ALDOC_MOUSE
ID ALDOC_MOUSE Reviewed; 363 AA.
AC P05063; Q64011; Q8CA91; Q99K96; Q9DBA4; Q9JK32;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Fructose-bisphosphate aldolase C;
DE EC=4.1.2.13;
DE AltName: Full=Aldolase 3;
DE AltName: Full=Brain-type aldolase;
DE AltName: Full=Scrapie-responsive protein 2;
DE AltName: Full=Zebrin II;
GN Name=Aldoc; Synonyms=Aldo3, Scrg2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=7925012; DOI=10.1242/dev.120.8.2081;
RA Ahn A.H., Dziennis S., Hawkes R., Herrup K.;
RT "The cloning of zebrin II reveals its identity with aldolase C.";
RL Development 120:2081-2090(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-227.
RX PubMed=3009179; DOI=10.1111/j.1432-1033.1986.tb09572.x;
RA Paolella G., Buono P., Mancini P., Izzo P., Salvatore F.;
RT "Structure and expression of mouse aldolase genes. Brain-specific aldolase
RT C amino acid sequence is closely related to aldolase A.";
RL Eur. J. Biochem. 156:229-235(1986).
RN [5]
RP PROTEIN SEQUENCE OF 2-13; 29-57; 61-69; 73-96; 102-108; 112-134; 154-215;
RP 244-258; 260-289; 305-315; 319-330 AND 332-363, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 281-363, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10719228; DOI=10.1016/s0169-328x(00)00028-0;
RA Dandoy-Dron F.C., Benboudjema L., Guillo F., Jaegly A., Jasmin C.,
RA Dormont D., Tovey M.G., Dron M.;
RT "Enhanced levels of scrapie responsive gene mRNA in BSE-infected mouse
RT brain.";
RL Brain Res. Mol. Brain Res. 76:173-179(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
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 (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in Purkinje cells in bands
CC running from anterior to posterior across most of the cerebellum.
CC Expressed at higher levels in the brains of BSE-infected animals.
CC {ECO:0000269|PubMed:10719228, ECO:0000269|PubMed:7925012}.
CC -!- DEVELOPMENTAL STAGE: Expression begins in the first week of postnatal
CC life. {ECO:0000269|PubMed:7925012}.
CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver
CC and aldolase C in brain.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; S72537; AAB32064.1; -; mRNA.
DR EMBL; AK005077; BAB23801.1; -; mRNA.
DR EMBL; AK039267; BAC30300.1; -; mRNA.
DR EMBL; BC004802; AAH04802.1; -; mRNA.
DR EMBL; BC008184; AAH08184.1; -; mRNA.
DR EMBL; X03796; CAA27422.1; -; mRNA.
DR EMBL; AJ132391; CAB77178.1; -; mRNA.
DR CCDS; CCDS25099.1; -.
DR PIR; A25388; ADMSC.
DR PIR; I53145; I53145.
DR RefSeq; NP_001290352.1; NM_001303423.1.
DR RefSeq; NP_033787.2; NM_009657.4.
DR AlphaFoldDB; P05063; -.
DR SMR; P05063; -.
DR BioGRID; 198068; 26.
DR IntAct; P05063; 3.
DR STRING; 10090.ENSMUSP00000099536; -.
DR iPTMnet; P05063; -.
DR PhosphoSitePlus; P05063; -.
DR SwissPalm; P05063; -.
DR REPRODUCTION-2DPAGE; IPI00119458; -.
DR UCD-2DPAGE; P05063; -.
DR EPD; P05063; -.
DR jPOST; P05063; -.
DR MaxQB; P05063; -.
DR PaxDb; P05063; -.
DR PeptideAtlas; P05063; -.
DR PRIDE; P05063; -.
DR ProteomicsDB; 296172; -.
DR Antibodypedia; 1111; 463 antibodies from 34 providers.
DR DNASU; 11676; -.
DR Ensembl; ENSMUST00000017534; ENSMUSP00000017534; ENSMUSG00000017390.
DR Ensembl; ENSMUST00000102478; ENSMUSP00000099536; ENSMUSG00000017390.
DR GeneID; 11676; -.
DR KEGG; mmu:11676; -.
DR UCSC; uc007kiw.2; mouse.
DR CTD; 230; -.
DR MGI; MGI:101863; Aldoc.
DR VEuPathDB; HostDB:ENSMUSG00000017390; -.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; P05063; -.
DR OMA; QKDNAGA; -.
DR OrthoDB; 799973at2759; -.
DR PhylomeDB; P05063; -.
DR TreeFam; TF314203; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-70171; Glycolysis.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR SABIO-RK; P05063; -.
DR UniPathway; UPA00109; UER00183.
DR BioGRID-ORCS; 11676; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Aldoc; mouse.
DR PRO; PR:P05063; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P05063; protein.
DR Bgee; ENSMUSG00000017390; Expressed in cerebellar vermis and 214 other tissues.
DR Genevisible; P05063; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; IDA:MGI.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Glycolysis; Lyase; Phosphoprotein;
KW Reference proteome; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09117"
FT CHAIN 2..363
FT /note="Fructose-bisphosphate aldolase C"
FT /id="PRO_0000216949"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT BINDING 56
FT /ligand="substrate"
FT BINDING 147
FT /ligand="substrate"
FT SITE 363
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT MOD_RES 5
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05065"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09972"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09972"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09972"
FT MOD_RES 111
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09972"
FT CONFLICT 25
FT /note="T -> A (in Ref. 3; AAH04802/AAH08184)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="Q -> E (in Ref. 2; BAC30300)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="V -> A (in Ref. 4; CAA27422)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="V -> L (in Ref. 4; CAA27422)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="R -> H (in Ref. 3; AAH04802/AAH08184)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="A -> V (in Ref. 1; AAB32064)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="I -> V (in Ref. 3; AAH04802/AAH08184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 39395 MW; 085C58AF163581C6 CRC64;
MPHSYPALSA EQKKELSDIA LRIVTPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR
QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGILVGIKVD KGVVPLAGTD
GETTTQGLDG LLERCAQYKK DGADFAKWRC VLKISDRTPS ALAILENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC
PIKYSPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC PLPRPWALTF
SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEMNGLAAQ GRYEGSGDGG AAAQSLYIAN
HAY
