Full text data of ALDOC
ALDOC
(ALDC)
[Confidence: high (present in two of the MS resources)]
Fructose-bisphosphate aldolase C; 4.1.2.13 (Brain-type aldolase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Fructose-bisphosphate aldolase C; 4.1.2.13 (Brain-type aldolase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00418262
IPI00418262 ALDOC protein ALDOC protein membrane n/a 1 1 n/a n/a n/a 1 n/a 6 n/a n/a n/a n/a n/a n/a n/a n/a 3 n/a n/a Glycolisis n/a found at its expected molecular weight found at molecular weight
IPI00418262 ALDOC protein ALDOC protein membrane n/a 1 1 n/a n/a n/a 1 n/a 6 n/a n/a n/a n/a n/a n/a n/a n/a 3 n/a n/a Glycolisis n/a found at its expected molecular weight found at molecular weight
UniProt
P09972
ID ALDOC_HUMAN Reviewed; 364 AA.
AC P09972; B2R5R3; Q3SYL3; Q6FH94; Q6P0L5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Fructose-bisphosphate aldolase C;
DE EC=4.1.2.13;
DE AltName: Full=Brain-type aldolase;
GN Name=ALDOC; Synonyms=ALDC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3105602; DOI=10.1016/0300-9084(87)90246-X;
RA Rottmann W.H., Deselms K.R., Niclas J., Camerato T., Holman P.S.,
RA Green C.J., Tolan D.R.;
RT "The complete amino acid sequence of the human aldolase C isozyme
RT derived from genomic clones.";
RL Biochimie 69:137-145(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3267224; DOI=10.1093/nar/16.10.4733;
RA Buono P., Paolella G., Mancini F.P., Izzo P., Salvatore F.;
RT "The complete nucleotide sequence of the gene coding for the human
RT aldolase C.";
RL Nucleic Acids Res. 16:4733-4733(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2209624; DOI=10.1111/j.1432-1033.1990.tb19294.x;
RA Buono P., Mancini F.P., Izzo P., Salvatore F.;
RT "Characterization of the transcription-initiation site and of the
RT promoter region within the 5' flanking region of the human aldolase C
RT gene.";
RL Eur. J. Biochem. 192:805-811(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Eye, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP INTERACTION WITH ATP6V1E1.
RX PubMed=11399750; DOI=10.1074/jbc.M008768200;
RA Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L.;
RT "Interaction between aldolase and vacuolar H+-ATPase: evidence for
RT direct coupling of glycolysis to the ATP-hydrolyzing proton pump.";
RL J. Biol. Chem. 276:30407-30413(2001).
RN [11]
RP INTERACTION WITH PLD2.
RX PubMed=11876650; DOI=10.1021/bi015700a;
RA Kim J.H., Lee S., Kim J.H., Lee T.G., Hirata M., Suh P.-G., Ryu S.H.;
RT "Phospholipase D2 directly interacts with aldolase via its PH
RT domain.";
RL Biochemistry 41:3414-3421(2002).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-364, CATALYTIC ACTIVITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15537755; DOI=10.1110/ps.04915904;
RA Arakaki T.L., Pezza J.A., Cronin M.A., Hopkins C.E., Zimmer D.B.,
RA Tolan D.R., Allen K.N.;
RT "Structure of human brain fructose 1,6-(bis)phosphate aldolase:
RT linking isozyme structure with function.";
RL Protein Sci. 13:3077-3084(2004).
CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC phosphate + D-glyceraldehyde 3-phosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.7 uM for fructose 1,6-bisphosphate;
CC KM=16 mM for fructose 1-phosphate;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. Interacts with ATP6V1E1. May interact with
CC PLD2.
CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in
CC liver and aldolase C in brain.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI03761.1; Type=Erroneous initiation;
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DR EMBL; X05196; CAA28825.1; -; Genomic_DNA.
DR EMBL; X07292; CAA30270.1; -; Genomic_DNA.
DR EMBL; AF054987; AAC09348.1; -; mRNA.
DR EMBL; BT007006; AAP35652.1; -; mRNA.
DR EMBL; CR541862; CAG46660.1; -; mRNA.
DR EMBL; CR541881; CAG46679.1; -; mRNA.
DR EMBL; AK312281; BAG35210.1; -; mRNA.
DR EMBL; CH471159; EAW51104.1; -; Genomic_DNA.
DR EMBL; BC003613; AAH03613.3; -; mRNA.
DR EMBL; BC103760; AAI03761.1; ALT_INIT; mRNA.
DR EMBL; BC065565; AAH65565.2; -; mRNA.
DR EMBL; BC106925; AAI06926.1; -; mRNA.
DR EMBL; BC106926; AAI06927.1; -; mRNA.
DR PIR; A25861; ADHUC.
DR RefSeq; NP_005156.1; NM_005165.2.
DR RefSeq; XP_005258006.1; XM_005257949.1.
DR UniGene; Hs.155247; -.
DR PDB; 1XFB; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-364.
DR PDBsum; 1XFB; -.
DR ProteinModelPortal; P09972; -.
DR SMR; P09972; 3-344.
DR IntAct; P09972; 3.
DR STRING; 9606.ENSP00000226253; -.
DR PhosphoSite; P09972; -.
DR DMDM; 113613; -.
DR UCD-2DPAGE; P09972; -.
DR PaxDb; P09972; -.
DR PRIDE; P09972; -.
DR DNASU; 230; -.
DR Ensembl; ENST00000226253; ENSP00000226253; ENSG00000109107.
DR Ensembl; ENST00000395321; ENSP00000378731; ENSG00000109107.
DR GeneID; 230; -.
DR KEGG; hsa:230; -.
DR UCSC; uc002hbp.3; human.
DR CTD; 230; -.
DR GeneCards; GC17M026900; -.
DR HGNC; HGNC:418; ALDOC.
DR HPA; CAB020828; -.
DR HPA; HPA003282; -.
DR MIM; 103870; gene.
DR neXtProt; NX_P09972; -.
DR PharmGKB; PA24711; -.
DR eggNOG; COG3588; -.
DR HOVERGEN; HBG002386; -.
DR InParanoid; P09972; -.
DR KO; K01623; -.
DR OMA; RGQQDNA; -.
DR PhylomeDB; P09972; -.
DR BioCyc; MetaCyc:HS03200-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P09972; -.
DR UniPathway; UPA00109; UER00183.
DR ChiTaRS; ALDOC; human.
DR EvolutionaryTrace; P09972; -.
DR GeneWiki; Aldolase_C; -.
DR GenomeRNAi; 230; -.
DR NextBio; 934; -.
DR PRO; PR:P09972; -.
DR ArrayExpress; P09972; -.
DR Bgee; P09972; -.
DR CleanEx; HS_ALDOC; -.
DR Genevestigator; P09972; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IC:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:BHF-UCL.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006000; P:fructose metabolic process; TAS:ProtInc.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0006096; P:glycolysis; TAS:Reactome.
DR GO; GO:0031100; P:organ regeneration; IEA:Ensembl.
DR GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR000741; Aldolase_I.
DR InterPro; IPR013785; Aldolase_TIM.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Glycolysis; Lyase;
KW Reference proteome; Schiff base.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 364 Fructose-bisphosphate aldolase C.
FT /FTId=PRO_0000216947.
FT ACT_SITE 188 188 Proton acceptor (By similarity).
FT ACT_SITE 230 230 Schiff-base intermediate with
FT dihydroxyacetone-P.
FT BINDING 56 56 Substrate.
FT BINDING 147 147 Substrate.
FT SITE 364 364 Necessary for preference for fructose
FT 1,6-bisphosphate over fructose 1-
FT phosphate.
FT MOD_RES 111 111 N6-acetyllysine.
FT CONFLICT 311 311 L -> V (in Ref. 2; CAA30270).
FT HELIX 10 23
FT STRAND 29 33
FT HELIX 37 45
FT HELIX 53 64
FT HELIX 68 70
FT TURN 71 73
FT STRAND 74 79
FT HELIX 82 85
FT HELIX 94 100
FT STRAND 104 108
FT STRAND 113 115
FT STRAND 119 121
FT STRAND 123 125
FT HELIX 131 140
FT STRAND 145 152
FT HELIX 161 179
FT TURN 180 182
FT STRAND 184 191
FT HELIX 199 219
FT HELIX 224 226
FT HELIX 246 257
FT TURN 258 260
FT STRAND 267 271
FT HELIX 277 288
FT STRAND 295 303
FT HELIX 304 314
FT HELIX 321 338
FT TURN 339 341
SQ SEQUENCE 364 AA; 39456 MW; 506A570B3E507971 CRC64;
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR
QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC
PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF
SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA
NHAY
//
ID ALDOC_HUMAN Reviewed; 364 AA.
AC P09972; B2R5R3; Q3SYL3; Q6FH94; Q6P0L5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Fructose-bisphosphate aldolase C;
DE EC=4.1.2.13;
DE AltName: Full=Brain-type aldolase;
GN Name=ALDOC; Synonyms=ALDC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3105602; DOI=10.1016/0300-9084(87)90246-X;
RA Rottmann W.H., Deselms K.R., Niclas J., Camerato T., Holman P.S.,
RA Green C.J., Tolan D.R.;
RT "The complete amino acid sequence of the human aldolase C isozyme
RT derived from genomic clones.";
RL Biochimie 69:137-145(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3267224; DOI=10.1093/nar/16.10.4733;
RA Buono P., Paolella G., Mancini F.P., Izzo P., Salvatore F.;
RT "The complete nucleotide sequence of the gene coding for the human
RT aldolase C.";
RL Nucleic Acids Res. 16:4733-4733(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2209624; DOI=10.1111/j.1432-1033.1990.tb19294.x;
RA Buono P., Mancini F.P., Izzo P., Salvatore F.;
RT "Characterization of the transcription-initiation site and of the
RT promoter region within the 5' flanking region of the human aldolase C
RT gene.";
RL Eur. J. Biochem. 192:805-811(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Eye, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP INTERACTION WITH ATP6V1E1.
RX PubMed=11399750; DOI=10.1074/jbc.M008768200;
RA Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L.;
RT "Interaction between aldolase and vacuolar H+-ATPase: evidence for
RT direct coupling of glycolysis to the ATP-hydrolyzing proton pump.";
RL J. Biol. Chem. 276:30407-30413(2001).
RN [11]
RP INTERACTION WITH PLD2.
RX PubMed=11876650; DOI=10.1021/bi015700a;
RA Kim J.H., Lee S., Kim J.H., Lee T.G., Hirata M., Suh P.-G., Ryu S.H.;
RT "Phospholipase D2 directly interacts with aldolase via its PH
RT domain.";
RL Biochemistry 41:3414-3421(2002).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-364, CATALYTIC ACTIVITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15537755; DOI=10.1110/ps.04915904;
RA Arakaki T.L., Pezza J.A., Cronin M.A., Hopkins C.E., Zimmer D.B.,
RA Tolan D.R., Allen K.N.;
RT "Structure of human brain fructose 1,6-(bis)phosphate aldolase:
RT linking isozyme structure with function.";
RL Protein Sci. 13:3077-3084(2004).
CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC phosphate + D-glyceraldehyde 3-phosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.7 uM for fructose 1,6-bisphosphate;
CC KM=16 mM for fructose 1-phosphate;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. Interacts with ATP6V1E1. May interact with
CC PLD2.
CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in
CC liver and aldolase C in brain.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI03761.1; Type=Erroneous initiation;
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DR EMBL; X05196; CAA28825.1; -; Genomic_DNA.
DR EMBL; X07292; CAA30270.1; -; Genomic_DNA.
DR EMBL; AF054987; AAC09348.1; -; mRNA.
DR EMBL; BT007006; AAP35652.1; -; mRNA.
DR EMBL; CR541862; CAG46660.1; -; mRNA.
DR EMBL; CR541881; CAG46679.1; -; mRNA.
DR EMBL; AK312281; BAG35210.1; -; mRNA.
DR EMBL; CH471159; EAW51104.1; -; Genomic_DNA.
DR EMBL; BC003613; AAH03613.3; -; mRNA.
DR EMBL; BC103760; AAI03761.1; ALT_INIT; mRNA.
DR EMBL; BC065565; AAH65565.2; -; mRNA.
DR EMBL; BC106925; AAI06926.1; -; mRNA.
DR EMBL; BC106926; AAI06927.1; -; mRNA.
DR PIR; A25861; ADHUC.
DR RefSeq; NP_005156.1; NM_005165.2.
DR RefSeq; XP_005258006.1; XM_005257949.1.
DR UniGene; Hs.155247; -.
DR PDB; 1XFB; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-364.
DR PDBsum; 1XFB; -.
DR ProteinModelPortal; P09972; -.
DR SMR; P09972; 3-344.
DR IntAct; P09972; 3.
DR STRING; 9606.ENSP00000226253; -.
DR PhosphoSite; P09972; -.
DR DMDM; 113613; -.
DR UCD-2DPAGE; P09972; -.
DR PaxDb; P09972; -.
DR PRIDE; P09972; -.
DR DNASU; 230; -.
DR Ensembl; ENST00000226253; ENSP00000226253; ENSG00000109107.
DR Ensembl; ENST00000395321; ENSP00000378731; ENSG00000109107.
DR GeneID; 230; -.
DR KEGG; hsa:230; -.
DR UCSC; uc002hbp.3; human.
DR CTD; 230; -.
DR GeneCards; GC17M026900; -.
DR HGNC; HGNC:418; ALDOC.
DR HPA; CAB020828; -.
DR HPA; HPA003282; -.
DR MIM; 103870; gene.
DR neXtProt; NX_P09972; -.
DR PharmGKB; PA24711; -.
DR eggNOG; COG3588; -.
DR HOVERGEN; HBG002386; -.
DR InParanoid; P09972; -.
DR KO; K01623; -.
DR OMA; RGQQDNA; -.
DR PhylomeDB; P09972; -.
DR BioCyc; MetaCyc:HS03200-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P09972; -.
DR UniPathway; UPA00109; UER00183.
DR ChiTaRS; ALDOC; human.
DR EvolutionaryTrace; P09972; -.
DR GeneWiki; Aldolase_C; -.
DR GenomeRNAi; 230; -.
DR NextBio; 934; -.
DR PRO; PR:P09972; -.
DR ArrayExpress; P09972; -.
DR Bgee; P09972; -.
DR CleanEx; HS_ALDOC; -.
DR Genevestigator; P09972; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IC:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:BHF-UCL.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006000; P:fructose metabolic process; TAS:ProtInc.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0006096; P:glycolysis; TAS:Reactome.
DR GO; GO:0031100; P:organ regeneration; IEA:Ensembl.
DR GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR000741; Aldolase_I.
DR InterPro; IPR013785; Aldolase_TIM.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Glycolysis; Lyase;
KW Reference proteome; Schiff base.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 364 Fructose-bisphosphate aldolase C.
FT /FTId=PRO_0000216947.
FT ACT_SITE 188 188 Proton acceptor (By similarity).
FT ACT_SITE 230 230 Schiff-base intermediate with
FT dihydroxyacetone-P.
FT BINDING 56 56 Substrate.
FT BINDING 147 147 Substrate.
FT SITE 364 364 Necessary for preference for fructose
FT 1,6-bisphosphate over fructose 1-
FT phosphate.
FT MOD_RES 111 111 N6-acetyllysine.
FT CONFLICT 311 311 L -> V (in Ref. 2; CAA30270).
FT HELIX 10 23
FT STRAND 29 33
FT HELIX 37 45
FT HELIX 53 64
FT HELIX 68 70
FT TURN 71 73
FT STRAND 74 79
FT HELIX 82 85
FT HELIX 94 100
FT STRAND 104 108
FT STRAND 113 115
FT STRAND 119 121
FT STRAND 123 125
FT HELIX 131 140
FT STRAND 145 152
FT HELIX 161 179
FT TURN 180 182
FT STRAND 184 191
FT HELIX 199 219
FT HELIX 224 226
FT HELIX 246 257
FT TURN 258 260
FT STRAND 267 271
FT HELIX 277 288
FT STRAND 295 303
FT HELIX 304 314
FT HELIX 321 338
FT TURN 339 341
SQ SEQUENCE 364 AA; 39456 MW; 506A570B3E507971 CRC64;
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR
QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC
PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF
SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA
NHAY
//
MIM
103870
*RECORD*
*FIELD* NO
103870
*FIELD* TI
*103870 ALDOLASE C, FRUCTOSE-BISPHOSPHATE; ALDOC
;;ALDOLASE 3;;
FRUCTOALDOLASE C; ALDC
read more*FIELD* TX
CLONING
Rottmann et al. (1987) determined the complete amino acid sequence of
aldolase C from recombinant genomic clones. The deduced polypeptide
contains 363 amino acids. Aldolase C shares 81% amino acid identity with
aldolase A (ALDOA; 103850) and 70% identity with aldolase B (ALDOB;
612724).
For additional background information, see 103850.
GENE STRUCTURE
Rottmann et al. (1987) determined that the gene structure of ALDOC is
the same as that in other aldolase genes in birds and mammals, having 9
exons separated by 8 introns, all in precisely the same positions, with
only the intron sizes being different. One of the exons is noncoding.
The entire gene is approximately 4 kb long. Buono et al. (1988)
presented the complete nucleotide sequence of ALDOC.
MAPPING
Tolan et al. (1987) reported the mapping of ALDOC to chromosome 17 by
spot-blot analysis of sorted chromosomes. Rocchi et al. (1989) also
mapped the gene and narrowed the assignment to 17cen-q21 by in situ
hybridization. In addition, they corroborated the assignment of ALDOA to
chromosome 16, and of ALDOB to chromosome 9.
*FIELD* RF
1. Buono, P.; Paolella, G.; Mancini, F. P.; Izzo, P.; Salvatore, F.
: The complete nucleotide sequence of the gene coding for the human
aldolase C. Nucleic Acids Res. 16: 4733 only, 1988.
2. Rocchi, M.; Vitale, E.; Covone, A.; Romeo, G.; Santamaria, R.;
Buono, P.; Paolella, G.; Salvatore, F.: Assignment of human aldolase
C gene to chromosome 17, region cen--q21.1. Hum. Genet. 82: 279-282,
1989.
3. Rottmann, W. H.; Deselms, K. R.; Niclas, J.; Camerato, T.; Holman,
P. S.; Green, C. J.; Tolan, D. R.: The complete amino acid sequence
of the human aldolase C isozyme derived from genomic clones. Biochimie 69:
137-145, 1987.
4. Tolan, D. R.; Niclas, J.; Bruce, B. D.; Lebo, R. V.: Evolutionary
implications of the human aldolase-A, -B, -C, and -pseudogene chromosome
locations. Am. J. Hum. Genet. 41: 907-924, 1987.
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 04/14/2009
dkim: 7/17/1998
mark: 8/8/1997
carol: 10/13/1993
carol: 3/31/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
root: 8/7/1989
*RECORD*
*FIELD* NO
103870
*FIELD* TI
*103870 ALDOLASE C, FRUCTOSE-BISPHOSPHATE; ALDOC
;;ALDOLASE 3;;
FRUCTOALDOLASE C; ALDC
read more*FIELD* TX
CLONING
Rottmann et al. (1987) determined the complete amino acid sequence of
aldolase C from recombinant genomic clones. The deduced polypeptide
contains 363 amino acids. Aldolase C shares 81% amino acid identity with
aldolase A (ALDOA; 103850) and 70% identity with aldolase B (ALDOB;
612724).
For additional background information, see 103850.
GENE STRUCTURE
Rottmann et al. (1987) determined that the gene structure of ALDOC is
the same as that in other aldolase genes in birds and mammals, having 9
exons separated by 8 introns, all in precisely the same positions, with
only the intron sizes being different. One of the exons is noncoding.
The entire gene is approximately 4 kb long. Buono et al. (1988)
presented the complete nucleotide sequence of ALDOC.
MAPPING
Tolan et al. (1987) reported the mapping of ALDOC to chromosome 17 by
spot-blot analysis of sorted chromosomes. Rocchi et al. (1989) also
mapped the gene and narrowed the assignment to 17cen-q21 by in situ
hybridization. In addition, they corroborated the assignment of ALDOA to
chromosome 16, and of ALDOB to chromosome 9.
*FIELD* RF
1. Buono, P.; Paolella, G.; Mancini, F. P.; Izzo, P.; Salvatore, F.
: The complete nucleotide sequence of the gene coding for the human
aldolase C. Nucleic Acids Res. 16: 4733 only, 1988.
2. Rocchi, M.; Vitale, E.; Covone, A.; Romeo, G.; Santamaria, R.;
Buono, P.; Paolella, G.; Salvatore, F.: Assignment of human aldolase
C gene to chromosome 17, region cen--q21.1. Hum. Genet. 82: 279-282,
1989.
3. Rottmann, W. H.; Deselms, K. R.; Niclas, J.; Camerato, T.; Holman,
P. S.; Green, C. J.; Tolan, D. R.: The complete amino acid sequence
of the human aldolase C isozyme derived from genomic clones. Biochimie 69:
137-145, 1987.
4. Tolan, D. R.; Niclas, J.; Bruce, B. D.; Lebo, R. V.: Evolutionary
implications of the human aldolase-A, -B, -C, and -pseudogene chromosome
locations. Am. J. Hum. Genet. 41: 907-924, 1987.
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 04/14/2009
dkim: 7/17/1998
mark: 8/8/1997
carol: 10/13/1993
carol: 3/31/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
root: 8/7/1989