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EXL2_ARATH
ID   EXL2_ARATH              Reviewed;         379 AA.
AC   Q94CH7; A0MEG6; Q1PFC9; Q9LQS6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=GDSL esterase/lipase EXL2;
DE            EC=3.1.1.-;
DE   AltName: Full=Family II extracellular lipase 2;
DE            Short=Family II lipase EXL2;
DE   Flags: Precursor;
GN   Name=EXL2; OrderedLocusNames=At1g75890; ORFNames=T4O12.240;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=11431566; DOI=10.1126/science.1060972;
RA   Mayfield J.A., Fiebig A., Johnstone S.E., Preuss D.;
RT   "Gene families from the Arabidopsis thaliana pollen coat proteome.";
RL   Science 292:2482-2485(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [5]
RP   REVIEW.
RX   PubMed=15522763; DOI=10.1016/j.plipres.2004.09.002;
RA   Akoh C.C., Lee G.-C., Liaw Y.-C., Huang T.-H., Shaw J.-F.;
RT   "GDSL family of serine esterases/lipases.";
RL   Prog. Lipid Res. 43:534-552(2004).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=18819574; DOI=10.3923/pjbs.2008.763.767;
RA   Ling H.;
RT   "Sequence analysis of GDSL lipase gene family in Arabidopsis thaliana.";
RL   Pak. J. Biol. Sci. 11:763-767(2008).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q94CH7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q94CH7-2; Sequence=VSP_036682;
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF79814.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g75880 has been split into 2 genes: At1g75880 and At1g75890.; Evidence={ECO:0000305};
CC       Sequence=ABK28470.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AY028610; AAK30017.1; -; mRNA.
DR   EMBL; AC007396; AAF79814.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE35770.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35771.1; -; Genomic_DNA.
DR   EMBL; DQ446434; ABE65777.1; -; mRNA.
DR   EMBL; DQ652936; ABK28470.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001077829.1; NM_001084360.1. [Q94CH7-2]
DR   RefSeq; NP_565121.1; NM_106239.2. [Q94CH7-1]
DR   AlphaFoldDB; Q94CH7; -.
DR   SMR; Q94CH7; -.
DR   STRING; 3702.AT1G75890.1; -.
DR   PaxDb; Q94CH7; -.
DR   PRIDE; Q94CH7; -.
DR   ProteomicsDB; 221813; -. [Q94CH7-1]
DR   EnsemblPlants; AT1G75890.1; AT1G75890.1; AT1G75890. [Q94CH7-1]
DR   EnsemblPlants; AT1G75890.2; AT1G75890.2; AT1G75890. [Q94CH7-2]
DR   GeneID; 843922; -.
DR   Gramene; AT1G75890.1; AT1G75890.1; AT1G75890. [Q94CH7-1]
DR   Gramene; AT1G75890.2; AT1G75890.2; AT1G75890. [Q94CH7-2]
DR   KEGG; ath:AT1G75890; -.
DR   Araport; AT1G75890; -.
DR   TAIR; locus:2204395; AT1G75890.
DR   eggNOG; ENOG502QW19; Eukaryota.
DR   InParanoid; Q94CH7; -.
DR   PhylomeDB; Q94CH7; -.
DR   PRO; PR:Q94CH7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q94CH7; baseline and differential.
DR   Genevisible; Q94CH7; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01837; SGNH_plant_lipase_like; 1.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR008265; Lipase_GDSL_AS.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR035669; SGNH_plant_lipase-like.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   PROSITE; PS01098; LIPASE_GDSL_SER; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..379
FT                   /note="GDSL esterase/lipase EXL2"
FT                   /id="PRO_0000367329"
FT   ACT_SITE        54
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        361
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         144..156
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17147637"
FT                   /id="VSP_036682"
SQ   SEQUENCE   379 AA;  42127 MW;  144196C4DC5BF73F CRC64;
     MKRNSINIHH VTSFSSSPFW CVFFLVLLCK TSTNALVKQP PNETTPAIIV FGDSIVDAGN
     NDDIMTTLAR CNYPPYGIDF DGGIPTGRFC NGKVATDFIA GKFGIKPSIP AYRNPNLKPE
     DLLTGVTFAS GGAGYVPFTT QLSTYLFIYK PLLFLKGGIA LSQQLKLFEE YVEKMKKMVG
     EERTKLIIKN SLFMVICGSN DITNTYFGLP SVQQQYDVAS FTTLMADNAR SFAQKLHEYG
     ARRIQVFGAP PVGCVPSQRT LAGGPTRNCV VRFNDATKLY NVKLAANLGS LSRTLGDKTI
     IYVDIYDSLL DIILDPRQYG FKVVDKGCCG TGLIEVALLC NNFAADVCPN RDEYVFWDSF
     HPTEKTYRIM ATKYFERYV
 
 
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