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FBP2_DROME
ID   FBP2_DROME              Reviewed;         256 AA.
AC   P54398; O61511; O61512; O61513; O61514; O62595; Q9VLC2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Fat body protein 2;
DE   AltName: Full=Fat body protein P6;
GN   Name=Fbp2; ORFNames=CG3763;
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].
RX   PubMed=1920455; DOI=10.1007/bf02193634;
RA   Rat L., Veuille M., Lepesant J.-A.;
RT   "Drosophila fat body protein P6 and alcohol dehydrogenase are derived from
RT   a common ancestral protein.";
RL   J. Mol. Evol. 33:194-203(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=L12, L126, L15, L19, L21, L27, L28, L3, L36, and L5;
RX   PubMed=10331261; DOI=10.1093/oxfordjournals.molbev.a026115;
RA   Benassi V., Depaulis F., Meghlaoui G.K., Veuille M.;
RT   "Partial sweeping of variation at the Fbp2 locus in a west African
RT   population of Drosophila melanogaster.";
RL   Mol. Biol. Evol. 16:347-353(1999).
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.
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].
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; S57693; AAB19930.1; -; Genomic_DNA.
DR   EMBL; AF045787; AAC15687.1; -; Genomic_DNA.
DR   EMBL; AF045788; AAC15688.1; -; Genomic_DNA.
DR   EMBL; AF045789; AAC15689.1; -; Genomic_DNA.
DR   EMBL; AF045790; AAC15690.1; -; Genomic_DNA.
DR   EMBL; AF045791; AAC15691.1; -; Genomic_DNA.
DR   EMBL; AF045792; AAC15692.1; -; Genomic_DNA.
DR   EMBL; AF045793; AAC15693.1; -; Genomic_DNA.
DR   EMBL; AF045794; AAC15694.1; -; Genomic_DNA.
DR   EMBL; AF045795; AAC15695.1; -; Genomic_DNA.
DR   EMBL; AF045796; AAC15696.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAF52772.1; -; Genomic_DNA.
DR   EMBL; AY061549; AAL29097.1; -; mRNA.
DR   RefSeq; NP_001285777.1; NM_001298848.1.
DR   RefSeq; NP_001285778.1; NM_001298849.1.
DR   RefSeq; NP_523522.1; NM_078798.4.
DR   AlphaFoldDB; P54398; -.
DR   SMR; P54398; -.
DR   BioGRID; 60363; 7.
DR   IntAct; P54398; 5.
DR   STRING; 7227.FBpp0079408; -.
DR   PaxDb; P54398; -.
DR   DNASU; 34259; -.
DR   GeneID; 34259; -.
DR   KEGG; dme:Dmel_CG3763; -.
DR   CTD; 8789; -.
DR   FlyBase; FBgn0000640; Fbp2.
DR   VEuPathDB; VectorBase:FBgn0000640; -.
DR   eggNOG; KOG4169; Eukaryota.
DR   HOGENOM; CLU_010194_2_16_1; -.
DR   InParanoid; P54398; -.
DR   PhylomeDB; P54398; -.
DR   BioGRID-ORCS; 34259; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Fbp2; fly.
DR   GenomeRNAi; 34259; -.
DR   PRO; PR:P54398; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   ExpressionAtlas; P54398; baseline and differential.
DR   Genevisible; P54398; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0045735; F:nutrient reservoir activity; NAS:UniProtKB.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   InterPro; IPR002426; ADH_Ceratitis-type.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR01169; CERATITISADH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..256
FT                   /note="Fat body protein 2"
FT                   /id="PRO_0000054696"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         10..34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   VARIANT         44
FT                   /note="E -> K (in strain: Berkeley and L28)"
FT   VARIANT         72
FT                   /note="E -> D (in strain: L21 and L126)"
FT   VARIANT         149
FT                   /note="A -> S (in strain: Berkeley and L28)"
FT   VARIANT         171
FT                   /note="Y -> H (in strain: L12)"
FT   VARIANT         215
FT                   /note="R -> S (in strain: L126)"
FT   CONFLICT        191
FT                   /note="I -> M (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="S -> N (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   256 AA;  28999 MW;  190D2AE61C0E9647 CRC64;
     MFDWTGKNVV YVGSFSGIGW QMMMQLMQKD IKMMGIMHRM ENVEMMKKLQ AINPSVKVVF
     MQMNLMEKMS IEQAMKKMGQ MMGHIDVMIN GEGVLLDKDV ETTMGMNLTG MIQSTMMAMP
     YMDKTQMGMG GMVVNMSSVY GLEPAPAFAV YAAAMHGILG FTRSMGDKMI YQKTGVMFMA
     MCPGLTNSEM IMNLRDNVTW HHSESMVEAI ESAKRQMPEE AAMQMIHAME MMKNGSMWIV
     SMGQLKEVTP TMHWQM
 
 
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