ID   Q3TKP4_MOUSE            Unreviewed;       339 AA.
AC   Q3TKP4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Fructose-1,6-bisphosphatase isozyme 2 {ECO:0000256|ARBA:ARBA00040321};
DE            EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 2 {ECO:0000256|ARBA:ARBA00042757};
DE   AltName: Full=Muscle FBPase {ECO:0000256|ARBA:ARBA00043165};
GN   Name=Fbp2 {ECO:0000313|MGI:MGI:95491};
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 {ECO:0000313|EMBL:BAE39101.1};
RN   [1] {ECO:0000313|EMBL:BAE39101.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39101.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27555.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE39101.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39101.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27555.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE39101.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39101.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27555.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE39101.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39101.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27555.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE39101.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39101.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27555.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:BAE39101.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39101.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27555.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:BAE39101.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39101.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27555.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAE39101.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE39101.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27555.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [9] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC       fructose 6-phosphate in the presence of divalent cations and probably
CC       participates in glycogen synthesis from carbohydrate precursors, such
CC       as lactate. {ECO:0000256|ARBA:ARBA00037516}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC         phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001273};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
CC   -!- SUBUNIT: Homotetramer. Interacts with ALDOA; the interaction blocks
CC       inhibition by physiological concentrations of AMP and reduces
CC       inhibition by Ca(2+). Interacts with alpha-actinin and F-actin.
CC       {ECO:0000256|ARBA:ARBA00038670}.
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC       Cytoplasm, myofibril, sarcomere, Z line
CC       {ECO:0000256|ARBA:ARBA00004216}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family.
CC       {ECO:0000256|ARBA:ARBA00010941, ECO:0000256|RuleBase:RU000508}.
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DR   EMBL; AK146946; BAE27555.1; -; mRNA.
DR   EMBL; AK166898; BAE39101.1; -; mRNA.
DR   EMBL; AK166973; BAE39156.1; -; mRNA.
DR   RefSeq; NP_032020.2; NM_007994.3.
DR   AlphaFoldDB; Q3TKP4; -.
DR   SMR; Q3TKP4; -.
DR   MaxQB; Q3TKP4; -.
DR   Antibodypedia; 2920; 274 antibodies from 27 providers.
DR   DNASU; 14120; -.
DR   GeneID; 14120; -.
DR   KEGG; mmu:14120; -.
DR   AGR; MGI:95491; -.
DR   CTD; 8789; -.
DR   MGI; MGI:95491; Fbp2.
DR   VEuPathDB; HostDB:ENSMUSG00000021456; -.
DR   HOGENOM; CLU_039977_1_0_1; -.
DR   OMA; NSRFWEP; -.
DR   OrthoDB; 292at2759; -.
DR   UniPathway; UPA00138; -.
DR   BioGRID-ORCS; 14120; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Fbp2; mouse.
DR   ExpressionAtlas; Q3TKP4; baseline and differential.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   CDD; cd00354; FBPase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   HAMAP; MF_01855; FBPase_class1; 1.
DR   InterPro; IPR044015; FBPase_C_dom.
DR   InterPro; IPR000146; FBPase_class-1.
DR   InterPro; IPR033391; FBPase_N.
DR   InterPro; IPR028343; FBPtase.
DR   InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR   PANTHER; PTHR11556:SF13; FRUCTOSE-1,6-BISPHOSPHATASE ISOZYME 2; 1.
DR   PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   Pfam; PF18913; FBPase_C; 1.
DR   PIRSF; PIRSF500210; FBPtase; 1.
DR   PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR   PRINTS; PR00115; F16BPHPHTASE.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00124; FBPASE; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000508};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000508};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          13..198
FT                   /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00316"
FT   DOMAIN          203..332
FT                   /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18913"
SQ   SEQUENCE   339 AA;  36947 MW;  442A3C5D09017415 CRC64;
     MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLANLYGI
     SGSVNVTGDE VKKLDVLSNS LVINMLQSSY STCVLVSEEN KEAVITAQER RGKYVVCFDP
     LDGSSNIDCL ASIGTIFAIY RKTTEDEPSE KDALQPGRNI VAAGYALYGS ATLVALSTGQ
     GVDLFMLDPA LGEFVLVEKD VRIKKKGKIF SLNEGYAKYF DAATAEYVQK KKFPEDGSEP
     YGARYVGSMV ADVHRTLVYG GIFMYPANQK SPNGKLRLLY ECNPVAYIIE QAGGMATTGT
     QPVLDVKPES IHQRVPLILG SPEDVQEYLS CVQRNQAGR
//