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LIP1_DROME
ID   LIP1_DROME              Reviewed;         439 AA.
AC   O46107; Q9VKR6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Lipase 1;
DE            Short=DmLip1;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=Lip1; ORFNames=CG7279;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=Canton-S;
RX   PubMed=9566193; DOI=10.1006/jmbi.1997.1536;
RA   Pistillo D., Manzi A., Tino A., Pilo Boyl P., Graziani F., Malva C.;
RT   "The Drosophila melanogaster lipase homologs: a gene family with tissue and
RT   developmental specific expression.";
RL   J. Mol. Biol. 276:877-885(1998).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Could be a digestive enzyme. {ECO:0000269|PubMed:9566193}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: In 14 hours embryos expression is seen in the
CC       foregut/midgut boundary. {ECO:0000269|PubMed:9566193}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from 14 hours embryos through to
CC       adulthood. There is a weak maternal contribution to early embryos.
CC       {ECO:0000269|PubMed:9566193}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA74736.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y14366; CAA74736.1; ALT_INIT; mRNA.
DR   EMBL; AE014134; AAF52994.1; -; Genomic_DNA.
DR   EMBL; AY075506; AAL68315.1; -; mRNA.
DR   RefSeq; NP_001285811.1; NM_001298882.1.
DR   RefSeq; NP_523540.1; NM_078816.4.
DR   AlphaFoldDB; O46107; -.
DR   SMR; O46107; -.
DR   STRING; 7227.FBpp0079713; -.
DR   ESTHER; drome-lip1; Acidic_Lipase.
DR   MEROPS; S33.A88; -.
DR   GlyGen; O46107; 5 sites.
DR   PaxDb; O46107; -.
DR   PRIDE; O46107; -.
DR   DNASU; 43973; -.
DR   EnsemblMetazoa; FBtr0080124; FBpp0079713; FBgn0023496.
DR   EnsemblMetazoa; FBtr0340248; FBpp0309221; FBgn0023496.
DR   GeneID; 43973; -.
DR   KEGG; dme:Dmel_CG7279; -.
DR   CTD; 43973; -.
DR   FlyBase; FBgn0023496; Lip1.
DR   VEuPathDB; VectorBase:FBgn0023496; -.
DR   eggNOG; KOG2624; Eukaryota.
DR   HOGENOM; CLU_010974_0_3_1; -.
DR   InParanoid; O46107; -.
DR   OMA; LLCHPRD; -.
DR   OrthoDB; 651396at2759; -.
DR   PhylomeDB; O46107; -.
DR   Reactome; R-DME-192456; Digestion of dietary lipid.
DR   Reactome; R-DME-6809371; Formation of the cornified envelope.
DR   BioGRID-ORCS; 43973; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 43973; -.
DR   PRO; PR:O46107; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0023496; Expressed in primary trachea (Drosophila) and 16 other tissues.
DR   ExpressionAtlas; O46107; baseline and differential.
DR   Genevisible; O46107; DM.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0004806; F:triglyceride lipase activity; ISS:FlyBase.
DR   GO; GO:0007586; P:digestion; IEP:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR006693; AB_hydrolase_lipase.
DR   InterPro; IPR025483; Lipase_euk.
DR   Pfam; PF04083; Abhydro_lipase; 1.
DR   PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..439
FT                   /note="Lipase 1"
FT                   /id="PRO_0000017810"
FT   REGION          28..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..49
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        197
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        393
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        426
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        10
FT                   /note="L -> I (in Ref. 1; CAA74736)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        213
FT                   /note="Y -> F (in Ref. 1; CAA74736)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412
FT                   /note="Q -> E (in Ref. 1; CAA74736)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   439 AA;  50661 MW;  9E32E20BEAE93E3F CRC64;
     MRCSLRMQLL LLLGLCVFIS RIQGQLIGGE EDEEDEEEEE EEEESVEDET PEDRLQRKNI
     KQDSTLSVDK LIAKYGYESE VHHVTTEDGY ILTMHRIRKQ GAPPFLLQHG LVDSSAGFVV
     MGPNVSLAYL LADHNYDVWL GNARGNRYSR NHTTLDPDES KFWDFSWHEI GMYDLPAMID
     HVLKVTGFPK LHYAGHSQGC TSFFVMCSMR PAYNDKVVSM QALAPAVYAK ETEDHPYIRA
     ISLYFNSLVG SSIREMFNGE FRFLCRMTEE TERLCIEAVF GIVGRNWNEF NRKMFPVILG
     HYPAGVAAKQ VKHFIQIIKS GRFAPYSYSS NKNMQLYRDH LPPRYNLSLV TVPTFVYYST
     NDLLCHPKDV ESMCDDLGNV TGKYLVPQKE FNHMDFLWAI DVRKMLYRRM LQVLGKVPEG
     SPEEANRSRR EIRGKFIRS
 
 
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