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GDL22_ARATH
ID   GDL22_ARATH             Reviewed;         408 AA.
AC   Q3ECP6; Q8GXJ3; Q8LFA1; Q9ZVL5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=GDSL esterase/lipase At1g54790;
DE            EC=3.1.1.-;
DE   AltName: Full=Extracellular lipase At1g54790;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g54790; ORFNames=T22H22.20;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-406 (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [7]
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   [8]
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=Q3ECP6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3ECP6-2; Sequence=VSP_036693;
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM61525.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BX842537; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC005388; AAC64890.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33147.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33148.1; -; Genomic_DNA.
DR   EMBL; AK118209; BAC42831.1; -; mRNA.
DR   EMBL; BT005698; AAO64118.1; -; mRNA.
DR   EMBL; AY084964; AAM61525.1; ALT_INIT; mRNA.
DR   EMBL; BX842537; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A96590; A96590.
DR   RefSeq; NP_001185228.1; NM_001198299.1.
DR   RefSeq; NP_564668.1; NM_104354.4. [Q3ECP6-2]
DR   RefSeq; NP_974029.1; NM_202300.2. [Q3ECP6-1]
DR   AlphaFoldDB; Q3ECP6; -.
DR   STRING; 3702.AT1G54790.2; -.
DR   PaxDb; Q3ECP6; -.
DR   PRIDE; Q3ECP6; -.
DR   ProteomicsDB; 247087; -. [Q3ECP6-1]
DR   EnsemblPlants; AT1G54790.1; AT1G54790.1; AT1G54790. [Q3ECP6-2]
DR   EnsemblPlants; AT1G54790.2; AT1G54790.2; AT1G54790. [Q3ECP6-1]
DR   GeneID; 841920; -.
DR   Gramene; AT1G54790.1; AT1G54790.1; AT1G54790. [Q3ECP6-2]
DR   Gramene; AT1G54790.2; AT1G54790.2; AT1G54790. [Q3ECP6-1]
DR   KEGG; ath:AT1G54790; -.
DR   Araport; AT1G54790; -.
DR   TAIR; locus:2199496; AT1G54790.
DR   eggNOG; ENOG502QRTJ; Eukaryota.
DR   InParanoid; Q3ECP6; -.
DR   OrthoDB; 704138at2759; -.
DR   PhylomeDB; Q3ECP6; -.
DR   BioCyc; ARA:AT1G54790-MON; -.
DR   PRO; PR:Q3ECP6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q3ECP6; baseline and differential.
DR   Genevisible; Q3ECP6; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; 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; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR035669; SGNH_plant_lipase-like.
DR   Pfam; PF00657; Lipase_GDSL; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..408
FT                   /note="GDSL esterase/lipase At1g54790"
FT                   /id="PRO_0000367364"
FT   ACT_SITE        38
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        370
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        373
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         295..320
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11910074,
FT                   ECO:0000303|PubMed:14593172, ECO:0000303|Ref.5"
FT                   /id="VSP_036693"
FT   CONFLICT        2
FT                   /note="N -> K (in Ref. 5; AAM61525)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   408 AA;  45381 MW;  F24204F497576CE2 CRC64;
     MNITKMKLFY VILFFISSLQ ISNSIDFNYP SAFNFGDSNS DTGDLVAGLG IRLDLPNGQN
     SFKTSSQRFC DGRLVIDFLM DEMDLPFLNP YLDSLGLPNF KKGCNFAAAG STILPANPTS
     VSPFSFDLQI SQFIRFKSRA IELLSKTGRK YEKYLPPIDY YSKGLYMIDI GQNDIAGAFY
     SKTLDQVLAS IPSILETFEA GLKRLYEEGG RNIWIHNTGP LGCLAQNIAK FGTDSTKLDE
     FGCVSSHNQA AKLFNLQLHA MSNKFQAQYP DANVTYVDIF SIKSNLIANY SRFGKHFTKP
     LIDLNHLENV GYNKILNVLG FEKPLMACCG VGGAPLNYDS RITCGQTKVL DGISVTAKAC
     NDSSEYINWD GIHYTEAANE FVSSQILTGK YSDPPFSDQM PFFLTLKF
 
 
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