P09972 (ALDOC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fructose-bisphosphate aldolase C
EC=4.1.2.13

Alternative name(s):
Brain-type aldolase

Gene names

Name:	ALDOC
Synonyms:	ALDC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	364 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. Ref.13
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Subunit structure	Homotetramer. Interacts with ATP6V1E1. May interact with PLD2. Ref.10 Ref.11
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.
Biophysicochemical properties	Kinetic parameters: KM=10.7 µM for fructose 1,6-bisphosphate Ref.13 KM=16 mM for fructose 1-phosphate
Sequence caution	The sequence AAI03761.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Schiff base
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome 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 direct assay Ref.13. Source: UniProtKB fructose metabolic process Traceable author statement Ref.1. Source: ProtInc gluconeogenesis Traceable author statement. Source: Reactome glycolysis Traceable author statement. Source: Reactome 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 small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	axon Inferred from electronic annotation. Source: Compara cytoskeleton Inferred by curator PubMed 9244396. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	cytoskeletal protein binding Inferred from direct assay PubMed 9244396. Source: BHF-UCL fructose-bisphosphate aldolase activity Inferred from direct assay Ref.13. 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 – 364

363

Fructose-bisphosphate aldolase C

PRO_0000216947

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

364

1

Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue

39

1

Phosphoserine By similarity

Modified residue

119

1

Phosphothreonine By similarity

Experimental info

Sequence conflict

311

1

L → V in CAA30270. Ref.2

Secondary structure

1

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364

Helix Strand Turn

Details...

Helix

10 – 23

14

Beta strand

29 – 33

5

Helix

37 – 45

9

Helix

53 – 64

12

Helix

68 – 70

3

Turn

71 – 73

3

Beta strand

74 – 79

6

Helix

82 – 85

4

Helix

94 – 100

7

Beta strand

104 – 108

5

Beta strand

113 – 115

3

Beta strand

119 – 121

3

Beta strand

123 – 125

3

Helix

131 – 140

10

Beta strand

145 – 152

8

Helix

161 – 179

19

Turn

180 – 182

3

Beta strand

184 – 191

8

Helix

199 – 219

21

Helix

224 – 226

3

Helix

246 – 257

12

Turn

258 – 260

3

Beta strand

267 – 271

5

Helix

277 – 288

12

Beta strand

295 – 303

9

Helix

304 – 314

11

Helix

321 – 338

18

Turn

339 – 341

3

Sequences

	Sequence		Length	Mass (Da)
	P09972 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 506A570B3E507971	FASTA	364	39,456
	10 20 30 40 50 60 MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR 70 80 90 100 110 120 QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD 130 140 150 160 170 180 GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ 190 200 210 220 230 240 NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC 250 260 270 280 290 300 PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF 310 320 330 340 350 360 SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA NHAY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete amino acid sequence of the human aldolase C isozyme derived from genomic clones." Rottmann W.H., Deselms K.R., Niclas J., Camerato T., Holman P.S., Green C.J., Tolan D.R. Biochimie 69:137-145(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete nucleotide sequence of the gene coding for the human aldolase C." Buono P., Paolella G., Mancini F.P., Izzo P., Salvatore F. Nucleic Acids Res. 16:4733-4733(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Characterization of the transcription-initiation site and of the promoter region within the 5' flanking region of the human aldolase C gene." Buono P., Mancini F.P., Izzo P., Salvatore F. Eur. J. Biochem. 192:805-811(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	Yu W., Gibbs R.A. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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: Colon, Eye and Uterus.
[10]	"Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump." Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L. J. Biol. Chem. 276:30407-30413(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATP6V1E1.
[11]	"Phospholipase D2 directly interacts with aldolase via its PH domain." Kim J.H., Lee S., Kim J.H., Lee T.G., Hirata M., Suh P.-G., Ryu S.H. Biochemistry 41:3414-3421(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLD2.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function." Arakaki T.L., Pezza J.A., Cronin M.A., Hopkins C.E., Zimmer D.B., Tolan D.R., Allen K.N. Protein Sci. 13:3077-3084(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-364, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05196 Genomic DNA. Translation: CAA28825.1.
X07292 Genomic DNA. Translation: CAA30270.1.
AF054987 mRNA. Translation: AAC09348.1.
BT007006 mRNA. Translation: AAP35652.1.
CR541862 mRNA. Translation: CAG46660.1.
CR541881 mRNA. Translation: CAG46679.1.
AK312281 mRNA. Translation: BAG35210.1.
CH471159 Genomic DNA. Translation: EAW51104.1.
BC003613 mRNA. Translation: AAH03613.3.
BC103760 mRNA. Translation: AAI03761.1. Different initiation.
BC065565 mRNA. Translation: AAH65565.2.
BC106925 mRNA. Translation: AAI06926.1.
BC106926 mRNA. Translation: AAI06927.1.

IPI

IPI00418262.

PIR

ADHUC. A25861.

RefSeq

NP_005156.1. NM_005165.2.

UniGene

Hs.155247.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XFB	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L	1-364	[»]

ProteinModelPortal

P09972.

ModBase

Search...

Protein-protein interaction databases

IntAct

P09972. 3 interactions.

STRING

9606.ENSP00000226253.

PTM databases

PhosphoSite

P09972.

Polymorphism databases

DMDM

113613.

2D gel databases

UCD-2DPAGE

P09972.

Proteomic databases

PaxDb

P09972.

PRIDE

P09972.

Protocols and materials databases

DNASU

230.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000226253; ENSP00000226253; ENSG00000109107.
ENST00000395321; ENSP00000378731; ENSG00000109107.

GeneID

230.

KEGG

hsa:230.

UCSC

uc002hbp.3. human.

Organism-specific databases

CTD

230.

GeneCards

GC17M026900.

HGNC

HGNC:418. ALDOC.

HPA

CAB020828.
HPA003282.

MIM

103870. gene.

neXtProt

NX_P09972.

PharmGKB

PA24711.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3588.

HOVERGEN

HBG002386.

InParanoid

P09972.

KO

K01623.

OMA

RGQQDNA.

OrthoDB

EOG4X3H1J.

PhylomeDB

P09972.

Enzyme and pathway databases

BioCyc

MetaCyc:HS03200-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P09972.

UniPathway

UPA00109; UER00183.

Gene expression databases

ArrayExpress

P09972.

Bgee

P09972.

CleanEx

HS_ALDOC.

Genevestigator

P09972.

GermOnline

ENSG00000109107. Homo sapiens.

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. human.

EvolutionaryTrace

P09972.

GenomeRNAi

230.

NextBio

934.

SOURCE

Search...

Entry information

Entry name

ALDOC_HUMAN

Accession

Primary (citable) accession number: P09972
Secondary accession number(s): B2R5R3 , Q3SYL3, Q6FH94, Q6P0L5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 140 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.