDB44B602FA9B3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti337 – 3393LAA → ACS in CAA30044. 1 Publication
Sequence conflicti337 – 3393LAA → ACS in CAA28889. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63656 Genomic DNA. Translation: AAA40717.1.
X06984 mRNA. Translation: CAA30044.1.
AB017483 Genomic DNA. Translation: BAA75659.1.
BC099749 mRNA. Translation: AAH99749.1.
X05277 mRNA. Translation: CAA28889.1.
PIRiS00326. ADRTC.
RefSeqiNP_036629.1. NM_012497.1.
UniGeneiRn.11211.

Genome annotation databases

EnsembliENSRNOT00000015535; ENSRNOP00000015535; ENSRNOG00000011452.
GeneIDi24191.
KEGGirno:24191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63656 Genomic DNA. Translation: AAA40717.1 .
X06984 mRNA. Translation: CAA30044.1 .
AB017483 Genomic DNA. Translation: BAA75659.1 .
BC099749 mRNA. Translation: AAH99749.1 .
X05277 mRNA. Translation: CAA28889.1 .
PIRi S00326. ADRTC.
RefSeqi NP_036629.1. NM_012497.1.
UniGenei Rn.11211.

3D structure databases

ProteinModelPortali P09117.
SMRi P09117. Positions 3-344.
ModBasei Search...

Protein-protein interaction databases

BioGridi 246381. 3 interactions.
IntActi P09117. 1 interaction.

PTM databases

PhosphoSitei P09117.

2D gel databases

World-2DPAGEi 0004:P09117.

Proteomic databases

PaxDbi P09117.
PRIDEi P09117.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000015535 ; ENSRNOP00000015535 ; ENSRNOG00000011452 .
GeneIDi 24191.
KEGGi rno:24191.

Organism-specific databases

CTDi 230.
RGDi 2091. Aldoc.

Phylogenomic databases

eggNOGi COG3588.
GeneTreei ENSGT00390000010235.
HOGENOMi HOG000220876.
HOVERGENi HBG002386.
InParanoidi P09117.
KOi K01623.
OMAi RGQQDNA.
OrthoDBi EOG744T94.
PhylomeDBi P09117.
TreeFami TF314203.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
Reactomei REACT_217998. Gluconeogenesis.
REACT_225694. Glycolysis.
SABIO-RKi P09117.

Miscellaneous databases

NextBioi 602567.

Gene expression databases

ArrayExpressi P09117.
Genevestigatori P09117.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view ]
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The structure of the brain-specific rat aldolase C gene and its regional expression."
    Mukai T., Yatsuki H., Masuko S., Arai Y., Joh K., Hori K.
    Biochem. Biophys. Res. Commun. 174:1035-1042(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  2. "The structure of brain-specific rat aldolase C mRNA and the evolution of aldolase isozyme genes."
    Kukita A., Mukai T., Miyata T., Hori K.
    Eur. J. Biochem. 171:471-478(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "The first exon of the rat aldolase C gene is essential for restoring the chromatin structure in transgenic mice."
    Arai Y., Sugama T., Hashido K., Ohishi S., Mukai T.
    J. Biochem. 122:927-938(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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: Prostate.
  5. Lubec G., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 15-22; 61-69; 73-96; 112-134; 158-215; 244-258; 260-289; 305-315; 319-330 AND 343-363, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  6. "Molecular cloning and expression of rat aldolase C messenger RNA during development and hepatocarcinogenesis."
    Skala H., Vibert M., Lamas E., Maire P., Schweighoffer F., Kahn A.
    Eur. J. Biochem. 163:513-518(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 251-363, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Wistar.
    Tissue: Brain.

Entry informationi

Entry nameiALDOC_RAT
AccessioniPrimary (citable) accession number: P09117
Secondary accession number(s): Q54AI4, Q63037
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 118 of the entry and version 3 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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