TPIS_DROME
ID TPIS_DROME Reviewed; 247 AA.
AC P29613; O76995; Q0KHY9; Q6NLI5; Q7JNU4; Q8IMJ1; Q9TY56;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=Tpi; ORFNames=CG2171;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND VARIANT
RP LYS-173.
RC STRAIN=Oregon-R;
RX PubMed=1720860; DOI=10.1007/bf00290672;
RA Shaw-Lee R.L., Lissemore J.L., Sullivan D.T.;
RT "Structure and expression of the triose phosphate isomerase (Tpi) gene of
RT Drosophila melanogaster.";
RL Mol. Gen. Genet. 230:225-229(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-173 AND PHE-230.
RC STRAIN=178.7, 709.6, A-26, DPF-13, DPF-2, DPF-30, DPF-46, DPF-53, DPF-62,
RC DPF-77, DPF-81, DPF-82.1, EM-10, Mali-10.2, Mali-4.2, Mali-4.4, Oregon-R,
RC R-60, VC-805, VC-815, Z-1, Z-35, Z-44, Z-48, and Z-5;
RX PubMed=9615457; DOI=10.1093/oxfordjournals.molbev.a025979;
RA Hasson E., Wang I.-N., Zeng L.-W., Kreitman M., Eanes W.F.;
RT "Nucleotide variation in the triosephosphate isomerase (Tpi) locus of
RT Drosophila melanogaster and D. simulans.";
RL Mol. Biol. Evol. 15:756-769(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Head, and Testis;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 158-170.
RC STRAIN=Vallecas; TISSUE=Wing imaginal disk;
RX PubMed=8500545; DOI=10.1006/excr.1993.1141;
RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J.,
RA Garcia-Bellido A.;
RT "Identification of Drosophila wing imaginal disc proteins by two-
RT dimensional gel analysis and microsequencing.";
RL Exp. Cell Res. 206:220-226(1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate;
CC Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC EC=5.3.1.1;
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1.
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=C;
CC IsoId=P29613-2; Sequence=Displayed;
CC Name=A;
CC IsoId=P29613-1; Sequence=VSP_015659;
CC -!- DEVELOPMENTAL STAGE: Present in substantial amounts in oocytes,
CC declines in abundance in early embryos, and begins to increase during
CC mid-embryogenesis. Levels peak in the third instar larva then decline
CC during pupal stages, rising again near the time of eclosion.
CC {ECO:0000269|PubMed:1720860}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; X57576; CAA40804.1; -; Genomic_DNA.
DR EMBL; U60836; AAC39041.1; -; Genomic_DNA.
DR EMBL; U60837; AAC39042.1; -; Genomic_DNA.
DR EMBL; U60838; AAC39043.1; -; Genomic_DNA.
DR EMBL; U60839; AAC39044.1; -; Genomic_DNA.
DR EMBL; U60840; AAC39045.1; -; Genomic_DNA.
DR EMBL; U60841; AAC39046.1; -; Genomic_DNA.
DR EMBL; U60842; AAC39047.1; -; Genomic_DNA.
DR EMBL; U60843; AAC39048.1; -; Genomic_DNA.
DR EMBL; U60844; AAC39049.1; -; Genomic_DNA.
DR EMBL; U60845; AAC39050.1; -; Genomic_DNA.
DR EMBL; U60846; AAC39051.1; -; Genomic_DNA.
DR EMBL; U60847; AAC39052.1; -; Genomic_DNA.
DR EMBL; U60848; AAC39053.1; -; Genomic_DNA.
DR EMBL; U60849; AAC39054.1; -; Genomic_DNA.
DR EMBL; U60850; AAC39055.1; -; Genomic_DNA.
DR EMBL; U60851; AAC39056.1; -; Genomic_DNA.
DR EMBL; U60852; AAC39057.1; -; Genomic_DNA.
DR EMBL; U60853; AAC39058.1; -; Genomic_DNA.
DR EMBL; U60854; AAC39059.1; -; Genomic_DNA.
DR EMBL; U60855; AAC39060.1; -; Genomic_DNA.
DR EMBL; U60856; AAC39061.1; -; Genomic_DNA.
DR EMBL; U60857; AAC39062.1; -; Genomic_DNA.
DR EMBL; U60858; AAC39063.1; -; Genomic_DNA.
DR EMBL; U60859; AAC39064.1; -; Genomic_DNA.
DR EMBL; U60860; AAC39065.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14218.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14219.1; -; Genomic_DNA.
DR EMBL; BT012347; AAS77472.1; -; mRNA.
DR EMBL; BT014664; AAT27288.1; -; mRNA.
DR PIR; S18604; S18604.
DR RefSeq; NP_788764.1; NM_176587.2. [P29613-1]
DR RefSeq; NP_788765.1; NM_176588.2. [P29613-2]
DR RefSeq; NP_788766.1; NM_176589.2. [P29613-2]
DR AlphaFoldDB; P29613; -.
DR SMR; P29613; -.
DR BioGRID; 68438; 22.
DR IntAct; P29613; 5.
DR STRING; 7227.FBpp0084948; -.
DR PaxDb; P29613; -.
DR PRIDE; P29613; -.
DR DNASU; 43582; -.
DR EnsemblMetazoa; FBtr0085582; FBpp0084948; FBgn0086355. [P29613-1]
DR EnsemblMetazoa; FBtr0085583; FBpp0084949; FBgn0086355. [P29613-2]
DR EnsemblMetazoa; FBtr0085584; FBpp0084950; FBgn0086355. [P29613-2]
DR GeneID; 43582; -.
DR KEGG; dme:Dmel_CG2171; -.
DR CTD; 43582; -.
DR FlyBase; FBgn0086355; Tpi.
DR VEuPathDB; VectorBase:FBgn0086355; -.
DR eggNOG; KOG1643; Eukaryota.
DR GeneTree; ENSGT00390000013354; -.
DR HOGENOM; CLU_024251_2_0_1; -.
DR InParanoid; P29613; -.
DR OMA; QEVCGAI; -.
DR PhylomeDB; P29613; -.
DR Reactome; R-DME-70171; Glycolysis.
DR Reactome; R-DME-70263; Gluconeogenesis.
DR SignaLink; P29613; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR BioGRID-ORCS; 43582; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43582; -.
DR PRO; PR:P29613; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0086355; Expressed in adult hindgut (Drosophila) and 28 other tissues.
DR ExpressionAtlas; P29613; baseline and differential.
DR Genevisible; P29613; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019682; P:glyceraldehyde-3-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IMP:FlyBase.
DR GO; GO:0050877; P:nervous system process; IMP:FlyBase.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:FlyBase.
DR CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00147_B; TIM_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 1.
DR TIGRFAMs; TIGR00419; tim; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Gluconeogenesis;
KW Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..247
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090130"
FT ACT_SITE 94
FT /note="Electrophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MPPGVLNDLNRNGIQCIASVTLLQRFPYHRNHHTIPTMDQNRPTVGG
FT VTAEVLKAVVSEALLGKFTAVFPKLFKCQWKTYEGQKKFYANFSTDCTDSNSNNM (in
FT isoform A)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_015659"
FT VARIANT 173
FT /note="Q -> K (in strain: 178.7, 709.6, A-26, DPF-13, DPF-
FT 2, DPF-30, DPF-46, DPF-53, DPF-62, DPF-77, DPF-81, DPF-
FT 82.1, EM-10, Mali-10.2, Mali-4.2, Mali-4.4, Oregon-R, R-60,
FT VC-805, VC-815, Z-1, Z-35, Z-44, Z-48 and Z-5)"
FT /evidence="ECO:0000269|PubMed:1720860,
FT ECO:0000269|PubMed:9615457"
FT VARIANT 230
FT /note="V -> F (in strain: 709.6)"
FT /evidence="ECO:0000269|PubMed:9615457"
FT CONFLICT 186
FT /note="F -> S (in Ref. 1; CAA40804)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="V -> L (in Ref. 1; CAA40804)"
FT /evidence="ECO:0000305"
FT CONFLICT P29613-1:12
FT /note="N -> I (in Ref. 5; AAS77472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 26626 MW; 68D7DCC8689C2D39 CRC64;
MSRKFCVGGN WKMNGDQKSI AEIAKTLSSA ALDPNTEVVI GCPAIYLMYA RNLLPCELGL
AGQNAYKVAK GAFTGEISPA MLKDIGADWV ILGHSERRAI FGESDALIAE KAEHALAEGL
KVIACIGETL EEREAGKTNE VVARQMCAYA QKIKDWKNVV VAYEPVWAIG TGQTATPDQA
QEVHAFLRQW LSDNISKEVS ASLRIQYGGS VTAANAKELA KKPDIDGFLV GGASLKPEFV
DIINARQ
